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Conserved domains on  [gi|262089307|gb|ACY24528|]
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Zn-dependent alcohol dehydrogenase [uncultured crenarchaeote 57a5]

Protein Classification

MDR/zinc-dependent alcohol dehydrogenase-like family protein( domain architecture ID 94789)

medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein may catalyze the reversible NAD(P)(H)-dependent conversion of an alcohol to its corresponding aldehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MDR super family cl16912
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 3.64e-119

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


The actual alignment was detected with superfamily member cd08266:

Pssm-ID: 450120 [Multi-domain]  Cd Length: 342  Bit Score: 347.32  E-value: 3.64e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES--EANKHS 78
Cdd:cd08266    1 MKAVVIRGHGGPEVLEYG-DLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAvgPGVTNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 K-GTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08266   80 KpGQRVVIYPGISCGRCEYCLAGRENLCAQYGILG--EHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHm 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd08266  158 LVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELTGKRGVD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDSIY 316
Cdd:cd08266  238 VVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPVIDSVF 317

                        330       340
                 ....*....|....*....|....*
gi 262089307 317 TLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08266  318 PLEEAAEAHRRLESREQFGKIVLTP 342
 
Name Accession Description Interval E-value
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1-341 3.64e-119

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 347.32  E-value: 3.64e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES--EANKHS 78
Cdd:cd08266    1 MKAVVIRGHGGPEVLEYG-DLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAvgPGVTNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 K-GTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08266   80 KpGQRVVIYPGISCGRCEYCLAGRENLCAQYGILG--EHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHm 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd08266  158 LVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELTGKRGVD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDSIY 316
Cdd:cd08266  238 VVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPVIDSVF 317

                        330       340
                 ....*....|....*....|....*
gi 262089307 317 TLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08266  318 PLEEAAEAHRRLESREQFGKIVLTP 342
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-341 2.45e-92

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 278.18  E-value: 2.45e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVG---SLESEANKH 77
Cdd:COG0604    1 MKAIVITEFGGPEVLELE-EVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGvvvAVGEGVTGF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLVYPGiscnhcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW-N 156
Cdd:COG0604   80 KVGDRVAGLGR-----------------------------GGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWqA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:COG0604  131 LFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRGVD 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGS-----KLELL-ELMKFVSKKNILP 310
Cdd:COG0604  211 VVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFArdpaeRRAALaELARLLAAGKLRP 290

                        330       340       350
                 ....*....|....*....|....*....|.
gi 262089307 311 KVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:COG0604  291 VIDRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 1-341 5.30e-54

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 179.76  E-value: 5.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307    1 MKAVPIYKHGPIEVLKYEKDfPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICG---SDIVGSLESEANKH 77
Cdd:TIGR02824   1 MKAIEITEPGGPEVLVLVEV-PLPVPKAGEVLIRVAAAGVNRPDLLQRAGKYPPPPGASDILGlevAGEVVAVGEGVSRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   78 SKGTRVlvypgiscnhcnycrtgneticrdFSIIGGlsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW-N 156
Cdd:TIGR02824  80 KVGDRV------------------------CALVAG-----GGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWsN 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:TIGR02824 131 LFQRGGLKAGETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEALGADIAINYREEDFVEVVKAETGGKGVD 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGIL-----IGSKLELL-ELMKFV----SKK 306
Cdd:TIGR02824 211 VILDIVGGSYLNRNIKALALDGRIVQIGFQGGRKAELDLGPLLAKRLTITGSTlrarpVAEKAAIAaELREHVwpllASG 290

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 262089307  307 NILPKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:TIGR02824 291 RVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1-341 1.17e-45

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 158.28  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGpiEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKpISFPHICGSDIVGSLE---SEANKH 77
Cdd:PRK13771   1 MKAVILPGFK--QGYRIE-EVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPR-MKYPVILGHEVVGTVEevgENVKGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRV--LVYpgISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:PRK13771  77 KPGDRVasLLY--APDGTCEYCRSGEEAYCKNRLGYG--EELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLgSDNVINRKKKEVEVEVEKitggvGV 235
Cdd:PRK13771 153 RGLRRAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKY-ADYVIVGSKFSEEVKKIG-----GA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 DAVVDNAGQKTFTTSINCVRKGGKIALCgttsGNI---ANFQIRTFYS--KQIQLLGILIGSKLELLELMKFVSKKNILP 310
Cdd:PRK13771 227 DIVIETVGTPTLEESLRSLNMGGKIIQI----GNVdpsPTYSLRLGYIilKDIEIIGHISATKRDVEEALKLVAEGKIKP 302

                        330       340       350
                 ....*....|....*....|....*....|.
gi 262089307 311 KVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:PRK13771 303 VIGAEVSLSEIDKALEELKDKSRIGKILVKP 333
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 30-134 4.80e-30

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 110.39  E-value: 4.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   30 ESLIKIKYCGLNHLDIWTRTGiAGKPISFPHICGSDIVGSLE---SEANKHSKGTRVLVYPGISCNHCNYCRTGNETICR 106
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKG-GNPPVKLPLILGHEFAGEVVevgPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80

                          90       100
                  ....*....|....*....|....*...
gi 262089307  107 DFSIIGglSNYNGGYAEYVVVPKTNIVP 134
Cdd:pfam08240  81 NGRFLG--YDRDGGFAEYVVVPERNLVP 106
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 33-339 4.57e-26

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 105.16  E-value: 4.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307    33 IKIKYCGLNHLDIWTRTGIAGKPISFPHICgSDIVGSLESEANKHSKGTRVLvypgiscnhcnycrtgneticrdfsiig 112
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVLGGEC-AGVVTRVGPGVTGLAVGDRVM---------------------------- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   113 GLSNynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKL-QLKKHDTLLVYGATGGLGMAVIQFAKALEI 191
Cdd:smart00829  52 GLAP--GAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLaRLRPGESVLIHAAAGGVGQAAIQLARHLGA 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   192 KIITSVSDDSKLNFARSLG--SDNVINRKKKEVEVEVEKITGGVGVDaVVDN--AGQKTfTTSINCVRKGGKIALCGTT- 266
Cdd:smart00829 130 EVFATAGSPEKRDFLRALGipDDHIFSSRDLSFADEILRATGGRGVD-VVLNslSGEFL-DASLRCLAPGGRFVEIGKRd 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   267 ---SGNIANFQIR---TFYSkqIQLLGILIGSKL--ELL-ELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKI 337
Cdd:smart00829 208 irdNSQLAMAPFRpnvSYHA--VDLDALEEGPDRirELLaEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKV 285


                   ..
gi 262089307   338 LI 339
Cdd:smart00829 286 VL 287
 
Name Accession Description Interval E-value
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1-341 3.64e-119

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 347.32  E-value: 3.64e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES--EANKHS 78
Cdd:cd08266    1 MKAVVIRGHGGPEVLEYG-DLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMPGIKLPLPHILGSDGAGVVEAvgPGVTNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 K-GTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08266   80 KpGQRVVIYPGISCGRCEYCLAGRENLCAQYGILG--EHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHm 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd08266  158 LVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELTGKRGVD 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDSIY 316
Cdd:cd08266  238 VVVEHVGAATWEKSLKSLARGGRLVTCGATTGYEAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPVIDSVF 317

                        330       340
                 ....*....|....*....|....*
gi 262089307 317 TLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08266  318 PLEEAAEAHRRLESREQFGKIVLTP 342
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-341 2.45e-92

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 278.18  E-value: 2.45e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVG---SLESEANKH 77
Cdd:COG0604    1 MKAIVITEFGGPEVLELE-EVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGvvvAVGEGVTGF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLVYPGiscnhcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW-N 156
Cdd:COG0604   80 KVGDRVAGLGR-----------------------------GGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWqA 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:COG0604  131 LFDRGRLKPGETVLVHGAAGGVGSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGGRGVD 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGS-----KLELL-ELMKFVSKKNILP 310
Cdd:COG0604  211 VVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFArdpaeRRAALaELARLLAAGKLRP 290

                        330       340       350
                 ....*....|....*....|....*....|.
gi 262089307 311 KVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:COG0604  291 VIDRVFPLEEAAEAHRLLESGKHRGKVVLTV 321
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 1-340 1.05e-84

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 258.89  E-value: 1.05e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGkPISFPHICGSDIVG---SLESEANK 76
Cdd:COG1064    1 MKAAVLTEPGgPLEL----EEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWP-VPKLPLVPGHEIVGrvvAVGPGVTG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  77 HSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGlsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN 156
Cdd:COG1064   76 FKVGDRVGVGWVDSCGTCEYCRSGRENLCENGRFTGY--TTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINrkkKEVEVEVEKITGGVGVD 236
Cdd:COG1064  154 ALRRAGVGPGDRVAVIGA-GGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVN---SSDEDPVEAVRELTGAD 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDsI 315
Cdd:COG1064  230 VVIDTVGaPATVNAALALLRRGGRLVLVGLPGGPI-PLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVE-T 307

                        330       340
                 ....*....|....*....|....*
gi 262089307 316 YTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:COG1064  308 IPLEEANEALERLRAGKVRGRAVLD 332
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 30-303 1.91e-75

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 233.37  E-value: 1.91e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  30 ESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLE---SEANKHSKGTRVLVYPGISCNHCNYCRTGnetiCR 106
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVevgPGVTGVKVGDRVVVLPNLGCGTCELCREL----CP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 107 DFSIIGGlsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN-IFKKLQLKKHDTLLVYGAtGGLGMAVIQF 185
Cdd:cd05188   77 GGGILGE--GLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHaLRRAGVLKPGDTVLVLGA-GGVGLLAAQL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 186 AKALEIKIITSVSDDSKLNFARSLGSDNVINRkKKEVEVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCG 264
Cdd:cd05188  154 AKAAGARVIVTDRSDEKLELAKELGADHVIDY-KEEDLEEELRLTGGGGADVVIDAVGgPETLAQALRLLRPGGRIVVVG 232

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 262089307 265 TTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFV 303
Cdd:cd05188  233 GTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 1.55e-73

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 231.03  E-value: 1.55e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTG-------------------IAGKPISFPHI 61
Cdd:cd08274    1 MRAVLLTGHGGLDKLVYRDDVPVPTPAPGEVLIRVGACGVNNTDINTREGwystevdgatdstgageagWWGGTLSFPRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  62 CGSDIVG---SLESEANKHSKGTRVLVYPGIscnhcnycRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNE 138
Cdd:cd08274   81 QGADIVGrvvAVGEGVDTARIGERVLVDPSI--------RDPPEDDPADIDYIG--SERDGGFAEYTVVPAENAYPVNSP 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 139 ISDEHAATLSISYLTAWNIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDsKLNFARSLGSDNVINRk 218
Cdd:cd08274  151 LSDVELATFPCSYSTAENMLERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVAGAA-KEEAVRALGADTVILR- 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 219 kKEVEVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLE 298
Cdd:cd08274  229 -DAPLLADAKALGGEPVDVVADVVGGPLFPDLLRLLRPGGRYVTAGAIAGPVVELDLRTLYLKDLTLFGSTLGTREVFRR 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 262089307 299 LMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08274  308 LVRYIEEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVLVP 350
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 2-341 1.46e-66

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 212.30  E-value: 1.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   2 KAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAgkPISFPHICGSDIVGSLE---SEANKHS 78
Cdd:cd05286    1 KAVRIHKTGGPEVLEYE-DVPVPEPGPGEVLVRNTAIGVNFIDTYFRSGLY--PLPLPFVLGVEGAGVVEavgPGVTGFK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 KGTRVlVYPGIscnhcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIF 158
Cdd:cd05286   78 VGDRV-AYAGP----------------------------PGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 159 KKL-QLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVDA 237
Cdd:cd05286  129 RETyPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAELARAAGADHVINYRDEDFVERVREITGGRGVDV 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 238 VVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQL----LGILIGSKLELL----ELMKFVSKKNIL 309
Cdd:cd05286  209 VYDGVGKDTFEGSLDSLRPRGTLVSFGNASGPVPPFDLLRLSKGSLFLtrpsLFHYIATREELLaraaELFDAVASGKLK 288

                        330       340       350
                 ....*....|....*....|....*....|..
gi 262089307 310 PKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd05286  289 VEIGKRYPLADAAQAHRDLESRKTTGKLLLIP 320
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1-338 4.95e-66

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 211.06  E-value: 4.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGpIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPIsfPHICGSDIVGSLEsEANKH--- 77
Cdd:cd08264    1 MKALVFEKSG-IENLKVE-DVKDPKPGPGEVLIRVKMAGVNPVDYNVINAVKVKPM--PHIPGAEFAGVVE-EVGDHvkg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 -SKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSNynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN 156
Cdd:cd08264   76 vKKGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGIIGVVSN--GGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIItSVSDDSKLnfaRSLGSDNVINRkkKEVEVEVEKITGgvGVD 236
Cdd:cd08264  154 ALKTAGLGPGETVVVFGASGNTGIFAVQLAKMMGAEVI-AVSRKDWL---KEFGADEVVDY--DEVEEKVKEITK--MAD 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVskKNILPKVDSIY 316
Cdd:cd08264  226 VVINSLGSSFWDLSLSVLGRGGRLVTFGTLTGGEVKLDLSDLYSKQISIIGSTGGTRKELLELVKIA--KDLKVKVWKTF 303

                        330       340
                 ....*....|....*....|..
gi 262089307 317 TLAEIHKAHTLLERGQQLGKIL 338
Cdd:cd08264  304 KLEEAKEALKELFSKERDGRIL 325
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-341 1.48e-64

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 207.68  E-value: 1.48e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKpISFPHICGSDIVG---SLESEANKH 77
Cdd:COG1063    1 MKALVLHGPGDLRL----EEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPF-VRPPLVLGHEFVGevvEVGEGVTGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGgLSNYNGGYAEYVVVPKTNIVPIPNEISDEHAA---TLSisylTA 154
Cdd:COG1063   76 KVGDRVVVEPNIPCGECRYCRRGRYNLCENLQFLG-IAGRDGGFAEYVRVPAANLVKVPDGLSDEAAAlvePLA----VA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKAL---EIkIITSVSDDsKLNFARSLGSDNVINRKKKEVEVEVEKITG 231
Cdd:COG1063  151 LHAVERAGVKPGDTVLVIGA-GPIGLLAALAARLAgaaRV-IVVDRNPE-RLELARELGADAVVNPREEDLVEAVRELTG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 232 GVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILP 310
Cdd:COG1063  228 GRGADVVIEAVGaPAALEQALDLVRPGGTVVLVGVPGGPV-PIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDL 306

                        330       340       350
                 ....*....|....*....|....*....|....
gi 262089307 311 K--VDSIYTLAEIHKA-HTLLERGQQLGKILIKI 341
Cdd:COG1063  307 EplITHRFPLDDAPEAfEAAADRADGAIKVVLDP 340
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1-339 2.75e-63

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 203.56  E-value: 2.75e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTG--IAGKPISFPHICGSDIVGSLE---SEAN 75
Cdd:cd05289    1 MKAVRIHEYGGPEVLELA-DVPTPEPGPGEVLVKVHAAGVNPVDLKIREGllKAAFPLTLPLIPGHDVAGVVVavgPGVT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVlvypgiscnhcnYCRTGneticrdfsiigglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd05289   80 GFKVGDEV------------FGMTP--------------FTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAW 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 N-IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSdDSKLNFARSLGSDNVINRKKKEVEVEvekiTGGVG 234
Cdd:cd05289  134 QaLFELGGLKAGQTVLIHGAAGGVGSFAVQLAKARGARVIATAS-AANADFLRSLGADEVIDYTKGDFERA----AAPGG 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 235 VDAVVDNAGQKTFTTSINCVRKGGKIAlcgttsgNIANFQIRTFYSK--QIQLLGILIGSKLELL-ELMKFVSKKNILPK 311
Cdd:cd05289  209 VDAVLDTVGGETLARSLALVKPGGRLV-------SIAGPPPAEQAAKrrGVRAGFVFVEPDGEQLaELAELVEAGKLRPV 281

                        330       340
                 ....*....|....*....|....*...
gi 262089307 312 VDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd05289  282 VDRVFPLEDAAEAHERLESGHARGKVVL 309
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1-339 2.78e-63

