|
Name |
Accession |
Description |
Interval |
E-value |
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
1-381 |
0e+00 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 595.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 1 MQ-FSYVNPTMIHFGQGQIASIRRDIPKD-HKVLVLYGGGSIKRNGVYDQVVEALSE--HQWVEFSGVEPNPTKETLDKA 76
Cdd:COG1979 1 MNnFTFYNPTKIIFGKGQIAKLGEEIPKYgKKVLLVYGGGSIKKNGLYDQVKAALKEagIEVVEFGGVEPNPRLETVRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 77 VHIVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDK 156
Cdd:COG1979 81 VELCKEEGIDFILAVGGGSVIDGAKAIAAGAKYDGDPWDILTGKAPVEKALPLGTVLTLPATGSEMNSGSVITNEETKEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 157 LAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVQEGYAEVLLRNLLALGADFV-NRDNDAW 235
Cdd:COG1979 161 LGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVMEQYFTYPVDAPLQDRFAEGLLRTLIEEGPKALkDPEDYDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 236 RANLMWTANQALNGLIGTGVPQDWATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLPQSDD- 314
Cdd:COG1979 241 RANLMWAATLALNGLIGAGVPQDWATHMIEHELSALYDIDHGAGLAIVLPAWMRYVLEEKPEKFAQYAERVWGITEGDDe 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447083498 315 -LAEKTIAAIEAFYHQLNVATQFGEHGmAKEAAVDAVLQQLTAHGMHKLGEQGTIDLQESRKILENAL 381
Cdd:COG1979 321 eRALEGIEATEEFFESLGLPTRLSEYG-IDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
3-378 |
1.53e-179 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 503.50 E-value: 1.53e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 3 FSYVNPTMIHFGQGQIASIRRDIPK-DHKVLVLYGGGSIKRNGVYDQVVEALSE--HQWVEFSGVEPNPTKETLDKAVHI 79
Cdd:cd08187 2 FTFYNPTKIIFGKGAIEELGEEIKKyGKKVLLVYGGGSIKKNGLYDRVVASLKEagIEVVEFGGVEPNPRLETVREGIEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 80 VKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAF 159
Cdd:cd08187 82 AREENVDFILAVGGGSVIDAAKAIAAGAKYDGDVWDFFTGKAPPEKALPVGTVLTLAATGSEMNGGAVITNEETKEKLGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 160 LSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVQEGYAEVLLRNLLALGADFVNR-DNDAWRAN 238
Cdd:cd08187 162 GSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQYFTGTEDAPLQDRLAEGLLRTVIENGPKALKDpDDYEARAN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 239 LMWTANQALNGLIGTGVPQDWATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLPQSDD---L 315
Cdd:cd08187 242 LMWAATLALNGLLGAGRGGDWATHAIEHELSALYDITHGAGLAIVFPAWMRYVLKKKPERFAQFARRVFGIDPGGDdeeT 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447083498 316 AEKTIAAIEAFYHQLNVATQFGEHGmAKEAAVDAVLQQLTAHGMhKLGEQGTIDLQESRKILE 378
Cdd:cd08187 322 ALEGIEALEEFFKSIGLPTTLSELG-IDEEDIEEMAEKAVRGGG-LGGGFKPLTREDIEEILK 382
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
1-380 |
1.17e-151 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 433.07 E-value: 1.17e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 1 MQ-FSYVNPTMIHFGQGQIASIRRDIPKDHKVLVLYGGGSIKRNGVYDQVVEALSEHQWVEFSGVEPNPTKETLDKAVHI 79
Cdd:PRK15138 1 MNnFNLHTPTRILFGKGAIAGLREQIPADARVLITYGGGSVKKTGVLDQVLDALKGMDVLEFGGIEPNPTYETLMKAVKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 80 VKNQHIDFILAVGGGSVIDGSKYVAAAAFYEG--DGWDIL-TGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDK 156
Cdd:PRK15138 81 VREEKITFLLAVGGGSVLDGTKFIAAAANYPEniDPWHILeTGGKEIKSAIPMGSVLTLPATGSESNAGAVISRKTTGDK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 157 LAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVQEGYAEVLLRNLLALGADFVNR-DNDAW 235
Cdd:PRK15138 161 QAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTVEQYVTYPVDAKIQDRFAEGILLTLIEEGPKALKEpENYDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 236 RANLMWTANQALNGLIGTGVPQDWATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLPQ--SD 313