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 203.83  E-value: 2.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICG---SDIVGSLESEANKH 77
Cdd:cd05276    1 MKAIVIKEPGGPEVLELG-EVPKPAPGPGEVLIRVAAAGVNRADLLQRQGLYPPPPGASDILGlevAGVVVAVGPGVTGW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVlvypgiscnhcnycrtgneticrdFSIIGGlsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW-N 156
Cdd:cd05276   80 KVGDRV------------------------CALLAG-----GGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWqN 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd05276  131 LFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDFAEEVKEATGGRGVD 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQllgiLIGSKL-------------ELLE--LMK 301
Cdd:cd05276  211 VILDMVGGDYLARNLRALAPDGRLVLIGLLGGAKAELDLAPLLRKRLT----LTGSTLrsrsleekaalaaAFREhvWPL 286

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262089307 302 FVSKKnILPKVDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd05276  287 FASGR-IRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 8.50e-63

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 203.15  E-value: 8.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSD---IVGSLESEANKH 77
Cdd:cd08276    1 MKAWRLSGGGGLDNLKLV-EEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPPPVKDPLIPLSDgagEVVAVGEGVTRF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLvyPGISCNHcnycRTGNETICRDFSIIGGlsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08276   80 KVGDRVV--PTFFPNW----LDGPPTAEDEASALGG--PIDGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNa 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGaTGGLGMAVIQFAKALEIK-IITSvSDDSKLNFARSLGSDNVIN-RKKKEVEVEVEKITGGVG 234
Cdd:cd08276  152 LFGLGPLKPGDTVLVQG-TGGVSLFALQFAKAAGARvIATS-SSDEKLERAKALGADHVINyRTTPDWGEEVLKLTGGRG 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 235 VDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDS 314
Cdd:cd08276  230 VDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAHRIRPVIDR 309

                        330       340
                 ....*....|....*....|....*..
gi 262089307 315 IYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08276  310 VFPFEEAKEAYRYLESGSHFGKVVIRV 336
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-340 8.86e-63

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 202.93  E-value: 8.86e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGpiEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGI--AGKPisfPHICGSDIVGSLESEANKHS 78
Cdd:cd08259    1 MKAAILHKPN--KPLQIE-EVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFfpRGKY---PLILGHEIVGTVEEVGEGVE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 ---KGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSNynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd08259   75 rfkPGDRVILYYYIPCGKCEYCLSGEENLCRNRAEYGEEVD--GGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEkitggVGV 235
Cdd:cd08259  153 HALKRAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARVIAVTRSPEKLKILKELGADYVIDGSKFSEDVKKL-----GGA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 DAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDSI 315
Cdd:cd08259  228 DVVIELVGSPTIEESLRSLNKGGRLVLIGNVTPDPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKPVIDRV 307

                        330       340
                 ....*....|....*....|....*
gi 262089307 316 YTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08259  308 VSLEDINEALEDLKSGKVVGRIVLK 332
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1-339 6.40e-61

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 197.83  E-value: 6.40e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGkPISFPHICGSDIVGSLES-EANKHSK 79
Cdd:cd08243    1 MKAIVIEQPGGPEVLKLR-EIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSP-SVKFPRVLGIEAVGEVEEaPGGTFTP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  80 GTRVlvypgiscnhcnycrtgneticrdFSIIGGLS-NYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN-I 157
Cdd:cd08243   79 GQRV------------------------ATAMGGMGrTFDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGsL 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 158 FKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVInrkKKEVEVEVEKITGGVGVDA 237
Cdd:cd08243  135 FRSLGLQPGDTLLIRGGTSSVGLAALKLAKALGATVTATTRSPERAALLKELGADEVV---IDDGAIAEQLRAAPGGFDK 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 238 VVDNAGQKTFTTSINCVRKGGKIALCGTTSGN-----------IANFQIRTFYSKqiQLLGIligSKLELLELMKFVSKK 306
Cdd:cd08243  212 VLELVGTATLKDSLRHLRPGGIVCMTGLLGGQwtledfnpmddIPSGVNLTLTGS--SSGDV---PQTPLQELFDFVAAG 286

                        330       340       350
                 ....*....|....*....|....*....|...
gi 262089307 307 NILPKVDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd08243  287 HLDIPPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1-341 1.76e-59

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 193.95  E-value: 1.76e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES---EANKH 77
Cdd:cd08253    1 MRAIRYHEFGAPDVLRLG-DLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEAvgeGVDGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVlvypgiscnhcnycrtgneticrdFSIIGGLSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08253   80 KVGDRV------------------------WLTNLGWGRRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRa 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd08253  136 LFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNYRAEDLADRILAATAGQGVD 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTsGNIANFQIRTFYSKQIQLLGILIG--SKLELLE----LMKFVSKKNILP 310
Cdd:cd08253  216 VIIEVLANVNLAKDLDVLAPGGRIVVYGSG-GLRGTIPINPLMAKEASIRGVLLYtaTPEERAAaaeaIAAGLADGALRP 294

                        330       340       350
                 ....*....|....*....|....*....|.
gi 262089307 311 KVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08253  295 VIAREYPLEEAAAAHEAVESGGAIGKVVLDP 325
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-341 3.34e-59

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 193.90  E-value: 3.34e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG--PIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICG---SDIVGSLESEAN 75
Cdd:cd08297    1 MKAAVVEEFGekPYEV----KDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPKLPLIGGhegAGVVVAVGPGVS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVlvypGI-----SCNHCNYCRTGNETICrDFSIIGGLSNyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSIS 150
Cdd:cd08297   77 GLKVGDRV----GVkwlydACGKCEYCRTGDETLC-PNQKNSGYTV-DGTFAEYAIADARYVTPIPDGLSFEQAAPLLCA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 151 YLTAWNIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKIT 230
Cdd:cd08297  151 GVTVYKALKKAGLKPGDWVVISGAGGGLGHLGVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVDFKKSDDVEAVKELT 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 231 GGVGVDAVVDNAGQKT-FTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNIL 309
Cdd:cd08297  231 GGGGAHAVVVTAVSAAaYEQALDYLRPGGTLVCVGLPPGGFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVK 310

                        330       340       350
                 ....*....|....*....|....*....|..
gi 262089307 310 PKVdSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08297  311 PHI-QVVPLEDLNEVFEKMEEGKIAGRVVVDF 341
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 1-335 4.54e-58

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 190.85  E-value: 4.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGpiEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGK--PISFPHICGSDIVGSLE---SEAN 75
Cdd:cd05284    1 MKAARLYEYG--KPLRLE-DVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGilPYKLPFTLGHENAGWVEevgSGVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd05284   78 GLKEGDPVVVHPPWGCGTCRYCRRGEENYCENARFPG--IGTDGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAY 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKH--DTLLVYGAtGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVINrKKKEVEVEVEKITGG 232
Cdd:cd05284  156 HAVKKALPYLDpgSTVVVIGV-GGLGHIAVQILRALTPATVIAVDrSEEALKLAERLGADHVLN-ASDDVVEEVRELTGG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 233 VGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTtsgnIANFQIRTFY--SKQIQLLGILIGSKLELLELMKFVSKKNIL 309
Cdd:cd05284  234 RGADAVIDFVGsDETLALAAKLLAKGGRYVIVGY----GGHGRLPTSDlvPTEISVIGSLWGTRAELVEVVALAESGKVK 309

                        330       340
                 ....*....|....*....|....*.
gi 262089307 310 PKVdSIYTLAEIHKAHTLLERGQQLG 335
Cdd:cd05284  310 VEI-TKFPLEDANEALDRLREGRVTG 334
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 1-331 1.49e-56

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 187.07  E-value: 1.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVpiYKHGPIEVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTG----IAGKPISFPH-ICGsdIVGSLESEAN 75
Cdd:cd08254    1 MKAW--RFHKGSKGLLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGgvptLTKLPLTLGHeIAG--TVVEVGAGVT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd08254   77 NFKVGDRVAVPAVIPCGACALCRRGRGNLCLNQGMPG--LGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPY 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 N-IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINrKKKEVEVEVEKITGGVG 234
Cdd:cd08254  155 HaVVRAGEVKPGETVLVIGL-GGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLN-SLDDSPKDKKAAGLGGG 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 235 VDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVD 313
Cdd:cd08254  233 FDVIFDFVGtQPTFEDAQKAVKPGGRIVVVGLGRDKL-TVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVE 311

                        330
                 ....*....|....*...
gi 262089307 314 SIyTLAEIHKAHTLLERG 331
Cdd:cd08254  312 TR-PLDEIPEVLERLHKG 328
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-340 5.26e-56

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 185.01  E-value: 5.26e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEKDFPKPVPnSSESLIKIKYCGLNHLDIWTrtgIAG----KPiSFPHICGSDIVGSLESEANK 76
Cdd:cd08241    1 MKAVVCKELGGPEDLVLEEVPPEPGA-PGEVRIRVEAAGVNFPDLLM---IQGkyqvKP-PLPFVPGSEVAGVVEAVGEG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  77 HSK---GTRVLVYPGIscnhcnycrtgneticrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLT 153
Cdd:cd08241   76 VTGfkvGDRVVALTGQ-----------------------------GGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 154 AWNIFKKL-QLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGG 232
Cdd:cd08241  127 AYHALVRRaRLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTGG 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 233 VGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLE---------LLELMKFV 303
Cdd:cd08241  207 RGVDVVYDPVGGDVFEASLRSLAWGGRLLVIGFASGEIPQIPANLLLLKNISVVGVYWGAYARrepellranLAELFDLL 286

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 262089307 304 SKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08241  287 AEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 1-340 1.31e-55

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 184.74  E-value: 1.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEvlkyEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIA----GKPIS-------FPHICGSDIVG 68
Cdd:cd08240    1 MKAAAVVEPGkPLE----EVEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGYdlggGKTMSlddrgvkLPLVLGHEIVG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  69 ---SLESEANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSNynGGYAEYVVVPKTNIVPIPNEISDEHAA 145
Cdd:cd08240   77 evvAVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGIFQD--GGYAEYVIVPHSRYLVDPGGLDPALAA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 146 TLSISYLTAWNIFKKLQLKKHDT-LLVYGAtGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVINRKKKEVE 223
Cdd:cd08240  155 TLACSGLTAYSAVKKLMPLVADEpVVIIGA-GGLGLMALALLKALGPANIIVVDiDEAKLEAAKAAGADVVVNGSDPDAA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 224 VEVEKITGGvGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNiANFQIRTFYSKQIQLLGILIGSKLELLELMKF 302
Cdd:cd08240  234 KRIIKAAGG-GVDAVIDFVNnSATASLAFDILAKGGKLVLVGLFGGE-ATLPLPLLPLRALTIQGSYVGSLEELRELVAL 311

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262089307 303 VSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08240  312 AKAGKLKPIPLTERPLSDVNDALDDLKAGKVVGRAVLK 349
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1-287 3.25e-55

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 183.58  E-value: 3.25e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDI--WTRTGiagkPISFPHICG---SDIVGSLESEAN 75
Cdd:cd08236    1 MKALVLTGPGDLRY----EDIPKPEPGPGEVLVKVKACGICGSDIprYLGTG----AYHPPLVLGhefSGTVEEVGSGVD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLS-ISylTA 154
Cdd:cd08236   73 DLAVGDRVAVNPLLPCGKCEYCKKGEYSLCSNYDYIG--SRRDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEpAA--VA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVINrKKKEVEVEVEKITGGV 233
Cdd:cd08236  149 LHAVRLAGITLGDTVVVIGA-GTIGLLAIQWLKILGAKRVIAVDiDDEKLAVARELGADDTIN-PKEEDVEKVRELTEGR 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 262089307 234 GVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSG--NIANFQIRTFYSKQIQLLG 287
Cdd:cd08236  227 GADLVIEAAGsPATIEQALALARPGGKVVLVGIPYGdvTLSEEAFEKILRKELTIQG 283
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
 1-341 5.30e-54

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 179.76  E-value: 5.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307    1 MKAVPIYKHGPIEVLKYEKDfPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICG---SDIVGSLESEANKH 77
Cdd:TIGR02824   1 MKAIEITEPGGPEVLVLVEV-PLPVPKAGEVLIRVAAAGVNRPDLLQRAGKYPPPPGASDILGlevAGEVVAVGEGVSRW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   78 SKGTRVlvypgiscnhcnycrtgneticrdFSIIGGlsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW-N 156
Cdd:TIGR02824  80 KVGDRV------------------------CALVAG-----GGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWsN 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:TIGR02824 131 LFQRGGLKAGETVLIHGGASGIGTTAIQLAKAFGARVFTTAGSDEKCAACEALGADIAINYREEDFVEVVKAETGGKGVD 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGIL-----IGSKLELL-ELMKFV----SKK 306
Cdd:TIGR02824 211 VILDIVGGSYLNRNIKALALDGRIVQIGFQGGRKAELDLGPLLAKRLTITGSTlrarpVAEKAAIAaELREHVwpllASG 290

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 262089307  307 NILPKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:TIGR02824 291 RVRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 2-339 3.30e-53

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 177.90  E-value: 3.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   2 KAVPIYK-HGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGiAGKPISFPHICGSDIVGSLE---SEANKH 77
Cdd:cd08245    1 KAAVVHAaGGPLEP----EEVPVPEPGPGEVLIKIEACGVCHTDLHAAEG-DWGGSKYPLVPGHEIVGEVVevgAGVEGR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLV-YPGISCNHCNYCRTGNETICRDFSIIGGlsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN 156
Cdd:cd08245   76 KVGDRVGVgWLVGSCGRCEYCRRGLENLCQKAVNTGY--TTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYS 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEkitGGVGVD 236
Cdd:cd08245  154 ALRDAGPRPGERVAVLGI-GGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQAAA---GGADVI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGqKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDsIY 316
Cdd:cd08245  230 LVTVVSG-AAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIE-TF 307

                        330       340
                 ....*....|....*....|...
gi 262089307 317 TLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd08245  308 PLDQANEAYERMEKGDVRFRFVL 330
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-287 3.03e-49

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 167.75  E-value: 3.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGiaGKP-ISFPHICGSDIVGSLES--EANKH 77
Cdd:cd08261    1 MKALVCEKPGRLEV----VDIPEPVPGAGEVLVRVKRVGICGSDLHIYHG--RNPfASYPRILGHELSGEVVEvgEGVAG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SK-GTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNiVPIPNEISDEHAA---TLSISYlt 153
Cdd:cd08261   75 LKvGDRVVVDPYISCGECYACRKGRPNCCENLQVLG--VHRDGGFAEYIVVPADA-LLVPEGLSLDQAAlvePLAIGA-- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 154 awNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGV 233
Cdd:cd08261  150 --HAVRRAGVTAGDTVLVVGA-GPIGLGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGE 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262089307 234 GVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIAnFQIRTFYSKQIQLLG 287
Cdd:cd08261  227 GADVVIDATGnPASMEEAVELVAHGGRVVLVGLSKGPVT-FPDPEFHKKELTILG 280
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 4.63e-49

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 167.01  E-value: 4.63e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES--EANKHS 78
Cdd:cd08268    1 MRAVRFHQFGGPEVLRIE-ELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIEPPPLPARLGYEAAGVVEAvgAGVTGF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 K-GTRVLVYPGISCNHcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08268   80 AvGDRVSVIPAADLGQ------------------------YGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGa 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd08268  136 LVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRITGGKGVD 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKL---ELLE-LMKFVS---KKNIL 309
Cdd:cd08268  216 VVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPTPFPLKAALKKSLTFRGYSLDEITldpEARRrAIAFILdglASGAL 295

                        330       340       350
                 ....*....|....*....|....*....|...
gi 262089307 310 -PKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08268  296 kPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-339 6.28e-49

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 167.93  E-value: 6.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKyekDFPKPVPNSSESLIKIKYCGLNHLDIWTRTG-IAGKPisfPHICGSDIVGSLE------SE 73
Cdd:cd08263    1 MKAAVLKGPNPPLTIE---EIPVPRPKEGEILIRVAACGVCHSDLHVLKGeLPFPP---PFVLGHEISGEVVevgpnvEN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  74 ANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSII-------------------GGLSNY-NGGYAEYVVVPKTNIV 133
Cdd:cd08263   75 PYGLSVGDRVVGSFIMPCGKCRYCARGKENLCEDFFAYnrlkgtlydgttrlfrldgGPVYMYsMGGLAEYAVVPATALA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 134 PIPNEISDEHAATLSISYLTAWNIFKKLQLKKH-DTLLVYGaTGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGS 211
Cdd:cd08263  155 PLPESLDYTESAVLGCAGFTAYGALKHAADVRPgETVAVIG-VGGVGSSAIQLAKAFGASPIIAVDvRDEKLAKAKELGA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 212 DNVINRKKKEVEVEVEKITGGVGVDAVVDNAGQ-KTFTTSINCVRKGGKIALCG-TTSGNIANFQIRTFYSKQIQLLGIL 289
Cdd:cd08263  234 THTVNAAKEDAVAAIREITGGRGVDVVVEALGKpETFKLALDVVRDGGRAVVVGlAPGGATAEIPITRLVRRGIKIIGSY 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 262089307 290 IG-SKLELLELMKFVSKKNILPK--VDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd08263  314 GArPRQDLPELVGLAASGKLDPEalVTHKYKLEEINEAYENLRKGLIHGRAIV 366
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 1.08e-47

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 163.50  E-value: 1.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLESeankhskg 80
Cdd:cd08272    1 MKALVLESFGGPEVFELR-EVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPLPAILGCDVAGVVEA-------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  81 trvlVYPGIScnhcNYcRTGNETicrdFSIIGGLSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN-IFK 159
Cdd:cd08272   72 ----VGEGVT----RF-RVGDEV----YGCAGGLGGLQGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEgLVD 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 160 KLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDsKLNFARSLGSDNVINRKKKEVEVEVEKiTGGVGVDAVV 239
Cdd:cd08272  139 RAAVQAGQTVLIHGGAGGVGHVAVQLAKAAGARVYATASSE-KAAFARSLGADPIIYYRETVVEYVAEH-TGGRGFDVVF 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 240 DNAGQKTFTTSINCVRKGGKIA-LCGTTSGNIANFQIRTF-YSKQIQLLGILIGSKLE-----LLELMKFVSKKNILPKV 312
Cdd:cd08272  217 DTVGGETLDASFEAVALYGRVVsILGGATHDLAPLSFRNAtYSGVFTLLPLLTGEGRAhhgeiLREAARLVERGQLRPLL 296

                        330       340       350
                 ....*....|....*....|....*....|
gi 262089307 313 DSI-YTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08272  297 DPRtFPLEEAAAAHARLESGSARGKIVIDV 326
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-340 1.36e-47

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 163.54  E-value: 1.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLD--IWTRTGIAGKPisfPHICGSDIVG---SLESEAN 75
Cdd:cd08235    1 MKAAVLHGPNDVRL----EEVPVPEPGPGEVLVKVRACGICGTDvkKIRGGHTDLKP---PRILGHEIAGeivEVGDGVT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVP-----KTNIVPIPNEISDEHAA---TL 147
Cdd:cd08235   74 GFKVGDRVFVAPHVPCGECHYCLRGNENMCPNYKKFG--NLYDGGFAEYVRVPawavkRGGVLKLPDNVSFEEAAlvePL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 148 SisylTAWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEI-KIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEV 226
Cdd:cd08235  152 A----CCINAQRKAGIKPGDTVLVIGA-GPIGLLHAMLAKASGArKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKV 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 227 EKITGGVGVDAVVDNAGQ-KTFTTSINCVRKGGKIALCGTTS-GNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVS 304
Cdd:cd08235  227 RELTDGRGADVVIVATGSpEAQAQALELVRKGGRILFFGGLPkGSTVNIDPNLIHYREITITGSYAASPEDYKEALELIA 306

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262089307 305 KKNILPK--VDSIYTLAEIHKAHTLLERGQQLgKILIK 340
Cdd:cd08235  307 SGKIDVKdlITHRFPLEDIEEAFELAADGKSL-KIVIT 343
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1-341 1.17e-45

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 158.28  E-value: 1.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGpiEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKpISFPHICGSDIVGSLE---SEANKH 77
Cdd:PRK13771   1 MKAVILPGFK--QGYRIE-EVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPR-MKYPVILGHEVVGTVEevgENVKGF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRV--LVYpgISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:PRK13771  77 KPGDRVasLLY--APDGTCEYCRSGEEAYCKNRLGYG--EELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLgSDNVINRKKKEVEVEVEKitggvGV 235
Cdd:PRK13771 153 RGLRRAGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKY-ADYVIVGSKFSEEVKKIG-----GA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 DAVVDNAGQKTFTTSINCVRKGGKIALCgttsGNI---ANFQIRTFYS--KQIQLLGILIGSKLELLELMKFVSKKNILP 310
Cdd:PRK13771 227 DIVIETVGTPTLEESLRSLNMGGKIIQI----GNVdpsPTYSLRLGYIilKDIEIIGHISATKRDVEEALKLVAEGKIKP 302

                        330       340       350
                 ....*....|....*....|....*....|.
gi 262089307 311 KVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:PRK13771 303 VIGAEVSLSEIDKALEELKDKSRIGKILVKP 333
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-340 4.46e-45

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 156.92  E-value: 4.46e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLD--IWtrtgiAGKPIS-FPHICGSDIVGSLE---SEA 74
Cdd:cd08234    1 MKALVYEGPGELEV----EEVPVPEPGPDEVLIKVAACGICGTDlhIY-----EGEFGAaPPLVPGHEFAGVVVavgSKV 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  75 NKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA 154
Cdd:cd08234   72 TGFKVGDRVAVDPNIYCGECFYCRRGRPNLCENLTAVG--VTRNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAV 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WNIfKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEI-KIITSVSDDSKLNFARSLGSDNVINrkKKEVEVEVEKITGGV 233
Cdd:cd08234  150 HGL-DLLGIKPGDSVLVFGA-GPIGLLLAQLLKLNGAsRVTVAEPNEEKLELAKKLGATETVD--PSREDPEAQKEDNPY 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 234 GVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNiANFQIRTF--YSKQIQLLGILI-----GSKLELLElmkfvSK 305
Cdd:cd08234  226 GFDVVIEATGvPKTLEQAIEYARRGGTVLVFGVYAPD-ARVSISPFeiFQKELTIIGSFInpytfPRAIALLE-----SG 299

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 262089307 306 K-NILPKVDSIYTLAEIHKAHTLLERGQQLgKILIK 340
Cdd:cd08234  300 KiDVKGLVSHRLPLEEVPEALEGMRSGGAL-KVVVV 334
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 19-339 3.18e-43

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 152.09  E-value: 3.18e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  19 KDFPKPVPNSSESLIKIKYCGLNHLDI--WTRT--GIAGKPISFPH-ICGsdIVGSLESEANKHSKGTRVLVYPGISCNH 93
Cdd:cd08239   15 REFPVPVPGPGEVLLRVKASGLCGSDLhyYYHGhrAPAYQGVIPGHePAG--VVVAVGPGVTHFRVGDRVMVYHYVGCGA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  94 CNYCRTGNETICRDFSIIGGLsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQLKKHDTLLVYG 173
Cdd:cd08239   93 CRNCRRGWMQLCTSKRAAYGW-NRDGGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALRRVGVSGRDTVLVVG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 174 AtGGLGMAVIQFAKAL--EIKIITSVSdDSKLNFARSLGSDNVINRkKKEVEVEVEKITGGVGVDAVVDNAGQKTF-TTS 250
Cdd:cd08239  172 A-GPVGLGALMLARALgaEDVIGVDPS-PERLELAKALGADFVINS-GQDDVQEIRELTSGAGADVAIECSGNTAArRLA 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 251 INCVRKGGKIALCGttSGNIANFQI-RTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPK--VDSIYTLAEIHKAHTL 327
Cdd:cd08239  249 LEAVRPWGRLVLVG--EGGELTIEVsNDLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVDrlVTHRFGLDQAPEAYAL 326

                        330
                 ....*....|..
gi 262089307 328 LERGqQLGKILI 339
Cdd:cd08239  327 FAQG-ESGKVVF 337
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 6-339 5.81e-43

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 150.83  E-value: 5.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   6 IYKHGPIEVLKYEK-DFPKPVPNSSESLIKIKYCGLNHLDIWTRTG--IAGKPISFPHICGSDIVGSLESEANKHS---K 79
Cdd:cd08267    3 YTRYGSPEVLLLLEvEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGppKLLLGRPFPPIPGMDFAGEVVAVGSGVTrfkV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  80 GTRVlvypgiscnhcnycrtgneticrdFSIIGGLSnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN-IF 158
Cdd:cd08267   83 GDEV------------------------FGRLPPKG--GGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQaLR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 159 KKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSdDSKLNFARSLGSDNVINRKKKEVEVEVekiTGGVGVDAV 238
Cdd:cd08267  137 DAGKVKPGQRVLINGASGGVGTFAVQIAKALGAHVTGVCS-TRNAELVRSLGADEVIDYTTEDFVALT---AGGEKYDVI 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 239 VDNAGQKTFT--TSINCVRKGGK-IALCGTTSG----NIANFQIRTFYSKQIQLLgILIGSKLELLELMKFVSKKNILPK 311
Cdd:cd08267  213 FDAVGNSPFSlyRASLALKPGGRyVSVGGGPSGlllvLLLLPLTLGGGGRRLKFF-LAKPNAEDLEQLAELVEEGKLKPV 291

                        330       340
                 ....*....|....*....|....*...
gi 262089307 312 VDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd08267  292 IDSVYPLEDAPEAYRRLKSGRARGKVVI 319
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 2-340 9.76e-43

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 150.81  E-value: 9.76e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   2 KAVPIYKHGPIEVLKYEKdFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES---EANKHS 78
Cdd:cd08275    1 RAVVLTGFGGLDKLKVEK-EALPEPSSGEVRVRVEACGLNFADLMARQGLYDSAPKPPFVPGFECAGTVEAvgeGVKDFK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 KGTRVLVYpgiscnhcnycrtgneticrdfsiigglsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW-NI 157
Cdd:cd08275   80 VGDRVMGL-----------------------------TRFGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYyAL 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 158 FKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGvGVDA 237
Cdd:cd08275  131 FELGNLRPGQSVLVHSAAGGVGLAAGQLCKTVPNVTVVGTASASKHEALKENGVTHVIDYRTQDYVEEVKKISPE-GVDI 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 238 VVDNAGQKTFTTSINCVRKGGKIALCGttSGNIANFQIRTFYS--KQ---------IQL-----------LGILIGSKLE 295
Cdd:cd08275  210 VLDALGGEDTRKSYDLLKPMGRLVVYG--AANLVTGEKRSWFKlaKKwwnrpkvdpMKLisenksvlgfnLGWLFEEREL 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 262089307 296 LLE----LMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08275  288 LTEvmdkLLKLYEEGKIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLT 336
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-260 7.75e-42

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 148.84  E-value: 7.75e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIwtrTGIAGKPISFP-----HICG-----------S 64
Cdd:cd08233    1 MKAARYHGRKDIRV----EEVPEPPVKPGEVKIKVAWCGICGSDL---HEYLDGPIFIPteghpHLTGetapvtlghefS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  65 DIVGSLESEANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGgLSNYNGGYAEYVVVPKTNIVPIPNEISDEHA 144
Cdd:cd08233   74 GVVVEVGSGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIG-LGGGGGGFAEYVVVPAYHVHKLPDNVPLEEA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 145 AT---LSIsyltAWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEI-KIItsVSD--DSKLNFARSLGSDNVINRK 218
Cdd:cd08233  153 ALvepLAV----AWHAVRRSGFKPGDTALVLGA-GPIGLLTILALKAAGAsKII--VSEpsEARRELAEELGATIVLDPT 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 262089307 219 KKEVEVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKI 260
Cdd:cd08233  226 EVDVVAEVRKLTGGGGVDVSFDCAGvQATLDTAIDALRPRGTA 268
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1-340 4.27e-41

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 146.33  E-value: 4.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLE---SEANKH 77
Cdd:PTZ00354   2 MRAVTLKGFGGVDVLKI-GESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPPPGSSEILGLEVAGYVEdvgSDVKRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVlvypgiscnhcnycrtgneticrdFSIIGGlsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNI 157
Cdd:PTZ00354  81 KEGDRV------------------------MALLPG-----GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 158 FKKL-QLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINR-KKKEVEVEVEKITGGVGV 235
Cdd:PTZ00354 132 LKKHgDVKKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTSSEEKVDFCKKLAAIILIRYpDEEGFAPKVKKLTGEKGV 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 DAVVDNAGQKTFTTSINCVRKGGKIALCGTTSG-NIANFQIRTFYSKQIQllgiLIGSKL---------ELL-----ELM 300
Cdd:PTZ00354 212 NLVLDCVGGSYLSETAEVLAVDGKWIVYGFMGGaKVEKFNLLPLLRKRAS----IIFSTLrsrsdeykaDLVasferEVL 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 262089307 301 KFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:PTZ00354 288 PYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIGKVVLT 327
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-332 9.50e-40

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 142.71  E-value: 9.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEV--LKYEkDFPKPVPNSSESLIKIKYCGLNH--LDIwtrtgIAG--KPISFPHICGSDIVGSLE--- 71
Cdd:cd08298    1 MKAMVLEKPGPIEEnpLRLT-EVPVPEPGPGEVLIKVEACGVCRtdLHI-----VEGdlPPPKLPLIPGHEIVGRVEavg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  72 SEANKHSKGTRVLVYP-GISCNHCNYCRTGNETICRDFSIIGglsnY--NGGYAEYVVVPKTNIVPIPNEISDEHAATLS 148
Cdd:cd08298   75 PGVTRFSVGDRVGVPWlGSTCGECRYCRSGRENLCDNARFTG----YtvDGGYAEYMVADERFAYPIPEDYDDEEAAPLL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 149 ISYLTAWNIFKKLQLKKHDTLLVYGaTGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEK 228
Cdd:cd08298  151 CAGIIGYRALKLAGLKPGQRLGLYG-FGASAHLALQIARYQGAEVFAFTRSGEHQELARELGADWAGDSDDLPPEPLDAA 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 229 ITGGvGVDAVVDNAgqktfttsINCVRKGGKIALCGTTSGNIANFQI-RTFYSKQIqlLGILIGSKLELLELMKFVSKKN 307
Cdd:cd08298  230 IIFA-PVGALVPAA--------LRAVKKGGRVVLAGIHMSDIPAFDYeLLWGEKTI--RSVANLTRQDGEEFLKLAAEIP 298

                        330       340
                 ....*....|....*....|....*
gi 262089307 308 ILPKVdSIYTLAEIHKAHTLLERGQ 332
Cdd:cd08298  299 IKPEV-ETYPLEEANEALQDLKEGR 322
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-287 4.00e-39

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 141.59  E-value: 4.00e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDiWTrtGIAGKP--ISFPHICGSDIVGSLES---EA 74
Cdd:cd08260    1 MRAAVYEEFGePLEI----REVPDPEPPPDGVVVEVEACGVCRSD-WH--GWQGHDpdVTLPHVPGHEFAGVVVEvgeDV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  75 NKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPK--TNIVPIPNEISDEHAATLSISYL 152
Cdd:cd08260   74 SRWRVGDRVTVPFVLGCGTCPYCRAGDSNVCEHQVQPG--FTHPGSFAEYVAVPRadVNLVRLPDDVDFVTAAGLGCRFA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 153 TAWN-IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVIN-RKKKEVEVEVEKIT 230
Cdd:cd08260  152 TAFRaLVHQARVKPGEWVAVHGC-GGVGLSAVMIASALGARVIAVDIDDDKLELARELGAVATVNaSEVEDVAAAVRDLT 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 231 GGvGVDAVVDNAGQK-TFTTSINCVRKGGKIALCGTTSGNIANFQIRT--FYSKQIQLLG 287
Cdd:cd08260  231 GG-GAHVSVDALGIPeTCRNSVASLRKRGRHVQVGLTLGEEAGVALPMdrVVARELEIVG 289
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 8-332 3.26e-37

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 136.09  E-value: 3.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   8 KHGPIEVLKYEKDFPKPvpnsSESLIKIKYCGLNHLDIWTRTGIAGkPISFPHICGSDIVG---SLESEANKHSKGTRVl 84
Cdd:cd05283    8 ASGKLEPFTFERRPLGP----DDVDIKITYCGVCHSDLHTLRNEWG-PTKYPLVPGHEIVGivvAVGSKVTKFKVGDRV- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  85 vypGI-----SCNHCNYCRTGNETICRDFSIIGGLSNYN-----GGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA 154
Cdd:cd05283   82 ---GVgcqvdSCGTCEQCKSGEEQYCPKGVVTYNGKYPDgtitqGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WNIFKKLQLKKHDTLLVYGaTGGLG-MAvIQFAKAL--EIKIITsvSDDSKLNFARSLGSDNVINRKkkevevevekitg 231
Cdd:cd05283  159 YSPLKRNGVGPGKRVGVVG-IGGLGhLA-VKFAKALgaEVTAFS--RSPSKKEDALKLGADEFIATK------------- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 232 gvgvDAVVDNAGQKTF-----TTS--------INCVRKGGKIALCGTTSGNIAnFQIRTFYSKQIQLLGILIGSKLELLE 298
Cdd:cd05283  222 ----DPEAMKKAAGSLdliidTVSashdldpyLSLLKPGGTLVLVGAPEEPLP-VPPFPLIFGRKSVAGSLIGGRKETQE 296