Cdd:PRK15138 241 RANVMWAATQALNGLIGAGVPQDWATHMLGHELTAMHGLDHAQTLAIVLPALWNEKRDTKRAKLLQYAERVWNITEgsDD 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447083498 314 DLAEKTIAAIEAFYHQLNVATQFGEHGMAKeAAVDAVLQQLTAHGMHKLGEQGTIDLQESRKILENA 380
Cdd:PRK15138 321 ERIDAAIAATRNFFEQMGVPTRLSDYGLDG-SSIPALLKKLEEHGMTQLGEHHDITLDVSRRIYEAA 386
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
8-359 |
1.24e-88 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 271.78 E-value: 1.24e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPK-DHKVLVLYGGGSIKrNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQH 84
Cdd:pfam00465 1 PTRIVFGAGALAELGEELKRlGARALIVTDPGSLK-SGLLDKVLASLEEAgiEVVVFDGVEPEPTLEEVDEAAALAREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 85 IDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSPAV 164
Cdd:pfam00465 80 ADVIIAVGGGSVIDTAKAIALLLTNPGDVWDYLGGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGIFSPKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 165 QPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMvQEGYAE----VLLRNLLALGADfvnRDNDAWRANLM 240
Cdd:pfam00465 160 LPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVSKGANPL-TDALALeairLIAENLPRAVAD---GEDLEARENML 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 241 WTANQALNGLIGTGVPqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLPQsDDLAEKTI 320
Cdd:pfam00465 236 LASTLAGLAFSNAGLG---AAHALAHALGGRYGIPHGLANAILLPYVLRFNAPAAPEKLAQLARALGEDSD-EEAAEEAI 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 447083498 321 AAIEAFYHQLNVATQFGEHGMAKE---AAVDAVLQQLTAHGM 359
Cdd:pfam00465 312 EALRELLRELGLPTTLSELGVTEEdldALAEAALRDRSLANN 353
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
8-345 |
2.61e-60 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 198.83 E-value: 2.61e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDI--PKDHKVLVLYGGGsIKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQ 83
Cdd:cd08551 1 PTRIVFGAGALARLGEELkaLGGKKVLLVTDPG-LVKAGLLDKVLESLKAAgiEVEVFDDVEPNPTVETVEAAAELAREE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 84 HIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSPA 163
Cdd:cd08551 80 GADLVIAVGGGSVLDTAKAIAVLATNGGSIRDYEGIGKVPKPGLPLIAIPTTAGTGSEVTPNAVITDPETGRKMGIVSPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 164 VQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVqEGYA----EVLLRNLLalgADFVNRDNDAWRANL 239
Cdd:cd08551 160 LLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKKANPIS-DALAleaiRLIGKNLR---RAVADGSDLEAREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 240 MWTANQALNGLIGTGVpqdWATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQ----MGKNVFGLPQsDDL 315
Cdd:cd08551 236 LLASLLAGIAFGNAGL---GAVHALAYPLGGRYHIPHGVANAILLPYVMEFNLPACPEKYAEiaeaLGEDVEGLSD-EEA 311
|
330 340 350
....*....|....*....|....*....|
gi 447083498 316 AEKTIAAIEAFYHQLNVATQFGEHGMAKEA 345
Cdd:cd08551 312 AEAAVEAVRELLRDLGIPTSLSELGVTEED 341
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
1-356 |
8.97e-59 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 195.34 E-value: 8.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 1 MQFSYVNPTMIHFGQGQIASIRRDIPK--DHKVLVLyGGGSIKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKA 76
Cdd:COG1454 1 MMFTFRLPTRIVFGAGALAELGEELKRlgAKRALIV-TDPGLAKLGLLDRVLDALEAAgiEVVVFDDVEPNPTVETVEAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 77 VHIVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDK 156