                        330       340       350
                 ....*....|....*....|....*....|....
gi 262089307 299 LMKFVSKKNILPKVDsIYTLAEIHKAHTLLERGQ 332
Cdd:cd05283  297 MLDFAAEHGIKPWVE-VIPMDGINEALERLEKGD 329
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 8-332 8.13e-37

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 136.39  E-value: 8.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   8 KHGPIEVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGI----------AGKPISFpHICGSD---IVGSLESEA 74
Cdd:cd08246   22 RYGDPAQAIQLEDVPVPELGPGEVLVAVMAAGVNYNNVWAALGEpvstfaarqrRGRDEPY-HIGGSDasgIVWAVGEGV 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  75 NKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSNYnGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA 154
Cdd:cd08246  101 KNWKVGDEVVVHCSVWDGNDPERAGGDPMFDPSQRIWGYETNY-GSFAQFALVQATQLMPKPKHLSWEEAAAYMLVGATA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WNIF---KKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEK--- 228
Cdd:cd08246  180 YRMLfgwNPNTVKPGDNVLIWGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGAEGVINRRDFDHWGVLPDvns 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 229 -------------------ITGG-VGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGI 288
Cdd:cd08246  260 eaytawtkearrfgkaiwdILGGrEDPDIVFEHPGRATFPTSVFVCDRGGMVVICAGTTGYNHTYDNRYLWMRQKRIQGS 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 262089307 289 LIGSKLELLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQ 332
Cdd:cd08246  340 HFANDREAAEANRLVMKGRIDPCLSKVFSLDETPDAHQLMHRNQ 383
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 1-332 1.02e-36

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADHs), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 134.68  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYK-HGPIEVLkyEKDFPKPVPNssESLIKIKYCGLNHLDIWTRTGiAGKPISFPHICGSDIVGSLE---SEANK 76
Cdd:cd08296    1 YKAVQVTEpGGPLELV--ERDVPLPGPG--EVLIKVEACGVCHSDAFVKEG-AMPGLSYPRVPGHEVVGRIDavgEGVSR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  77 HSKGTRVLV-YPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd08296   76 WKVGDRVGVgWHGGHCGTCDACRRGDFVHCENGKVTG--VTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGaTGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGV 235
Cdd:cd08296  154 NALRNSGAKPGDLVAVQG-IGGLGHLAVQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDTSKEDVAEALQELGGAKLI 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 DAVVDNAgqKTFTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDsI 315
Cdd:cd08296  233 LATAPNA--KAISALVGGLAPRGKLLILGAAGEPV-AVSPLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVE-T 308

                        330
                 ....*....|....*..
gi 262089307 316 YTLAEIHKAHTLLERGQ 332
Cdd:cd08296  309 FPLEKANEAYDRMMSGK 325
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 6-339 8.11e-36

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 132.02  E-value: 8.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   6 IYKHGPIEVLKYEK-DFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLE---SEANKHSKGT 81
Cdd:cd05282    3 YTQFGEPLPLVLELvSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSRPPLPAVPGNEGVGVVVevgSGVSGLLVGQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  82 RVLVYPGiscnhcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKL 161
Cdd:cd05282   83 RVLPLGG-----------------------------EGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEY 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 162 Q-LKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVDAVVD 240
Cdd:cd05282  134 LkLPPGDWVIQNAANSAVGRMLIQLAKLLGFKTINVVRRDEQVEELKALGADEVIDSSPEDLAQRVKEATGGAGARLALD 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 241 NAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELL----------ELMKFVSKKNILP 310
Cdd:cd05282  214 AVGGESATRLARSLRPGGTLVNYGLLSGEPVPFPRSVFIFKDITVRGFWLRQWLHSAtkeakqetfaEVIKLVEAGVLTT 293

                        330       340
                 ....*....|....*....|....*....
gi 262089307 311 KVDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd05282  294 PVGAKFPLEDFEEAVAAAEQPGRGGKVLL 322
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-261 8.09e-35

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 129.70  E-value: 8.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDiWTRTGIAGKPISFPHICGSDIVGSLESEANKHS-- 78
Cdd:cd08271    1 MKAWVLPKPGAALQLTLE-EIEIPGPGAGEVLVKVHAAGLNPVD-WKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTgw 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 -KGTRVLVYPGIScnhcnycrtgneticrdfsiigglsnYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN- 156
Cdd:cd08271   79 kVGDRVAYHASLA--------------------------RGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQa 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVsddSKLNFA--RSLGSDNVINRKKKEVEVEVEKITGGVG 234
Cdd:cd08271  133 LFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTC---SKRNFEyvKSLGADHVIDYNDEDVCERIKEITGGRG 209

                        250       260
                 ....*....|....*....|....*..
gi 262089307 235 VDAVVDNAGQKTFTTSINCVRKGGKIA 261
Cdd:cd08271  210 VDAVLDTVGGETAAALAPTLAFNGHLV 236
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 1-340 1.12e-34

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 129.38  E-value: 1.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKyEKDFPKPVPNssESLIKIKYCGLNHLDIWTRTGIAGKP--ISFPHIcGSDIVGSLESEANKHS 78
Cdd:PRK09422   1 MKAAVVNKDHTGDVVV-EKTLRPLKHG--EALVKMEYCGVCHTDLHVANGDFGDKtgRILGHE-GIGIVKEVGPGVTSLK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 KGTRVLV---YPGisCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:PRK09422  77 VGDRVSIawfFEG--CGHCEYCTTGRETLCRSVKNAG--YTVDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTTY 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAK-ALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGvG 234
Cdd:PRK09422 153 KAIKVSGIKPGQWIAIYGA-GGLGNLALQYAKnVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQEKTG-G 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 235 VDAVVDNAGQKT-FTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVD 313
Cdd:PRK09422 231 AHAAVVTAVAKAaFNQAVDAVRAGGRVVAVGLPPESM-DLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQ 309

                        330       340
                 ....*....|....*....|....*..
gi 262089307 314 SIyTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:PRK09422 310 LR-PLEDINDIFDEMEQGKIQGRMVID 335
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 30-339 1.43e-34

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 128.07  E-value: 1.43e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  30 ESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLESEANKHSKGTRVLvypgiscnhcnycrtgneticrdfs 109
Cdd:cd05195    2 EVEVEVKAAGLNFRDVLVALGLLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVM------------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 110 iigGLSNynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKL-QLKKHDTLLVYGATGGLGMAVIQFAKA 188
Cdd:cd05195   57 ---GLAP--GAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDLaRLQKGESVLIHAAAGGVGQAAIQLAQH 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 189 LEIKIITSVSDDSKLNFARSLG--SDNVINRKKKEVEVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTT 266
Cdd:cd05195  132 LGAEVFATVGSEEKREFLRELGgpVDHIFSSRDLSFADGILRATGGRGVDVVLNSLSGELLRASWRCLAPFGRFVEIGKR 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 267 sGNIANFQI--------RTFYSkqIQLLGILIGSKLE----LLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQL 334
Cdd:cd05195  212 -DILSNSKLgmrpflrnVSFSS--VDLDQLARERPELlrelLREVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHI 288


                 ....*
gi 262089307 335 GKILI 339
Cdd:cd05195  289 GKVVL 293
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 1-329 8.95e-32

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 122.00  E-value: 8.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNSS-ESLIKIKYCGLNHLDIWT-RTGIAGKPisFPHICGSDIVGSLE---SEAN 75
Cdd:cd05278    1 MKALVYLGPGKIGL----EEVPDPKIQGPhDAIVRVTATSICGSDLHIyRGGVPGAK--HGMILGHEFVGEVVevgSDVK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSN-YNGGYAEYVVVPK--TNIVPIPNEISDEHAATLSISYL 152
Cdd:cd05278   75 RLKPGDRVSVPCITFCGRCRFCRRGYHAHCENGLWGWKLGNrIDGGQAEYVRVPYadMNLAKIPDGLPDEDALMLSDILP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 153 TAWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEI-KIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITG 231
Cdd:cd05278  155 TGFHGAELAGIKPGSTVAVIGA-GPVGLCAVAGARLLGAaRIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELTG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 232 GVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILP 310
Cdd:cd05278  234 GRGVDCVIEAVGfEETFEQAVKVVRPGGTIANVGVYGKPDPLPLLGEWFGKNLTFKTGLVPVRARMPELLDLIEEGKIDP 313

                        330       340
                 ....*....|....*....|.
gi 262089307 311 K--VDSIYTLAEIHKAHTLLE 329
Cdd:cd05278  314 SklITHRFPLDDILKAYRLFD 334
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 1-340 1.26e-30

2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 118.20  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEVLKyEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGSLES--EANKH 77
Cdd:cd08292    1 MRAAVHTQFGdPADVLE-IGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYKPELPAIGGSEAVGVVDAvgEGVKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SK-GTRVLVYPGiscnhcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWN 156
Cdd:cd08292   80 LQvGQRVAVAPV-----------------------------HGTWAEYFVAPADGLVPLPDGISDEVAAQLIAMPLSALM 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVD 236
Cdd:cd08292  131 LLDFLGVKPGQWLIQNAAGGAVGKLVAMLAAARGINVINLVRRDAGVAELRALGIGPVVSTEQPGWQDKVREAAGGAPIS 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 237 AVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELL----------ELMKFVSKK 306
Cdd:cd08292  211 VALDSVGGKLAGELLSLLGEGGTLVSFGSMSGEPMQISSGDLIFKQATVRGFWGGRWSQEMsveyrkrmiaELLTLALKG 290

                        330       340       350
                 ....*....|....*....|....*....|....
gi 262089307 307 NILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08292  291 QLLLPVEAVFDLGDAAKAAAASMRPGRAGKVLLR 324
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 110-339 2.38e-30

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 117.14  E-value: 2.38e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 110 IIGGLSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKAL 189
Cdd:cd08251   65 VIAGTGESMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTATGGTGLMAVQLARLK 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 190 EIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGK---IALCGTT 266
Cdd:cd08251  145 GAEIYATASSDDKLEYLKQLGVPHVINYVEEDFEEEIMRLTGGRGVDVVINTLSGEAIQKGLNCLAPGGRyveIAMTALK 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 267 SGN------IANFQirTFYSKQIQLLGIL----IGSklELLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGK 336
Cdd:cd08251  225 SAPsvdlsvLSNNQ--SFHSVDLRKLLLLdpefIAD--YQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGK 300


                 ...
gi 262089307 337 ILI 339
Cdd:cd08251  301 VVV 303
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 1-332 3.63e-30

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 117.64  E-value: 3.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEVLKYEKDFPKPvpnsSESLIKIKYCGLNHLDIWTRTGiaGKPISFPHICG---SDIVGSLESEANK 76
Cdd:cd08279    1 MRAAVLHEVGkPLEIEEVELDDPGP----GEVLVRIAAAGLCHSDLHVVTG--DLPAPLPAVLGhegAGVVEEVGPGVTG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  77 HSKGTRVLVYPGISCNHCNYCRTGNETIC----------------------RDFSIIGGLsnynGGYAEYVVVPKTNIVP 134
Cdd:cd08279   75 VKPGDHVVLSWIPACGTCRYCSRGQPNLCdlgagilggqlpdgtrrftadgEPVGAMCGL----GTFAEYTVVPEASVVK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 135 IPNEISDEHAATLSISYLTAWN-IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAK-ALEIKIITSVSDDSKLNFARSLGSD 212
Cdd:cd08279  151 IDDDIPLDRAALLGCGVTTGVGaVVNTARVRPGDTVAVIGC-GGVGLNAIQGARiAGASRIIAVDPVPEKLELARRFGAT 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 213 NVINRKKKEVEVEVEKITGGVGVDAVVDNAGQK-TFTTSINCVRKGGKIALCG-TTSGNIANFQIRTFYSKQIQLLGILI 290
Cdd:cd08279  230 HTVNASEDDAVEAVRDLTDGRGADYAFEAVGRAaTIRQALAMTRKGGTAVVVGmGPPGETVSLPALELFLSEKRLQGSLY 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 262089307 291 GS-----------------KLELLELmkfVSKknilpkvdsIYTLAEIHKAHTLLERGQ 332
Cdd:cd08279  310 GSanprrdiprlldlyragRLKLDEL---VTR---------RYSLDEINEAFADMLAGE 356
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 30-134 4.80e-30

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 110.39  E-value: 4.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   30 ESLIKIKYCGLNHLDIWTRTGiAGKPISFPHICGSDIVGSLE---SEANKHSKGTRVLVYPGISCNHCNYCRTGNETICR 106
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKG-GNPPVKLPLILGHEFAGEVVevgPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80

                          90       100
                  ....*....|....*....|....*...
gi 262089307  107 DFSIIGglSNYNGGYAEYVVVPKTNIVP 134
Cdd:pfam08240  81 NGRFLG--YDRDGGFAEYVVVPERNLVP 106
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1-340 1.05e-29

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 116.20  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKPVPNS-SESLIKIKYCGLNHLDI-WTRTGIAGKPisfPHICGSDIVGSLE---SEAN 75
Cdd:cd08284    1 MKAVVFKGPGDVRV----EEVPIPQIQDpTDAIVKVTAAAICGSDLhIYRGHIPSTP---GFVLGHEFVGEVVevgPEVR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGISCNHCNYCRTGNETIC--RDFSIIGGLSNYNGGYAEYVVVPK--TNIVPIPNEISDEHAATLSISY 151
Cdd:cd08284   74 TLKVGDRVVSPFTIACGECFYCRRGQSGRCakGGLFGYAGSPNLDGAQAEYVRVPFadGTLLKLPDGLSDEAALLLGDIL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 152 LTAWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSV-SDDSKLNFARSLGSDnVINRKKKEVEVEVEKIT 230
Cdd:cd08284  154 PTGYFGAKRAQVRPGDTVAVIGC-GPVGLCAVLSAQVLGAARVFAVdPVPERLERAAALGAE-PINFEDAEPVERVREAT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 231 GGVGVDAVVDNAGQ-KTFTTSINCVRKGGKIALCGT-TSGNIAnFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNI 308
Cdd:cd08284  232 EGRGADVVLEAVGGaAALDLAFDLVRPGGVISSVGVhTAEEFP-FPGLDAYNKNLTLRFGRCPVRSLFPELLPLLESGRL 310

                        330       340       350
                 ....*....|....*....|....*....|....
gi 262089307 309 LPK--VDSIYTLAEIHKAHTLLERGQQLgKILIK 340
Cdd:cd08284  311 DLEflIDHRMPLEEAPEAYRLFDKRKVL-KVVLD 343
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1-264 3.25e-29

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 113.95  E-value: 3.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGP--IEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGiAGKPISFPHICGSDIVGSLE---SEAN 75
Cdd:cd08258    1 MKALVKTGPGPgnVEL----REVPEPEPGPGEVLIKVAAAGICGSDLHIYKG-DYDPVETPVVLGHEFSGTIVevgPDVE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVL-VYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA 154
Cdd:cd08258   76 GWKVGDRVVsETTFSTCGRCPYCRRGDYNLCPHRKGIG--TQADGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WNIFKKLQLKKHDTLLVYGaTGGLGMAVIQFAKAL--EIKIITSVSDDSKLNFARSLGSDnVINRKKKEVEVEVEKITGG 232
Cdd:cd08258  154 HAVAERSGIRPGDTVVVFG-PGPIGLLAAQVAKLQgaTVVVVGTEKDEVRLDVAKELGAD-AVNGGEEDLAELVNEITDG 231

                        250       260       270
                 ....*....|....*....|....*....|...
gi 262089307 233 VGVDAVVDNAGQ-KTFTTSINCVRKGGKIALCG 264
Cdd:cd08258  232 DGADVVIECSGAvPALEQALELLRKGGRIVQVG 264
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-339 5.25e-29

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 114.25  E-value: 5.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKyEKDFPKPVPNssESLIKIK---YCGLN-HLDIWTRTgiAGKPISFPHICGSDIVGSLEsEANK 76
Cdd:cd05281    1 MKAIVKTKAGPGAELV-EVPVPKPGPG--EVLIKVLaasICGTDvHIYEWDEW--AQSRIKPPLIFGHEFAGEVV-EVGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  77 HSK----GTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATL----- 147
Cdd:cd05281   75 GVTrvkvGDYVSAETHIVCGKCYQCRTGNYHVCQNTKILG--VDTDGCFAEYVVVPEENLWKNDKDIPPEIASIQeplgn 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 148 SISYLTAWNIFKKlqlkkhdTLLVYGAtGGLGMAVIQFAKAL-EIKIITSVSDDSKLNFARSLGSDNVINrKKKEVEVEV 226
Cdd:cd05281  153 AVHTVLAGDVSGK-------SVLITGC-GPIGLMAIAVAKAAgASLVIASDPNPYRLELAKKMGADVVIN-PREEDVVEV 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 227 EKITGGVGVDAVVDNAGQKT-FTTSINCVRKGGKIALCGTTSG----NIANFQIrtfySKQIQLLGIlIGSKL------- 294
Cdd:cd05281  224 KSVTDGTGVDVVLEMSGNPKaIEQGLKALTPGGRVSILGLPPGpvdiDLNNLVI----FKGLTVQGI-TGRKMfetwyqv 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 262089307 295 -ELLElmkfvSKK-NILPKVDSIYTLAEIHKAHTLLERGqQLGKILI 339
Cdd:cd05281  299 sALLK-----SGKvDLSPVITHKLPLEDFEEAFELMRSG-KCGKVVL 339
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 1-261 9.02e-29

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 113.45  E-value: 9.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAvpIYKHGPIEVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDiwTRTGIAGKPISFPHICGSDIVGSLE---SEANKH 77
Cdd:cd08249    1 QKA--AVLTGPGGGLLVVVDVPVPKPGPDEVLVKVKAVALNPVD--WKHQDYGFIPSYPAILGCDFAGTVVevgSGVTRF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLVypgiscnHCNYCRTGNeticrdfsiigglsNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA-WN 156
Cdd:cd08249   77 KVGDRVAG-------FVHGGNPND--------------PRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAaLA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 157 IFKKLQL----------KKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSddSKlNFA--RSLGSDNVINRKKKEVEV 224
Cdd:cd08249  136 LFQKLGLplpppkpspaSKGKPVLIWGGSSSVGTLAIQLAKLAGYKVITTAS--PK-NFDlvKSLGADAVFDYHDPDVVE 212

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 262089307 225 EVEKITGG---VGVDAVvdnAGQKTFTTSINCV--RKGGKIA 261
Cdd:cd08249  213 DIRAATGGklrYALDCI---STPESAQLCAEALgrSGGGKLV 251
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1-339 4.19e-28

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 111.31  E-value: 4.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEkDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPI--SFPHICGSDI---VGSLESEAN 75
Cdd:cd08244    1 MRAIRLHEFGPPEVLVPE-DVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWGPGPFppELPYVPGGEVagvVDAVGPGVD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVLVYPGIScnhcnycrtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd08244   80 PAWLGRRVVAHTGRA---------------------------GGGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTAL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGV 235
Cdd:cd08244  133 GLLDLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGGGGV 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 DAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGIL--IGSKLELLEL----MKFVSKKNIL 309
Cdd:cd08244  213 TVVLDGVGGAIGRAALALLAPGGRFLTYGWASGEWTALDEDDARRRGVTVVGLLgvQAERGGLRALearaLAEAAAGRLV 292

                        330       340       350
                 ....*....|....*....|....*....|
gi 262089307 310 PKVDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd08244  293 PVVGQTFPLERAAEAHAALEARSTVGKVLL 322
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-340 7.97e-28

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 110.82  E-value: 7.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLK-YEKDFPKPVPNssESLIKIKYCGLNHLDIWTRTGI-AGKPiSFPHICGSDIVG---SLESEAN 75
Cdd:cd08273    1 NREVVVTRRGGPEVLKvVEADLPEPAAG--EVVVKVEASGVSFADVQMRRGLyPDQP-PLPFTPGYDLVGrvdALGSGVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  76 KHSKGTRVlvypgiscnhcnycrtgneticrdfsiiGGLSNYnGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAW 155
Cdd:cd08273   78 GFEVGDRV----------------------------AALTRV-GGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAY 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 N-IFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSdDSKLNFARSLGS-------DNVINRkkkeveveve 227
Cdd:cd08273  129 QmLHRAAKVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTAS-ERNHAALRELGAtpidyrtKDWLPA---------- 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 228 KITGGvGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIAN---FQIRTFYSKQIQLLGILIGS------------ 292
Cdd:cd08273  198 MLTPG-GVDVVFDGVGGESYEESYAALAPGGTLVCYGGNSSLLQGrrsLAALGSLLARLAKLKLLPTGrratfyyvwrdr 276

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 262089307 293 -------KLELLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08273  277 aedpklfRQDLTELLDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVLL 331
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-271 1.06e-27

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 110.69  E-value: 1.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAvpIYKHGPIEVLKYEkDFPKPVPNSSESLIKIK---YCGLNhLDIWTRTGIAGKPISFPHICGSDIVGSLE---SEA 74
Cdd:PRK05396   1 MKA--LVKLKAEPGLWLT-DVPVPEPGPNDVLIKVKktaICGTD-VHIYNWDEWAQKTIPVPMVVGHEFVGEVVevgSEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  75 NKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAAtlsisylta 154
Cdd:PRK05396  77 TGFKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVG--VNRPGAFAEYLVIPAFNVWKIPDDIPDDLAA--------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 wnIFKKLQLKKHDTL---------LVYGAtGGLGM---AVIQFAKALEIkIITSVSDDsKLNFARSLGSDNVINRKKKEV 222
Cdd:PRK05396 146 --IFDPFGNAVHTALsfdlvgedvLITGA-GPIGImaaAVAKHVGARHV-VITDVNEY-RLELARKMGATRAVNVAKEDL 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 262089307 223 EVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIA 271
Cdd:PRK05396 221 RDVMAELGMTEGFDVGLEMSGaPSAFRQMLDNMNHGGRIAMLGIPPGDMA 270
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
177-305 2.38e-27

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 104.23  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  177 GLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVR 255
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGsPATLEQALKLLR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 262089307  256 KGGKIALCGTTSGNIAnFQIRTFYSKQIQLLGILIGSKLELLELMKFVSK 305
Cdd:pfam00107  81 PGGRVVVVGLPGGPLP-LPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 1-340 2.98e-27

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 109.62  E-value: 2.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEKDFPKPVPN-SSESLIKIKYCGLNHLDIWTRTG--------------IAGKPISFPHICGSD 65
Cdd:cd08248    1 MKAWQIHSYGGIDSLLLLENARIPVIRkPNQVLIKVHAASVNPIDVLMRSGygrtllnkkrkpqsCKYSGIEFPLTLGRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  66 IVGSLESeankhsKGTRVlvypgiscnhcnycrtgneticRDFSI----IGGLSNYN-GGYAEYVVVPKTNIVPIPNEIS 140
Cdd:cd08248   81 CSGVVVD------IGSGV----------------------KSFEIgdevWGAVPPWSqGTHAEYVVVPENEVSKKPKNLS 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 141 DEHAATLSISYLTAWNIFKKLQLKKHDT-----LLVYGATGGLGMAVIQFAKALEIKIITSVSDDSkLNFARSLGSDNVI 215
Cdd:cd08248  133 HEEAASLPYAGLTAWSALVNVGGLNPKNaagkrVLILGGSGGVGTFAIQLLKAWGAHVTTTCSTDA-IPLVKSLGADDVI 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 216 NRKKKEVEVEVEKITggvGVDAVVDNAGQKTFTTSINCVRKGGKIA--------------LCGTTSGNIANF-QIRTFYS 280
Cdd:cd08248  212 DYNNEDFEEELTERG---KFDVILDTVGGDTEKWALKLLKKGGTYVtlvspllkntdklgLVGGMLKSAVDLlKKNVKSL 288

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262089307 281 KQIQLL--GILIGSKLELLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08248  289 LKGSHYrwGFFSPSGSALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK 350
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 61-285 2.19e-26

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 107.62  E-value: 2.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  61 ICGSD-----------------------IVGSLESEANKHSKGTRVLVYPGISCNHCNYCRTGNETIC------RDFSII 111
Cdd:cd08283   37 ICGSDlhlyhgyipgmkkgdilghefmgVVEEVGPEVRNLKVGDRVVVPFTIACGECFYCKRGLYSQCdntnpsAEMAKL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 112 GG------------LSNYNGGYAEYVVVPKTNI--VPIPNEISDEHAATLSISYLTAWNIFKKLQLKKHDTLLVYGAtGG 177
Cdd:cd08283  117 YGhagagifgyshlTGGYAGGQAEYVRVPFADVgpFKIPDDLSDEKALFLSDILPTGYHAAELAEVKPGDTVAVWGC-GP 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 178 LGMAVIQFAKALEIKIITSV-SDDSKLNFARSLGSDNVINRKKKEVEVEV-EKITGGVGVDAVVDNAG------------ 243
Cdd:cd08283  196 VGLFAARSAKLLGAERVIAIdRVPERLEMARSHLGAETINFEEVDDVVEAlRELTGGRGPDVCIDAVGmeahgsplhkae 275

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 262089307 244 ----------QKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQL 285
Cdd:cd08283  276 qallkletdrPDALREAIQAVRKGGTVSIIGVYGGTVNKFPIGAAMNKGLTL 327
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 2.73e-26

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 106.56  E-value: 2.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAvpIYKHGPieVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGkpisFPHICGSDIVGSLESEANKHSKG 80
Cdd:cd08242    1 MKA--LVLDGG--LDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKGYYP----FPGVPGHEFVGIVEEGPEAELVG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  81 TRVLVYPGISCNHCNYCRTGNETICRDFSIIGgLSNYNGGYAEYVVVPKTNIVPIPNEISDEHAA---TLSisylTAWNI 157
Cdd:cd08242   73 KRVVGEINIACGRCEYCRRGLYTHCPNRTVLG-IVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVfaePLA----AALEI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 158 FKKLQLKKHDTLLVYGaTGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKevevevekiTGGVGVDA 237
Cdd:cd08242  148 LEQVPITPGDKVAVLG-DGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLGVETVLPDEAE---------SEGGGFDV 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 238 VVDNAG-QKTFTTSINCVRKGGKIALcGTTSGNIANFQIRTFYSKQIQLLGI---LIGSKLELLELMKFVSKknilPKVD 313
Cdd:cd08242  218 VVEATGsPSGLELALRLVRPRGTVVL-KSTYAGPASFDLTKAVVNEITLVGSrcgPFAPALRLLRKGLVDVD----PLIT 292

                        330       340       350
                 ....*....|....*....|....*....|
gi 262089307 314 SIYTLAEIHKAhtlLERGQQLG--KILIKI 341
Cdd:cd08242  293 AVYPLEEALEA---FERAAEPGalKVLLRP 319
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 3-341 3.47e-26

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 106.42  E-value: 3.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   3 AVPIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGlnhldiwtrtgiagkpisfphICGSDI-------VGSL----- 70
Cdd:cd05285    1 AAVLHGPGDLRL----EERPIPEPGPGEVLVRVRAVG---------------------ICGSDVhyykhgrIGDFvvkep 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  71 -----ES--------EANKHSK-GTRVLVYPGISCNHCNYCRTGNETICRD--FSiigGLSNYNGGYAEYVVVPKTNIVP 134
Cdd:cd05285   56 mvlghESagtvvavgSGVTHLKvGDRVAIEPGVPCRTCEFCKSGRYNLCPDmrFA---ATPPVDGTLCRYVNHPADFCHK 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 135 IPNEISDEHAA---TLSISYLTAwnifKKLQLKKHDTLLVYGAtGGLGMAVIQFAKAL---EIkIITSVsDDSKLNFARS 208
Cdd:cd05285  133 LPDNVSLEEGAlvePLSVGVHAC----RRAGVRPGDTVLVFGA-GPIGLLTAAVAKAFgatKV-VVTDI-DPSRLEFAKE 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 209 LGSDNVINRKKKEVEVEVEKI---TGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQ 284
Cdd:cd05285  206 LGATHTVNVRTEDTPESAEKIaelLGGKGPDVVIECTGaESCIQTAIYATRPGGTVVLVGMGKPEV-TLPLSAASLREID 284

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 285 LLGI------------LIGSKLEllelmkfvskkNILPKVDSIYTLAEIHKAHTLLERGQQLG-KILIKI 341
Cdd:cd05285  285 IRGVfryantyptaieLLASGKV-----------DVKPLITHRFPLEDAVEAFETAAKGKKGViKVVIEG 343
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 33-339 4.57e-26

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 105.16  E-value: 4.57e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307    33 IKIKYCGLNHLDIWTRTGIAGKPISFPHICgSDIVGSLESEANKHSKGTRVLvypgiscnhcnycrtgneticrdfsiig 112
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGLYPGEAVLGGEC-AGVVTRVGPGVTGLAVGDRVM---------------------------- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   113 GLSNynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKL-QLKKHDTLLVYGATGGLGMAVIQFAKALEI 191
Cdd:smart00829  52 GLAP--GAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLaRLRPGESVLIHAAAGGVGQAAIQLARHLGA 129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   192 KIITSVSDDSKLNFARSLG--SDNVINRKKKEVEVEVEKITGGVGVDaVVDN--AGQKTfTTSINCVRKGGKIALCGTT- 266
Cdd:smart00829 130 EVFATAGSPEKRDFLRALGipDDHIFSSRDLSFADEILRATGGRGVD-VVLNslSGEFL-DASLRCLAPGGRFVEIGKRd 207

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   267 ---SGNIANFQIR---TFYSkqIQLLGILIGSKL--ELL-ELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKI 337
Cdd:smart00829 208 irdNSQLAMAPFRpnvSYHA--VDLDALEEGPDRirELLaEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKV 285


                   ..
gi 262089307   338 LI 339
Cdd:smart00829 286 VL 287
PRK10083 PRK10083
putative oxidoreductase; Provisional
 22-216 1.66e-25

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 104.82  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  22 PKPVPNSSESLIKIKYCGLNHLDIWTRTGiaGKP-ISFPHICGSDIVGSLES--EANKHSK-GTRVLVYPGISCNHCNYC 97
Cdd:PRK10083  18 PIPQPAAGEVRVKVKLAGICGSDSHIYRG--HNPfAKYPRVIGHEFFGVIDAvgEGVDAARiGERVAVDPVISCGHCYPC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  98 RTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSiSYLTAWNIFKKLQLKKHDTLLVYGAtGG 177
Cdd:PRK10083  96 SIGKPNVCTSLVVLG--VHRDGGFSEYAVVPAKNAHRIPDAIADQYAVMVE-PFTIAANVTGRTGPTEQDVALIYGA-GP 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 262089307 178 LGMAVIQFAKAL-EIK-IITSVSDDSKLNFARSLGSDNVIN 216
Cdd:PRK10083 172 VGLTIVQVLKGVyNVKaVIVADRIDERLALAKESGADWVIN 212
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 9-334 2.57e-25

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 104.65  E-value: 2.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   9 HGPIEVlkYEKDFPKPVPNssESLIKIKYCGLNHLDIWTRTGIAGKpISFPHICGSDIVG---------SLESEANKHSK 79
Cdd:cd08231   10 GKPLEI--REVPLPDLEPG--AVLVRVRLAGVCGSDVHTVAGRRPR-VPLPIILGHEGVGrvvalgggvTTDVAGEPLKV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  80 GTRVLVYPGISCNHCNYCRTGNETICR--------DFSIIGGLSnynGGYAEYVVV-PKTNIVPIPNEISDEHAATLSIS 150
Cdd:cd08231   85 GDRVTWSVGAPCGRCYRCLVGDPTKCEnrkkygheASCDDPHLS---GGYAEHIYLpPGTAIVRVPDNVPDEVAAPANCA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 151 YLTAWNIFKKLQLK-KHDTLLVYGAtGGLGMAVIQFAKAL-EIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEK 228
Cdd:cd08231  162 LATVLAALDRAGPVgAGDTVVVQGA-GPLGLYAVAAAKLAgARRVIVIDGSPERLELAREFGADATIDIDELPDPQRRAI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 229 ---ITGGVGVDAVVDNAGQKT-FTTSINCVRKGGKIALCGTTSGN--IAnFQIRTFYSKQIQLLGILIGSKLELLELMKF 302
Cdd:cd08231  241 vrdITGGRGADVVIEASGHPAaVPEGLELLRRGGTYVLVGSVAPAgtVP-LDPERIVRKNLTIIGVHNYDPSHLYRAVRF 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 262089307 303 VSK-KNILP---KVDSIYTLAEIHKAHTLLERGQQL 334
Cdd:cd08231  320 LERtQDRFPfaeLVTHRYPLEDINEALELAESGTAL 355
PRK10754 PRK10754
NADPH:quinone reductase;
2-339 6.95e-24