Cdd:COG1454 80 AAAAREFGADVVIALGGGSAIDAAKAIALLATNPGDLEDYLGIKKVPGPPLPLIAIPTTAGTGSEVTPFAVITDPETGVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 157 LAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTL----PTQAMVQEGyAEVLLRNLLALGADfvNRDN 232
Cdd:COG1454 160 KGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSKganpLTDALALEA-IRLIARNLPRAVAD--GDDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 233 DAwRANLMWTANQAlnGL----IGTGvpqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKnVFG 308
Cdd:COG1454 237 EA-REKMALASLLA--GMafanAGLG-----AVHALAHPLGGLFHVPHGLANAILLPHVLRFNAPAAPERYAEIAR-ALG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 447083498 309 LPQS---DDLAEKTIAAIEAFYHQLNVATQFGEHGMAKEA----AVDAVLQQLTA 356
Cdd:COG1454 308 LDVGlsdEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDlpelAELALADRCLA 362
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
5-344 |
1.99e-57 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 191.56 E-value: 1.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 5 YVNPTMIHFGQGQIASIRrDIPKDH--KVLVLYGGGSIKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIV 80
Cdd:cd08185 1 YYQPTRILFGAGKLNELG-EEALRPgkKALIVTGKGSSKKTGLLDRVKKLLEKAgvEVVVFDKVEPNPLTTTVMEGAALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 81 KNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQ----HTVKQATPIGAILTLPATGSESNTGAVITKAETQDK 156
Cdd:cd08185 80 KEEGCDFVIGLGGGSSMDAAKAIAFMATNPGDIWDYIFGGtgkgPPPEKALPIIAIPTTAGTGSEVDPWAVITNPETKEK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 157 LAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVqEGYA----EVLLRNLLALGADfvNRDN 232
Cdd:cd08185 160 KGIGHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISKNANPFS-DMLAleaiRLVAKYLPRAVKD--GSDL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 233 DAwRANLMWTANQA--LNGLIGTGVPqdwatHMIGHELTAL-WHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGK-NVFG 308
Cdd:cd08185 237 EA-REKMAWASTLAgiVIANSGTTLP-----HGLEHPLSGYhPNIPHGAGLAALYPAYFEFTIEKAPEKFAFVARaEASG 310
|
330 340 350
....*....|....*....|....*....|....*.
gi 447083498 309 LPQSDDlAEKTIAAIEAFYHQLNVATQFGEHGMAKE 344
Cdd:cd08185 311 LSDAKA-AEDFIEALRKLLKDIGLDDLLSDLGVTEE 345
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
8-330 |
5.01e-44 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 155.82 E-value: 5.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPKD-HKVLVLYGGGSIKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQH 84
Cdd:cd08181 4 PTKVYFGKNCVEKHADELAALgKKALIVTGKHSAKKNGSLDDVTEALEENgiEYFIFDEVEENPSIETVEKGAELARKEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 85 IDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTvKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSPAV 164
Cdd:cd08181 84 ADFVIGIGGGSPLDAAKAIALLAANKDGDEDLFQNGKY-NPPLPIVAIPTTAGTGSEVTPYSILTDHEKGTKKSFGNPLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 165 QPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYL----TLPTQAMVQEGyaevlLRNLLALGADFVN-RDNDAWRANL 239
Cdd:cd08181 163 FPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLsvkaTPLSDALALEA-----LRLIGECLPNLLGdELDEEDREKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 240 MWTAnqALNGLI----GTGVPqdwatHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKnvfglpqsdDL 315
Cdd:cd08181 238 MYAS--TLAGMViaqtGTTLP-----HGLGYPLTYFKGIPHGRANGILLPAYLKLCEKQEPEKVDKILK---------LL 301
|
330
....*....|....*
gi 447083498 316 AEKTIAAIEAFYHQL 330
Cdd:cd08181 302 GFGSIEEFQKFLNRL 316
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-360 |
1.73e-43 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 154.66 E-value: 1.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 3 FSYVNPTMIHFGQGQIASIRRDI-PKDHKVLVLYGGGSIKRNGVYDQVVEALSEHQWVEFSGVEPNPTKETLDKAVHIVK 81