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 99.81  E-value: 6.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   2 KAVPIYKHGPIEVLKYeKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAgKPISFPHICGSDIVGSLES--EANKHSK 79
Cdd:PRK10754   3 KRIEFHKHGGPEVLQA-VEFTPADPAENEVQVENKAIGINYIDTYIRSGLY-PPPSLPSGLGTEAAGVVSKvgSGVKHIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  80 -GTRVLvypgiscnhcnYCRTGNeticrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIF 158
Cdd:PRK10754  81 vGDRVV-----------YAQSAL-----------------GAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLL 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 159 KKL-QLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVDA 237
Cdd:PRK10754 133 RKTyEIKPDEQFLFHAAAGGVGLIACQWAKALGAKLIGTVGSAQKAQRAKKAGAWQVINYREENIVERVKEITGGKKVRV 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 238 VVDNAGQKTFTTSINCVRKGGKIALCGTTSG-------NIANfQIRTFYSKQIQLLGiLIGSKLELL----ELMKFVSKK 306
Cdd:PRK10754 213 VYDSVGKDTWEASLDCLQRRGLMVSFGNASGpvtgvnlGILN-QKGSLYVTRPSLQG-YITTREELTeasnELFSLIASG 290

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 262089307 307 NIlpKVD----SIYTLAEIHKAHTLLE-RGQQLGKILI 339
Cdd:PRK10754 291 VI--KVDvaeqQKFPLKDAQRAHEILEsRATQGSSLLI 326
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 1-341 2.30e-23

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 98.38  E-value: 2.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPiEVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGS-LESEANKHSK 79
Cdd:cd05280    1 FKALVVEEQDG-GVSLFLRTLPLDDLPEGDVLIRVHYSSLNYKDALAATGNGGVTRNYPHTPGIDAAGTvVSSDDPRFRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  80 GTRVLVypgiscnhcnycrTGneticrdfsiiGGLS-NYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA---W 155
Cdd:cd05280   80 GDEVLV-------------TG-----------YDLGmNTDGGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTAalsV 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDT-LLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVG 234
Cdd:cd05280  136 HRLEDNGQTPEDGpVLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQADYLKSLGASEVLDREDLLDESKKPLLKARWA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 235 vdAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGIL-----IGSKLELLELMKFVSKKNIL 309
Cdd:cd05280  216 --GAIDTVGGDVLANLLKQTKYGGVVASCGNAAGPELTTTVLPFILRGVSLLGIDsvncpMELRKQVWQKLATEWKPDLL 293

                        330       340       350
                 ....*....|....*....|....*....|..
gi 262089307 310 PKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd05280  294 EIVVREISLEELPEAIDRLLAGKHRGRTVVKI 325
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 1-259 2.84e-23

Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 98.63  E-value: 2.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIykHGPiEVLKYEKdFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIA------GKP--ISFPHICGSDIVGSL-- 70
Cdd:cd08256    1 MRAVVC--HGP-QDYRLEE-VPVPRPGPGEILVKVEACGICAGDIKCYHGAPsfwgdeNQPpyVKPPMIPGHEFVGRVve 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  71 ---ESEANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSNYNGGYAEYVVVPKTNIV-PIPNEISDEHAAT 146
Cdd:cd08256   77 lgeGAEERGVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHDLYGFQNNVNGGMAEYMRFPKEAIVhKVPDDIPPEDAIL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 147 LSiSYLTAWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITsVSD--DSKLNFARSLGSDNVINRKKKEVEV 224
Cdd:cd08256  157 IE-PLACALHAVDRANIKFDDVVVLAGA-GPLGLGMIGAARLKNPKKLI-VLDlkDERLALARKFGADVVLNPPEVDVVE 233

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 262089307 225 EVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGK 259
Cdd:cd08256  234 KIKELTGGYGCDIYIEATGhPSAVEQGLNMIRKLGR 269
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 1-324 3.12e-23

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 98.48  E-value: 3.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVpIYkHGP--IEVlkyeKDFPKP-VPNSSESLIKIKY---CGLNhLDIWtrtgiAGK--PISFPHICGSDIVGSLE- 71
Cdd:cd08286    1 MKAL-VY-HGPgkISW----EDRPKPtIQEPTDAIVKMLKttiCGTD-LHIL-----KGDvpTVTPGRILGHEGVGVVEe 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  72 --SEANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDfsiiGG--LSNY-NGGYAEYVVVP--KTNIVPIPNEISDEHA 144
Cdd:cd08286   69 vgSAVTNFKVGDRVLISCISSCGTCGYCRKGLYSHCES----GGwiLGNLiDGTQAEYVRIPhaDNSLYKLPEGVDEEAA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 145 ATLSISYLTAWNI-FKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALE-IKIITSVSDDSKLNFARSLGSDNVINRKKKEV 222
Cdd:cd08286  145 VMLSDILPTGYECgVLNGKVKPGDTVAIVGA-GPVGLAALLTAQLYSpSKIIMVDLDDNRLEVAKKLGATHTVNSAKGDA 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 223 EVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTsGNIANFQIRTFYSKQIQLLGILIgSKLELLELMK 301
Cdd:cd08286  224 IEQVLELTDGRGVDVVIEAVGiPATFELCQELVAPGGHIANVGVH-GKPVDLHLEKLWIKNITITTGLV-DTNTTPMLLK 301

                        330       340
                 ....*....|....*....|....*
gi 262089307 302 FVSKKNILPK--VDSIYTLAEIHKA 324
Cdd:cd08286  302 LVSSGKLDPSklVTHRFKLSEIEKA 326
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 26-292 2.40e-22

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 96.03  E-value: 2.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  26 PNSSESLIKIKYCGLNHLDIWTRTGiaGKPISFPHICG---SDIVGSLESEANKHSKGTRV-LVYPgiSCNHCNYCRTGN 101
Cdd:cd08278   25 PRPDEVLVRIVATGICHTDLVVRDG--GLPTPLPAVLGhegAGVVEAVGSAVTGLKPGDHVvLSFA--SCGECANCLSGH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 102 ETICRDFSiiggLSNYNGG-------------------------YAEYVVVPKTNIVPIPNEISDEHAATLSISYLT-AW 155
Cdd:cd08278  101 PAYCENFF----PLNFSGRrpdgstplslddgtpvhghffgqssFATYAVVHERNVVKVDKDVPLELLAPLGCGIQTgAG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 156 NIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVsD--DSKLNFARSLGSDNVINRKKKEVEVEVEKITGGv 233
Cdd:cd08278  177 AVLNVLKPRPGSSIAVFGA-GAVGLAAVMAAKIAGCTTIIAV-DivDSRLELAKELGATHVINPKEEDLVAAIREITGG- 253

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262089307 234 GVDAVVDNAGQKT-FTTSINCVRKGGKIALCGTTS-GNIANFQIRTFYSKQIQLLGILIGS 292
Cdd:cd08278  254 GVDYALDTTGVPAvIEQAVDALAPRGTLALVGAPPpGAEVTLDVNDLLVSGKTIRGVIEGD 314
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 1-325 1.40e-21

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 93.91  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKP-VPNSSESLIKIK---YCGLnhlDIWTRTGIAgkPISFPHICGSDIVGSLE---SE 73
Cdd:cd08287    1 MRATVIHGPGDIRV----EEVPDPvIEEPTDAVIRVVatcVCGS---DLWPYRGVS--PTRAPAPIGHEFVGVVEevgSE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  74 ANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGLSnyNGGYAEYVVVPKTN--IVPIPNEISD-----EHAAT 146
Cdd:cd08287   72 VTSVKPGDFVIAPFAISDGTCPFCRAGFTTSCVHGGFWGAFV--DGGQGEYVRVPLADgtLVKVPGSPSDdedllPSLLA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 147 LSISYLTAWNIFKKLQLKKHDTLLVYGaTGGLG-MAVIQfAKALEIK-IITSVSDDSKLNFARSLGSDNVINRKKKEVEV 224
Cdd:cd08287  150 LSDVMGTGHHAAVSAGVRPGSTVVVVG-DGAVGlCAVLA-AKRLGAErIIAMSRHEDRQALAREFGATDIVAERGEEAVA 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 225 EVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFV 303
Cdd:cd08287  228 RVRELTGGVGADAVLECVGtQESMEQAIAIARPGGRVGYVGVPHGGV-ELDVRELFFRNVGLAGGPAPVRRYLPELLDDV 306

                        330       340
                 ....*....|....*....|....
gi 262089307 304 SKKNILP-KV-DSIYTLAEIHKAH 325
Cdd:cd08287  307 LAGRINPgRVfDLTLPLDEVAEGY 330
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1-340 2.39e-21

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 92.97  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPI---EVLKyEKDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISfPHICGSDIVGSLE---SEA 74
Cdd:cd08252    1 MKAIGFTQPLPItdpDSLI-DIELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQ-PKILGWDASGVVEavgSEV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  75 NKHSKGTRVLvYPGiscnhcnycrtgneTICRDfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA 154
Cdd:cd08252   79 TLFKVGDEVY-YAG--------------DITRP-----------GSNAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTA 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 155 WN-IFKKLQLKKHD-----TLLVYGATGGLGMAVIQFAKAL-EIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVE 227
Cdd:cd08252  133 WEaLFDRLGISEDAenegkTLLIIGGAGGVGSIAIQLAKQLtGLTVIATASRPESIAWVKELGADHVINHHQDLAEQLEA 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 228 KitGGVGVDAVVD-NAGQKTFTTSINCVRKGGKIALcgtTSGNIANFQIRTFYSKQIQLLGILIGSKL-----------E 295
Cdd:cd08252  213 L--GIEPVDYIFClTDTDQHWDAMAELIAPQGHICL---IVDPQEPLDLGPLKSKSASFHWEFMFTRSmfqtpdmieqhE 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 262089307 296 LL-ELMKFVSKKNILPKVDSIY---TLAEIHKAHTLLERGQQLGKILIK 340
Cdd:cd08252  288 ILnEVADLLDAGKLKTTLTETLgpiNAENLREAHALLESGKTIGKIVLE 336
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 1-216 7.39e-21

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 91.51  E-value: 7.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEVLKYEKDFPKPVPNSSESLIKIKYCGLNHLDIWTrtgIAG----KP---ISFPHICGSDIVGSLEs 72
Cdd:cd08290    1 AKALVYTEHGePKEVLQLESYEIPPPGPPNEVLVKMLAAPINPADINQ---IQGvypiKPpttPEPPAVGGNEGVGEVV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  73 EANKHSKGTRV--LVYPGISCNhcnycrtgneticrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSIS 150
Cdd:cd08290   77 KVGSGVKSLKPgdWVIPLRPGL--------------------------GTWRTHAVVPADDLIKVPNDVDPEQAATLSVN 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 262089307 151 YLTAWNIFKK-LQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKL----NFARSLGSDNVIN 216
Cdd:cd08290  131 PCTAYRLLEDfVKLQPGDWVIQNGANSAVGQAVIQLAKLLGIKTINVVRDRPDLeelkERLKALGADHVLT 201
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 30-341 5.96e-20

Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 88.92  E-value: 5.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  30 ESLIKIKYCGLNHLDiwtrtGIAGKPI-----SFPHICGSDIVGSLESEankhskgtrvlvypgiscNHCNYcRTGNETI 104
Cdd:cd08289   29 DVLIRVAYSSVNYKD-----GLASIPGgkivkRYPFIPGIDLAGTVVES------------------NDPRF-KPGDEVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 105 CRDFSIigGLSNYnGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQLK----KHDTLLVYGATGGLGM 180
Cdd:cd08289   85 VTSYDL--GVSHH-GGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFTAALSIHRLEENgltpEQGPVLVTGATGGVGS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 181 AVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKitGGVGVDAVVDNAGQKTFTTSINCVRKGGKI 260
Cdd:cd08289  162 LAVSILAKLGYEVVASTGKADAADYLKKLGAKEVIPREELQEESIKPL--EKQRWAGAVDPVGGKTLAYLLSTLQYGGSV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 261 ALCGTTSGNIANFQIRTFYSKQIQLLGilIGSKLELLELMKFVSKK--------NILPKVDSIYTLAEIHKAHTLLERGQ 332
Cdd:cd08289  240 AVSGLTGGGEVETTVFPFILRGVNLLG--IDSVECPMELRRRIWRRlatdlkptQLLNEIKQEITLDELPEALKQILQGR 317


                 ....*....
gi 262089307 333 QLGKILIKI 341
Cdd:cd08289  318 VTGRTVVKL 326
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
 119-339 1.02e-19

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 88.31  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 119 GGYAEYVVVPKTNIV-PIPNEISDEHAATLSI---SYLTAWNIFKK-LQLKKHDTLLVYGATGGLGMAVIQFAKALEIKI 193
Cdd:cd05288   94 LGWQEYAVVDGASGLrKLDPSLGLPLSAYLGVlgmTGLTAYFGLTEiGKPKPGETVVVSAAAGAVGSVVGQIAKLLGARV 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 194 ITSVSDDSKLNFARS-LGSDNVINRKKKEVEVEVEKITGGvGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSG---- 268
Cdd:cd05288  174 VGIAGSDEKCRWLVEeLGFDAAINYKTPDLAEALKEAAPD-GIDVYFDNVGGEILDAALTLLNKGGRIALCGAISQynat 252

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262089307 269 ---NIANFQIRTFysKQIQLLGILIGSKLELL-----ELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:cd05288  253 eppGPKNLGNIIT--KRLTMQGFIVSDYADRFpealaELAKWLAEGKLKYREDVVEGLENAPEAFLGLFTGKNTGKLVV 329
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-280 1.21e-19

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 87.81  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLKYEKDFPKPVPNssESLIKIKYCGLNHLDIwtrTGIAGKPISFPHicGSDIVGSLESEANKHS-- 78
Cdd:cd08270    1 MRALVVDPDAPLRLRLGEVPDPQPAPH--EALVRVAAISLNRGEL---KFAAERPDGAVP--GWDAAGVVERAAADGSgp 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  79 -KGTRVLvypgiscnhcnycrTGNETicrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNI 157
Cdd:cd08270   74 aVGARVV--------------GLGAM---------------GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRA 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 158 FKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVInrkkkeveVEVEKITGGvGVDA 237
Cdd:cd08270  125 LRRGGPLLGRRVLVTGASGGVGRFAVQLAALAGAHVVAVVGSPARAEGLRELGAAEVV--------VGGSELSGA-PVDL 195

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 262089307 238 VVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYS 280
Cdd:cd08270  196 VVDSVGGPQLARALELLAPGGTVVSVGSSSGEPAVFNPAAFVG 238
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 11-338 3.42e-19

Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 87.11  E-value: 3.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  11 PIEVLKYEKDFPKPvpnsSESLIKIKYCGLNHLDIWTRTGiaGKPISFPHICG---SDIVGSLESEANKHSKGTRVLVYP 87
Cdd:cd05279   12 PLSIEEIEVAPPKA----GEVRIKVVATGVCHTDLHVIDG--KLPTPLPVILGhegAGIVESIGPGVTTLKPGDKVIPLF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  88 GISCNHCNYCRTGNETICRDFSIIG---------------GLSNYN----GGYAEYVVVPKTNIVPIPNEISDEHAATLS 148
Cdd:cd05279   86 GPQCGKCKQCLNPRPNLCSKSRGTNgrglmsdgtsrftckGKPIHHflgtSTFAEYTVVSEISLAKIDPDAPLEKVCLIG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 149 ISYLTAWN-IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVIN--RKKKEVEV 224
Cdd:cd05279  166 CGFSTGYGaAVNTAKVTPGSTCAVFGL-GGVGLSVIMGCKAAGASRIIAVDiNKDKFEKAKQLGATECINprDQDKPIVE 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 225 EVEKITGGvGVDAVVDNAGQ-KTFTTSINCVR-KGGKIALCGTT-SGNIANFQIRTFYSKQiQLLGILIGSK------LE 295
Cdd:cd05279  245 VLTEMTDG-GVDYAFEVIGSaDTLKQALDATRlGGGTSVVVGVPpSGTEATLDPNDLLTGR-TIKGTVFGGWkskdsvPK 322

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 262089307 296 LLELmkFVSKKNIL-PKVDSIYTLAEIHKAHTLLERGQQLGKIL 338
Cdd:cd05279  323 LVAL--YRQKKFPLdELITHVLPFEEINDGFDLMRSGESIRTIL 364
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 1-332 1.03e-18

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 85.89  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG---------PIEVLKYEKDFPKPvpnsSESLIKIKYCGLNHLDIWTRTGIAGKPIsfPHICGSDIVGSLE 71
Cdd:cd08281    1 MRAAVLRETGaptpyadsrPLVIEEVELDPPGP----GEVLVKIAAAGLCHSDLSVINGDRPRPL--PMALGHEAAGVVV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  72 S--------EANKHSkgtrVLVY-PgiSCNHCNYCRTGNETIC----------------RDFSIIGGLSNYNGG---YAE 123
Cdd:cd08281   75 EvgegvtdlEVGDHV----VLVFvP--SCGHCRPCAEGRPALCepgaaangagtllsggRRLRLRGGEINHHLGvsaFAE 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 124 YVVVPKTNIVPIPNEISDEHAATLSISYLT-AWNIFKKLQLKKHDTLLVYGaTGGLGMAVIQFAKALEIKIITSVS-DDS 201
Cdd:cd08281  149 YAVVSRRSVVKIDKDVPLEIAALFGCAVLTgVGAVVNTAGVRPGQSVAVVG-LGGVGLSALLGAVAAGASQVVAVDlNED 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 202 KLNFARSLGSDNVINRKKKEVEVEVEKITGGvGVDAVVDNAGQ-KTFTTSINCVRKGGKIALCGTTSGNiANFQIR--TF 278
Cdd:cd08281  228 KLALARELGATATVNAGDPNAVEQVRELTGG-GVDYAFEMAGSvPALETAYEITRRGGTTVTAGLPDPE-ARLSVPalSL 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 279 YSKQIQLLGILIGSKLELLELMKFVS--KKNILPkVDSIYT----LAEIHKAHTLLERGQ 332
Cdd:cd08281  306 VAEERTLKGSYMGSCVPRRDIPRYLAlyLSGRLP-VDKLLThrlpLDEINEGFDRLAAGE 364
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 20-268 2.25e-18

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 84.62  E-value: 2.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  20 DFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVG---SLESEANKHSKGTRVlVYPGiscnhcny 96
Cdd:cd08250   22 DVPVPLPGPGEVLVKNRFVGINASDINFTAGRYDPGVKPPFDCGFEGVGevvAVGEGVTDFKVGDAV-ATMS-------- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  97 crtgneticrdfsiigglsnyNGGYAEYVVVPKTNIVPIPnEISDEhAATLSISYLTAWNIFKKL-QLKKHDTLLVYGAT 175
Cdd:cd08250   93 ---------------------FGAFAEYQVVPARHAVPVP-ELKPE-VLPLLVSGLTASIALEEVgEMKSGETVLVTAAA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 176 GGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEvevevekiTGGV-------GVDAVVDNAGQKTFT 248
Cdd:cd08250  150 GGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKSLGCDRPINYKTED--------LGEVlkkeypkGVDVVYESVGGEMFD 221

                        250       260
                 ....*....|....*....|
gi 262089307 249 TSINCVRKGGKIALCGTTSG 268
Cdd:cd08250  222 TCVDNLALKGRLIVIGFISG 241
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 20-287 4.35e-18

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 83.82  E-value: 4.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  20 DFPKPVPNSSESLIKIKY---CGlNHLDIWTRTGIAGKPISFPHICGSDIVG---SLESEANKHSKGTRVLVYPGISCNH 93
Cdd:cd08232   13 ERPAPEPGPGEVRVRVAAggiCG-SDLHYYQHGGFGTVRLREPMVLGHEVSGvveAVGPGVTGLAPGQRVAVNPSRPCGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  94 CNYCRTGNETICRDFSIIGGLSNY---NGGYAEYVVVPKTNIVPIPNEISDEHAA---TLSISyLTAWNIFKKLQLKkhd 167
Cdd:cd08232   92 CDYCRAGRPNLCLNMRFLGSAMRFphvQGGFREYLVVDASQCVPLPDGLSLRRAAlaePLAVA-LHAVNRAGDLAGK--- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 168 TLLVYGA--TGGLGMAVIQFAKALEIkIITSVSdDSKLNFARSLGSDNVINrkkkEVEVEVEKITGGVG-VDAVVDNAG- 243
Cdd:cd08232  168 RVLVTGAgpIGALVVAAARRAGAAEI-VATDLA-DAPLAVARAMGADETVN----LARDPLAAYAADKGdFDVVFEASGa 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 262089307 244 QKTFTTSINCVRKGGKIALCGTTsGNIANFQIRTFYSKQIQLLG 287
Cdd:cd08232  242 PAALASALRVVRPGGTVVQVGML-GGPVPLPLNALVAKELDLRG 284
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1-261 6.87e-18

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 83.44  E-value: 6.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVLkyEKdfPKPVPNSSESLIKI---KYCGLnhlDIWTrtgIAGKPISFPH--ICGSDIVGSLE---S 72
Cdd:cd08285    1 MKAFAMLGIGKVGWI--EK--PIPVCGPNDAIVRPtavAPCTS---DVHT---VWGGAPGERHgmILGHEAVGVVEevgS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  73 EANKHSKGTRVLVYPGISCNHCNYCRTGNETICRdfsiiGGLSNY------NGGYAEYVVVPKT--NIVPIPNEISDEHA 144
Cdd:cd08285   71 EVKDFKPGDRVIVPAITPDWRSVAAQRGYPSQSG-----GMLGGWkfsnfkDGVFAEYFHVNDAdaNLAPLPDGLTDEQA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 145 ATLSISYLTAWNIFKKLQLKKHDTLLVYGAtGGLG-MAVIQfAKALEIKIITSV-SDDSKLNFARSLGSDNVINRKKKEV 222
Cdd:cd08285  146 VMLPDMMSTGFHGAELANIKLGDTVAVFGI-GPVGlMAVAG-ARLRGAGRIIAVgSRPNRVELAKEYGATDIVDYKNGDV 223

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 262089307 223 EVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIA 261
Cdd:cd08285  224 VEQILKLTGGKGVDAVIIAGGgQDTFEQALKVLKPGGTIS 263
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 32-288 1.42e-17

putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of pfam00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 82.22  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   32 LIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGS-LESEANKHSKGTRVLVypgiscnhcnycrTGneticrdfsi 110
Cdd:TIGR02823  30 LIKVAYSSLNYKDALAITGKGGVVRSYPMIPGIDAAGTvVSSEDPRFREGDEVIV-------------TG---------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  111 iGGLS-NYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQ----LKKHDTLLVYGATGGLGMAVIQF 185
Cdd:TIGR02823  87 -YGLGvSHDGGYSQYARVPADWLVPLPEGLSLREAMALGTAGFTAALSVMALErnglTPEDGPVLVTGATGGVGSLAVAI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  186 AKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVE--VEKITGGvgvdaVVDNAGQKTFTTSINCVRKGGKIALC 263
Cdd:TIGR02823 166 LSKLGYEVVASTGKAEEEDYLKELGASEVIDREDLSPPGKplEKERWAG-----AVDTVGGHTLANVLAQLKYGGAVAAC 240

                         250       260
                  ....*....|....*....|....*
gi 262089307  264 GTTSGNIANFQIRTFYSKQIQLLGI 288
Cdd:TIGR02823 241 GLAGGPDLPTTVLPFILRGVSLLGI 265
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 51-264 7.03e-17

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 80.59  E-value: 7.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  51 IAGKPISFPHICGSdIVGSLESEANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGGlSNYNGGYAEYVVVPKT 130
Cdd:PLN02702  70 VVKEPMVIGHECAG-IIEEVGSEVKHLVVGDRVALEPGISCWRCNLCKEGRYNLCPEMKFFAT-PPVHGSLANQVVHPAD 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 131 NIVPIPNEISDEHAAT---LSISYLTAwnifKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEI-KIITSVSDDSKLNFA 206
Cdd:PLN02702 148 LCFKLPENVSLEEGAMcepLSVGVHAC----RRANIGPETNVLVMGA-GPIGLVTMLAARAFGApRIVIVDVDDERLSVA 222

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 262089307 207 RSLGSDNVI----NRKKKEVEVEVEKITGGVGVDAVVDNAG-QKTFTTSINCVRKGGKIALCG 264
Cdd:PLN02702 223 KQLGADEIVlvstNIEDVESEVEEIQKAMGGGIDVSFDCVGfNKTMSTALEATRAGGKVCLVG 285
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-216 2.15e-16

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 79.11  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGPIEVlkyeKDFPKP-VPNSSESLIKIKYCGLNHLDI--WTRTGIAGKPISFPHICgSDIVGSLESEANKH 77
Cdd:PRK10309   1 MKSVVNDTDGIVRV----AESPIPeIKHQDDVLVKVASSGLCGSDIprIFKNGAHYYPITLGHEF-SGYVEAVGSGVDDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  78 SKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSiSYLTAWNI 157
Cdd:PRK10309  76 HPGDAVACVPLLPCFTCPECLRGFYSLCAKYDFIG--SRRDGGNAEYIVVKRKNLFALPTDMPIEDGAFIE-PITVGLHA 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 158 FKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVSDDS-KLNFARSLGSDNVIN 216
Cdd:PRK10309 153 FHLAQGCEGKNVIIIGA-GTIGLLAIQCAVALGAKSVTAIDINSeKLALAKSLGAMQTFN 211
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 6-287 2.44e-15

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 76.01  E-value: 2.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   6 IYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDI-WTRTGIAGKPI-----SFPHICGSDIVGSLE---SEANK 76
Cdd:cd08265   33 VWRYPELRV----EDVPVPNLKPDEILIRVKACGICGSDIhLYETDKDGYILypgltEFPVVIGHEFSGVVEktgKNVKN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  77 HSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIGglSNYNGGYAEYVVVPK------TNIVPIPNEISDEHAATLSIS 150
Cdd:cd08265  109 FEKGDPVTAEEMMWCGMCRACRSGSPNHCKNLKELG--FSADGAFAEYIAVNAryaweiNELREIYSEDKAFEAGALVEP 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 151 YLTAWN--IFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKAL-EIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVE 227
Cdd:cd08265  187 TSVAYNglFIRGGGFRPGAYVVVYGA-GPIGLAAIALAKAAgASKVIAFEISEERRNLAKEMGADYVFNPTKMRDCLSGE 265

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 262089307 228 KI---TGGVGVDAVVDNAG--QKTFTTSINCVRKGGKIALCGTTSGNIAnFQIRTFYSKQIQLLG 287
Cdd:cd08265  266 KVmevTKGWGADIQVEAAGapPATIPQMEKSIAINGKIVYIGRAATTVP-LHLEVLQVRRAQIVG 329
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 118-264 3.09e-15

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 74.61  E-value: 3.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 118 NGGYAEYVVVPKTNIVPIPNEISDEHAAtLSISYLTAWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSV 197
Cdd:cd08255   51 FGPHAERVVVPANLLVPLPDGLPPERAA-LTALAATALNGVRDAEPRLGERVAVVGL-GLVGLLAAQLAKAAGAREVVGV 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 262089307 198 S-DDSKLNFARSLGSDNVINRKKKEVevevekiTGGVGVDAVVDNAGQKT-FTTSINCVRKGGKIALCG 264
Cdd:cd08255  129 DpDAARRELAEALGPADPVAADTADE-------IGGRGADVVIEASGSPSaLETALRLLRDRGRVVLVG 190
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 19-331 6.92e-15

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 74.32  E-value: 6.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  19 KDFPKPVPNSSESLIKIKYCGL--NHLDIWTRtgiaGKPISF----PHICGSDIVGSLESEANKHSK---GTRVLVYPGi 89
Cdd:cd08269   10 EEHPRPTPGPGQVLVRVEGCGVcgSDLPAFNQ----GRPWFVypaePGGPGHEGWGRVVALGPGVRGlavGDRVAGLSG- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  90 scnhcnycrtgneticrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISylTAWNIFKKLQLKKHDTL 169
Cdd:cd08269   85 -----------------------------GAFAEYDLADADHAVPLPSLLDGQAFPGEPLG--CALNVFRRGWIRAGKTV 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 170 LVYGAtGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGVDAVVDNAG-QKTF 247
Cdd:cd08269  134 AVIGA-GFIGLLFLQLAAAAGARRVIAIDrRPARLALARELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGhQWPL 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 248 TTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGILIGSKLELLELM----KFVSKKNILPK--VDSIYTLAEI 321
Cdd:cd08269  213 DLAGELVAERGRLVIFGYHQDGPRPVPFQTWNWKGIDLINAVERDPRIGLEGMreavKLIADGRLDLGslLTHEFPLEEL 292

                        330
                 ....*....|
gi 262089307 322 HKAHTLLERG 331
Cdd:cd08269  293 GDAFEAARRR 302
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 1-215 1.53e-14

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 73.50  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVpIYKHGPIEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDI-WTRTGIA-------------GKPISFPH-ICGsD 65
Cdd:cd08262    1 MRAA-VFRDGPLVV----RDVPDPEPGPGQVLVKVLACGICGSDLhATAHPEAmvddaggpslmdlGADIVLGHeFCG-E 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  66 IVGSLESEANKHSKGTRVLVYPGISCNHCNYCRTG--NETIcrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEH 143
Cdd:cd08262   75 VVDYGPGTERKLKVGTRVTSLPLLLCGQGASCGIGlsPEAP--------------GGYAEYMLLSEALLLRVPDGLSMED 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 262089307 144 AAtlsisyLT-----AWNIFKKLQLKKHDTLLVYGAtGGLGMAVIQFAKALEIK-IITSVSDDSKLNFARSLGSDNVI 215
Cdd:cd08262  141 AA------LTeplavGLHAVRRARLTPGEVALVIGC-GPIGLAVIAALKARGVGpIVASDFSPERRALALAMGADIVV 211
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 1-216 1.89e-14

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 73.02  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHG-PIEVLKYE-KDFPKPVPNSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGS----DIVGSLESEA 74
Cdd:cd08291    1 MKALLLEEYGkPLEVKELSlPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKALPVPPGFegsgTVVAAGGGPL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  75 NKHSKGTRVLVYPGIScnhcnycrtgneticrdfsiigglsnynGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTA 154
Cdd:cd08291   81 AQSLIGKRVAFLAGSY----------------------------GTYAEYAVADAQQCLPLPDGVSFEQGASSFVNPLTA 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 262089307 155 WNIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVIN 216
Cdd:cd08291  133 LGMLETAREEGAKAVVHTAAASALGRMLVRLCKADGIKVINIVRRKEQVDLLKKIGAEYVLN 194
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 26-278 3.93e-14

Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 72.37  E-value: 3.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  26 PNSSESLIKIKYCGLNHLDIWTRTGiaGKPISFPHICGSDIVGSLES--EANKHSKGTRVLVYPGIS-CNHCNYCRTGNE 102
Cdd:cd08277   25 PKANEVRIKMLATSVCHTDILAIEG--FKATLFPVILGHEGAGIVESvgEGVTNLKPGDKVIPLFIGqCGECSNCRSGKT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 103 TICRD---------------FSIIGG-LSNYNG--GYAEYVVVPKTNIVPIPNEISDEHAATLSISYLT----AWNIFKk 160
Cdd:cd08277  103 NLCQKyranesglmpdgtsrFTCKGKkIYHFLGtsTFSQYTVVDENYVAKIDPAAPLEHVCLLGCGFSTgygaAWNTAK- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 161 lqLKKHDTLLVYGaTGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVIN--RKKKEVEVEVEKITGGvGVDA 237
Cdd:cd08277  182 --VEPGSTVAVFG-LGAVGLSAIMGAKIAGASRIIGVDiNEDKFEKAKEFGATDFINpkDSDKPVSEVIREMTGG-GVDY 257

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 262089307 238 VVDNAGQ-KTFTTSINCVRKG-GKIALCGTTSGniANFQIRTF 278
Cdd:cd08277  258 SFECTGNaDLMNEALESTKLGwGVSVVVGVPPG--AELSIRPF 298
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
209-339 1.25e-13

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 66.97  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  209 LGSDNVINrkkkEVEVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQIRTFYSKQIQLLGI 288
Cdd:pfam13602   1 LGADEVID----YRTTDFVQATGGEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGGPPLSAGLLLPARKRGGRGVKYLF 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 262089307  289 LI----GSKLELLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILI 339
Cdd:pfam13602  77 LFvrpnLGADILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 47-216 2.08e-13