Cdd:cd08196 1 WSYYQPVKIIFGEGILKELPDIIkELGGKRGLLVTDPSFIKSGLAKRIVESLKGRIVAVFSDVEPNPTVENVDKCARLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 82 NQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTV-KQATPIGAILTLPATGSESNTGAVITKAETQDKLAFL 160
Cdd:cd08196 81 ENGADFVIAIGGGSVLDTAKAAACLAKTDGSIEDYLEGKKKIpKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 161 SPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAmVQEGYAE----VLLRNLLALgadfVNRDNDAW- 235
Cdd:cd08196 161 SPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSINHQP-ISDALALeaakLVLENLEKA----YNNPNDKEa 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 236 RANLMWTANQAlnGLiGTGVPQDWATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVfGLPQSDDL 315
Cdd:cd08196 236 REKMALASLLA--GL-AFSQTRTTASHACSYPLTSHFGIPHGEACALTLPSFIRLNAEALPGRLDELAKQL-GFKDAEEL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 447083498 316 AEKtiaaIEAFYHQLNVATQFGEHGMAKEAavdavLQQLTAHGMH 360
Cdd:cd08196 312 ADK----IEELKKRIGLRTRLSELGITEED-----LEEIVEESFH 347
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-381 |
3.31e-43 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 154.23 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 4 SYVNPTMIHFGQG---QIASIRRDIPKDhKVLVLYGGGsIKRNGVYDQVVEALSE--HQWVEFSGVEPNPTKETLDKAVH 78
Cdd:cd14863 1 TYSQLTPVIFGAGaveQIGELLKELGCK-KVLLVTDKG-LKKAGIVDKIIDLLEEagIEVVVFDDVEPDPPDEIVDEAAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 79 IVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWD-ILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKL 157
Cdd:cd14863 79 IAREEGADGVIGIGGGSVLDTAKAIAVLLTNPGPIIDyALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 158 AFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVqEGYAE----VLLRNL-LAlgadFVNRDN 232
Cdd:cd14863 159 SLLGPFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTSKLANPMT-DALALqairLIVKNLpRA----VKDGDN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 233 DAWRANLMWTANQALNGLIGTGVpqdWATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKnVFGLPQS 312
Cdd:cd14863 234 LEARENMLLASNLAGIAFNNAGT---HIGHAIAHALGALYHIPHGLACALALPVVLEFNAEAYPEKVKKIAK-ALGVSFP 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447083498 313 DD----LAEKTIAAIEAFYHQLNVATQFGEHGMAKE---AAVDAVLQQLTAHGMHKlgeqgTIDLQESRKILENAL 381
Cdd:cd14863 310 GEsdeeLGEAVADAIREFMKELGIPSLFEDYGIDKEdldKIAEAVLKDPFAMFNPR-----PITEEEVAEILEAIY 380
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
8-330 |
6.68e-43 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 150.59 E-value: 6.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRrDIPKDH--KVLVLYGGGSIKrnGVYDQVVEALSEHQ-WVEFSGVEPNPTKETLDKAVHIVKNQH 84
Cdd:cd07766 1 PTRIVFGEGAIAKLG-EIKRRGfdRALVVSDEGVVK--GVGEKVADSLKKGLaVAIFDFVGENPTFEEVKNAVERARAAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 85 IDFILAVGGGSVIDGSKYVAAAAFyegdgwdiltgqhtvkQATPIGAILTLPATGSESNTGAVITKAETQDKlaFLSPAV 164
Cdd:cd07766 78 ADAVIAVGGGSTLDTAKAVAALLN----------------RGIPFIIVPTTASTDSEVSPKSVITDKGGKNK--QVGPHY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 165 QPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEqyltlptqamvqegyaevllrnllalgadfvnrdndawRANLMWTAN 244
Cdd:cd07766 140 NPDVVFVDTDITKGLPPRQVASGGVDALAHAVE--------------------------------------LEKVVEAAT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 245 QALNGLIgtGVPQDWATHMIGHELTALWHVDHARSLAIVQPWLLRNQlKHKKAKLEQMGKNVF------GLPQsdDLAEK 318
Cdd:cd07766 182 LAGMGLF--ESPGLGLAHAIGHALTAFEGIPHGEAVAVGLPYVLKVA-NDMNPEPEAAIEAVFkfledlGLPT--HLADL 256
|
330
....*....|....