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 70.10  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  47 TRTGIAGKPISF-------------PHICGSDIVGSL-ESEANKHSKGTRVLVYPGISCNHCNYCRTGNETICRDFSIIG 112
Cdd:PRK09880  35 TRGGICGSDLHYyqegkvgnfvikaPMVLGHEVIGKIvHSDSSGLKEGQTVAINPSKPCGHCKYCLSHNENQCTTMRFFG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 113 G---LSNYNGGYAEYVVVPKTNIVPIPNEISDE---HAATLSISyLTAWNIFKKLQLKKhdtLLVYGAtGGLGMAVIQFA 186
Cdd:PRK09880 115 SamyFPHVDGGFTRYKVVDTAQCIPYPEKADEKvmaFAEPLAVA-IHAAHQAGDLQGKR---VFVSGV-GPIGCLIVAAV 189

                        170       180       190
                 ....*....|....*....|....*....|...
gi 262089307 187 KAL---EIkIITSVSDDSkLNFARSLGSDNVIN 216
Cdd:PRK09880 190 KTLgaaEI-VCADVSPRS-LSLAREMGADKLVN 220
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 8-341 1.45e-12

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 67.68  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   8 KHGPIEVLKYEKDFPKPVPnSSESLIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSD----IVGSLESEANKHSKGTRV 83
Cdd:cd08247    9 NTSPLTITTIKLPLPNCYK-DNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKGLGRDysgvIVKVGSNVASEWKVGDEV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  84 L-VYPGIScnhcnycrtgneticrdfsiigglsNYNGGYAEYVVV-PKTN---IVPIPNEISDEHAATLSISYLTAWNIF 158
Cdd:cd08247   88 CgIYPHPY-------------------------GGQGTLSQYLLVdPKKDkksITRKPENISLEEAAAWPLVLGTAYQIL 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 159 KKLQ--LKKHDTLLVYGATGGLGMAVIQFAK-ALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGVGV 235
Cdd:cd08247  143 EDLGqkLGPDSKVLVLGGSTSVGRFAIQLAKnHYNIGTVVGTCSSRSAELNKKLGADHFIDYDAHSGVKLLKPVLENVKG 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 236 ----DAVVDNAGQKTFTTSIN-CVRKGGKIALCGTTSG-NIANF------QIRTFYSKQIQLLGILIGS----KLELLEL 299
Cdd:cd08247  223 qgkfDLILDCVGGYDLFPHINsILKPKSKNGHYVTIVGdYKANYkkdtfnSWDNPSANARKLFGSLGLWsynyQFFLLDP 302

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 262089307 300 MK--------FVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIKI 341
Cdd:cd08247  303 NAdwiekcaeLIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVIKV 352
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
 32-268 1.90e-12

Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 67.18  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  32 LIKIKYCGLNHLDIWTRTGIAGKPISFPHICGSDIVGS-LESEANKHSKGTRVLVypgiscnhcnycrTGneticrdfsi 110
Cdd:cd08288   31 TVEVHYSTLNYKDGLAITGKGGIVRTFPLVPGIDLAGTvVESSSPRFKPGDRVVL-------------TG---------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 111 iGGLS-NYNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAwnIFKKLQLKKHDT------LLVYGATGGLGMAVI 183
Cdd:cd08288   88 -WGVGeRHWGGYAQRARVKADWLVPLPEGLSARQAMAIGTAGFTA--MLCVMALEDHGVtpgdgpVLVTGAAGGVGSVAV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 184 QFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKevevevekitGGVG-------VDAVVDNAGQKTFTTSINCVRK 256
Cdd:cd08288  165 ALLARLGYEVVASTGRPEEADYLRSLGASEIIDRAEL----------SEPGrplqkerWAGAVDTVGGHTLANVLAQTRY 234

                        250
                 ....*....|..
gi 262089307 257 GGKIALCGTTSG 268
Cdd:cd08288  235 GGAVAACGLAGG 246
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
 118-268 2.92e-11

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 63.54  E-value: 2.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 118 NGGYAEYVVVPKTNIVPIPNEISDEHAA--TLSISYLTAW-NIFKKLQLKKHDTLLVYGATGGLGMAVIQFAKALEIKII 194
Cdd:COG2130   96 MLGWQDYAVSDGAGLRKVDPSLAPLSAYlgVLGMPGLTAYfGLLDIGKPKAGETVVVSAAAGAVGSVVGQIAKLKGCRVV 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 195 TSVSDDSKLNFARS-LGSDNVINRKkkevevevekiTGGV----------GVDAVVDNAGQKTFTTSINCVRKGGKIALC 263
Cdd:COG2130  176 GIAGGAEKCRYLVEeLGFDAAIDYK-----------AGDLaaalaaacpdGIDVYFDNVGGEILDAVLPLLNTFARIAVC 244


                 ....*
gi 262089307 264 GTTSG 268
Cdd:COG2130  245 GAISQ 249
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
 120-341 2.05e-10

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 61.18  E-value: 2.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 120 GYAEYVVVPKTNI--------VPIPNeisdeHAATLSISYLTAWNIFKKL-QLKKHDTLLVYGATGGLGMAVIQFAKALE 190
Cdd:cd08295  102 GWEEYSLIPRGQDlrkidhtdVPLSY-----YLGLLGMPGLTAYAGFYEVcKPKKGETVFVSAASGAVGQLVGQLAKLKG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 191 IKIITSVSDDSKLNFARS-LGSDNVINRKKKEVEVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTS-- 267
Cdd:cd08295  177 CYVVGSAGSDEKVDLLKNkLGFDDAFNYKEEPDLDAALKRYFPNGIDIYFDNVGGKMLDAVLLNMNLHGRIAACGMISqy 256

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 268 ------GNIANFQIrtfYSKQIQLLGILIGSKLELL-----ELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGK 336
Cdd:cd08295  257 nlewpeGVRNLLNI---IYKRVKIQGFLVGDYLHRYpefleEMSGYIKEGKLKYVEDIADGLESAPEAFVGLFTGSNIGK 333


                 ....*
gi 262089307 337 ILIKI 341
Cdd:cd08295  334 QVVKV 338
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 33-212 3.63e-10

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 60.66  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  33 IKIKYCGLNHLDIWTRTGIAGKPiSFPHICGSDIVG---SLESEANKHSKGTRVLVypGI---SCNHCNYCRTGNETICR 106
Cdd:PLN02586  42 VKILYCGVCHSDLHTIKNEWGFT-RYPIVPGHEIVGivtKLGKNVKKFKEGDRVGV--GVivgSCKSCESCDQDLENYCP 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 107 DFSII------GGLSNYnGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQLKKHDTLLVYGATGGLGM 180
Cdd:PLN02586 119 KMIFTynsighDGTKNY-GGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYYGMTEPGKHLGVAGLGGLGH 197

                        170       180       190
                 ....*....|....*....|....*....|...
gi 262089307 181 AVIQFAKALEIKI-ITSVSDDSKLNFARSLGSD 212
Cdd:PLN02586 198 VAVKIGKAFGLKVtVISSSSNKEDEAINRLGAD 230
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
 164-268 3.80e-10

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 60.35  E-value: 3.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 164 KKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEVEVEVEKITGGvGVDAVVDNAG 243
Cdd:cd08294  142 KAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAGSDDKVAWLKELGFDAVFNYKTVSLEEALKEAAPD-GIDCYFDNVG 220

                         90       100
                 ....*....|....*....|....*
gi 262089307 244 QKTFTTSINCVRKGGKIALCGTTSG 268
Cdd:cd08294  221 GEFSSTVLSHMNDFGRVAVCGSIST 245
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 32-212 4.92e-09

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 57.11  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  32 LIKIKYCGLNHLDIWTRTGIAGKPiSFPHICGSDIVGS---LESEANKHSKGTRVLVypGI---SCNHCNYCRTGNETIC 105
Cdd:PLN02514  38 VIKVIYCGICHTDLHQIKNDLGMS-NYPMVPGHEVVGEvveVGSDVSKFTVGDIVGV--GVivgCCGECSPCKSDLEQYC 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 106 --RDFSiigglsnYN----------GGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQLKKHDTLLVYG 173
Cdd:PLN02514 115 nkRIWS-------YNdvytdgkptqGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLSHFGLKQSGLRGGIL 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 262089307 174 ATGGLGMAVIQFAKAL--EIKIITSvSDDSKLNFARSLGSD 212
Cdd:PLN02514 188 GLGGVGHMGVKIAKAMghHVTVISS-SDKKREEALEHLGAD 227
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
 146-340 1.36e-08

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 55.39  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  146 TLSISYLTAWniFKKLQL---KKHDTLLVYGATGGLGMAVIQFAKALEIKIITSVSDDSKLNFARSLGSDNVINRKKKEV 222
Cdd:TIGR02825 118 TVGMPGLTAY--FGLLEIcgvKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAYLKKLGFDVAFNYKTVKS 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  223 EVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGKIALCGTTSGNIANFQI------RTFYSKQIQLLGILIG----- 291
Cdd:TIGR02825 196 LEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTGPLppgpppEIVIYQELRMEGFIVNrwqge 275

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 262089307  292 -SKLELLELMKFVSKKNILPKVDSIYTLAEIHKAHTLLERGQQLGKILIK 340
Cdd:TIGR02825 276 vRQKALKELLKWVLEGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIVK 325
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 26-216 4.17e-08

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 54.16  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  26 PNSSESLIKIKYCGLNHLDIWTRTGIAGKPIsFPHICGSDIVGSLES---EANKHSKGTRVLVYPGISCNHCNYCRTGNE 102
Cdd:cd08300   25 PKAGEVRIKILATGVCHTDAYTLSGADPEGL-FPVILGHEGAGIVESvgeGVTSVKPGDHVIPLYTPECGECKFCKSGKT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 103 TIC---RD-------------FSIIGG-LSNYNG--GYAEYVVVPKTNIVPIPNEISDEHAATL----SISYLTAWNIFK 159
Cdd:cd08300  104 NLCqkiRAtqgkglmpdgtsrFSCKGKpIYHFMGtsTFSEYTVVAEISVAKINPEAPLDKVCLLgcgvTTGYGAVLNTAK 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 262089307 160 klqLKKHDTLLVYGAtGGLGMAVIQFAKALEIKIITSVS-DDSKLNFARSLGSDNVIN 216
Cdd:cd08300  184 ---VEPGSTVAVFGL-GAVGLAVIQGAKAAGASRIIGIDiNPDKFELAKKFGATDCVN 237
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 61-264 5.77e-07

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 50.67  E-value: 5.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  61 ICGSD-------------------IVGSLE---SEANKHSKGTRVLVYPGISCNHCNYCRTGNETIC------RDFSIIG 112
Cdd:cd08282   37 ICGSDlhmyrgrtgaepglvlgheAMGEVEevgSAVESLKVGDRVVVPFNVACGRCRNCKRGLTGVCltvnpgRAGGAYG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 113 --GLSNYNGGYAEYVVVP--KTNIVPIPNEISDEHA---ATLSISYLTAWNIFKKLQLKKHDTLLVYGAtGGLGM----- 180
Cdd:cd08282  117 yvDMGPYGGGQAEYLRVPyaDFNLLKLPDRDGAKEKddyLMLSDIFPTGWHGLELAGVQPGDTVAVFGA-GPVGLmaays 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 181 AVIQFAKaleiKIITSVSDDSKLNFARSLGSDnVINRKKKEVEVEVEKITGGvGVDAVVDNAGQKTFTTS---------- 250
Cdd:cd08282  196 AILRGAS----RVYVVDHVPERLDLAESIGAI-PIDFSDGDPVEQILGLEPG-GVDRAVDCVGYEARDRGgeaqpnlvln 269

                        250
                 ....*....|....*.
gi 262089307 251 --INCVRKGGKIALCG 264
Cdd:cd08282  270 qlIRVTRPGGGIGIVG 285
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 33-341 5.90e-07

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 50.79  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307  33 IKIKYCGLNHLDIWTRTGIAGKPiSFPHICGSDIVG---SLESEANKHSKGTRVLVYPGI-SCNHCNYCRTGNETICRDF 108
Cdd:PLN02178  36 VKILFCGVCHSDLHTIKNHWGFS-RYPIIPGHEIVGiatKVGKNVTKFKEGDRVGVGVIIgSCQSCESCNQDLENYCPKV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 109 SII------GGLSNyNGGYAEYVVVPKTNIVPIPNEISDEHAATLSISYLTAWNIFKKLQLKKHD-TLLVYGATGGLGMA 181
Cdd:PLN02178 115 VFTynsrssDGTRN-QGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYYGMTKESgKRLGVNGLGGLGHI 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 182 VIQFAKALEIKI-ITSVSDDSKLNFARSLGSDNVInrkkkeVEVEVEKITGGVG-VDAVVDN-AGQKTFTTSINCVRKGG 258
Cdd:PLN02178 194 AVKIGKAFGLRVtVISRSSEKEREAIDRLGADSFL------VTTDSQKMKEAVGtMDFIIDTvSAEHALLPLFSLLKVSG 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 259 KIALCGTTSGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSKKNILPKVDSIyTLAEIHKAHTLLERGQQLGKIL 338
Cdd:PLN02178 268 KLVALGLPEKPL-DLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELI-KMSDINSAMDRLAKSDVRYRFV 345


                 ...
gi 262089307 339 IKI 341
Cdd:PLN02178 346 IDV 348
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
 110-296 2.27e-05

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 45.60  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 110 IIGGLSnyngGYAEYVVVPKTNIVPIPNEISDE-----HAATLSISYLTAWNIFKKL-QLKKHDTLLVYGATGGLGMAVI 183
Cdd:PLN03154 101 LISGIT----GWEEYSLIRSSDNQLRKIQLQDDiplsyHLGLLGMAGFTAYAGFYEVcSPKKGDSVFVSAASGAVGQLVG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 184 QFAKALEIKIITSVSDDSKLNFARS-LGSDNVINRKKKEVEVEVEKITGGVGVDAVVDNAGQKTFTTSINCVRKGGKIAL 262
Cdd:PLN03154 177 QLAKLHGCYVVGSAGSSQKVDLLKNkLGFDEAFNYKEEPDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAV 256

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 262089307 263 CGTTSGN-IANFQ-IRTFYS---KQIQLLGILIGSKLEL 296
Cdd:PLN03154 257 CGMVSLNsLSASQgIHNLYNlisKRIRMQGFLQSDYLHL 295
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 115-324 5.77e-05

ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of the MDR/zinc-dependent alcohol dehydrogenase-like family, oxidizes the phosphate ester of ribitol-5-phosphate to xylulose-5-phosphate of the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176199 [Multi-domain]  Cd Length: 341  Bit Score: 44.28  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 115 SNYNGGYAEYVVVPKTNIVPIPNEISDEHAA---TLSISYlTAWNIFKKLQLKKHDTLLVYGaTGGLG--MAVIQFAKAL 189
Cdd:cd08237  111 SGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAfteLVSVGV-HAISRFEQIAHKDRNVIGVWG-DGNLGyiTALLLKQIYP 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307 190 EIKIITSVSDDSKLN---FARSlgSDNVINRKKKEVEVEVEKITGGVGVDAVVDNAgqktfttsINCVRKGGKIALCGTT 266
Cdd:cd08237  189 ESKLVVFGKHQEKLDlfsFADE--TYLIDDIPEDLAVDHAFECVGGRGSQSAINQI--------IDYIRPQGTIGLMGVS 258

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 262089307 267 SGNIaNFQIRTFYSKQIQLLGILIGSKLELLELMKFVSK--------KNILPKVDSIYTLAEIHKA 324
Cdd:cd08237  259 EYPV-PINTRMVLEKGLTLVGSSRSTREDFERAVELLSRnpevaeylRKLVGGVFPVRSINDIHRA 323
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 1-141 6.26e-03

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 37.97  E-value: 6.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262089307   1 MKAVPIYKHGP-IEVlkyeKDFPKPVPNSSESLIKIKYCGLNHLDiwtRTGIAGKPISFPH-----ICGSDIVGSLEsEA 74
Cdd:cd08230    1 MKAIAVKPGKPgVRV----VDIPEPEPTPGEVLVRTLEVGVCGTD---REIVAGEYGTAPPgedflVLGHEALGVVE-EV 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 262089307  75 NKH---SKGTrvLVYPGI--SCNHCNYCRTGNETICRDFSI----IGGLsnynGGY-AEYVVVPKTNIVPIPNEISD 141
Cdd:cd08230   73 GDGsglSPGD--LVVPTVrrPPGKCLNCRIGRPDFCETGEYtergIKGL----HGFmREYFVDDPEYLVKVPPSLAD 143
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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