gi 447083498 319 TIAA--IEAFYHQL 330
Cdd:cd07766 257 GVSKedIPKLAEKA 270
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-336 |
2.11e-39 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 144.15 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHfGQGQIASIRRDIPKDH--KVLVLYGGGSIKRnGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQ 83
Cdd:cd08189 6 PELFE-GAGSLLQLPEALKKLGikRVLIVTDKGLVKL-GLLDPLLDALKKAgiEYVVFDGVVPDPTIDNVEEGLALYKEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 84 HIDFILAVGGGSVIDGSKYVAAAAfyEGDGWDI--LTGQHTVKQAT-PIGAILTLPATGSESNTGAVITKAETQDKLAFL 160
Cdd:cd08189 84 GCDAIIAIGGGSVIDCAKVIAARA--ANPKKSVrkLKGLLKVRKKLpPLIAVPTTAGTGSEATIAAVITDPETHEKYAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 161 SPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVQEgYAE----VLLRNLLALgadFVNRDNDAWR 236
Cdd:cd08189 162 DPKLIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSATKETDE-YALeavkLIFENLPKA---YEDGSDLEAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 237 ANLMWTANQAlnGL------IGTgvpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVfGLP 310
Cdd:cd08189 238 ENMLLASYYA--GLaftrayVGY-------VHAIAHQLGGLYGVPHGLANAVVLPHVLEFYGPAAEKRLAELADAA-GLG 307
|
330 340 350
....*....|....*....|....*....|
gi 447083498 311 QSDD----LAEKTIAAIEAFYHQLNVATQF 336
Cdd:cd08189 308 DSGEsdseKAEAFIAAIRELNRRMGIPTTL 337
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
8-361 |
2.51e-35 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 133.12 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRR--DIPKDHKVLVLYGGGSIKRNGVYDQVVEALSEHQWVEFSGVEPNPTKETLDKAVHIVKNQHI 85
Cdd:cd08182 1 PVKIIFGPGALAELKDllGGLGARRVLLVTGPSAVRESGAADILDALGGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 86 DFILAVGGGSVIDGSKyvAAAAFYEGDGWDILT----GQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLS 161
Cdd:cd08182 81 DVIIAVGGGSVIDTAK--AIAALLGSPGENLLLlrtgEKAPEENALPLIAIPTTAGTGSEVTPFATIWDEAEGKKYSLAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 162 PAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQY---------LTLPTQAmvqegyAEVLLRNLLALgadFVNRDN 232
Cdd:cd08182 159 PSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIwsvnanpesRAYALRA------IRLILENLPLL---LENLPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 233 DAWRANLMWTANQAlnGL-I---GTGVPqdwatHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNV-- 306
Cdd:cd08182 230 LEAREAMAEASLLA--GLaIsitKTTAA-----HAISYPLTSRYGVPHGHACALTLPAVLRYNAGADDECDDDPRGREil 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 447083498 307 --FGLPQSDDLAEKtiaaIEAFYHQLNVATQFGEHGMAKEAavdavLQQLTAHGMHK 361
Cdd:cd08182 303 laLGASDPAEAAER----LRALLESLGLPTRLSEYGVTAED-----LEALAASVNTP 350
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
7-382 |
2.89e-35 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 133.08 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 7 NPTMIHFGQGQIASIRRdiPKDHKVLVLYGGGSIKRNGVYDQVVEALSEHQW-VE-FSGVEPNPTKETLDKAVHIVKNQH 84
Cdd:cd08179 4 VPRDIYFGEGALEYLKT--LKGKRAFIVTGGGSMKRNGFLDKVEDYLKEAGMeVKvFEGVEPDPSVETVEKGAEAMREFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 85 IDFILAVGGGSVIDGSKyvAAAAFYEGDGW---DILT--GQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAF 159
Cdd:cd08179 82 PDWIIAIGGGSVIDAAK--AMWVFYEYPELtfeDALVpfPLPELRKKARFIAIPSTSGTGSEVTRASVITDTEKGIKYPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 160 LSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQY-LTLP---TQAMVqEGYAEVLLRNLLalgADFVNRDNDAW 235
Cdd:cd08179 160 ASFEITPDVAILDPELTMTMPPHVTANTGMDALTHAIEAYvSTLAndfTDALA-LGAILDIFENLP---KSYNGGKDLEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 236 RANlMWTAnQALNGL----IGTGVpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLpq 311
Cdd:cd08179 236 REK-MHNA-SCLAGMafsnSGLGI-----VHSMAHKGGAFFGIPHGLANAILLPYVIEFNSKDPEARARYAALLIGLT-- 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447083498 312 SDDLAEKTIAAIEAFYHQLNVATQFGEHGMAKEAAVdAVLQQLTAHGMHKLGEQ---GTIDLQESRKILENALY 382
Cdd:cd08179 307 DEELVEDLIEAIEELNKKLGIPLSFKEAGIDEDEFF-AKLDEMAENAMNDACTGtnpRKPTVEEMKELLKAAYY 379
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
40-345 |
3.31e-34 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 130.04 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 40 IKRNGVYDQVVEALSEHQWVE--FSGVEPNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKyvAAAAFYEGDGWDIl 117
Cdd:cd14862 35 LVKLGLLKKVLKRLLQAGFEVevFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAK--AAWVLYERPDLDP- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 118 tgqHTVKQATPIG--------AILTLPATGSESNTGAVITKAETQDKLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLV 189
Cdd:cd14862 112 ---EDISPLDLLGlrkkakliAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEFVLGMPPKLTAGTGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 190 DAWVHVCEQYLT---------LPTQAmvqegyAEVLLRNL-LAlgadFVNRDNDAWRANLMWTANQA----LNGLIGTgv 255
Cdd:cd14862 189 DALAHAVEAYLStwsndfsdaLALKA------IELIFKYLpRA----YKDGDDLEAREKMHNAATIAglafGNSQAGL-- 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 256 pqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMgkNVFGLPQSDD--LAEKTIAAIEAFYHQLNVA 333
Cdd:cd14862 257 -----AHALGHSLGAVFHVPHGIAVGLFLPYVIEFYAKVTDERYDLL--KLLGIEARDEeeALKKLVEAIRELYKEVGQP 329
|
330
....*....|..
gi 447083498 334 TQFGEHGMAKEA 345
Cdd:cd14862 330 LSIKDLGISEEE 341
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
9-326 |
7.93e-33 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 126.23 E-value: 7.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 9 TMIHFGQGQIASIRrDIPKDH---KVLVLYGGGSIKRNGVYDQVVEALSEHQ--WVEFSGVEPNPTKETLDKAVHIVKNQ 83
Cdd:cd08186 2 TTLYFGVGAIAKIK-DILKDLgidKVIIVTGRSSYKKSGAWDDVEKALEENGieYVVYDKVTPNPTVDQADEAAKLARDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 84 HIDFILAVGGGSVIDGSKYVAAAAFYEG-DGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSP 162
Cdd:cd08186 81 GADAVIAIGGGSPIDTAKSVAVLLAYGGkTARDLYGFRFAPERALPLVAINLTHGTGSEVDRFAVATIPEKGYKPGIAYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 163 AVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLptqamVQEGYAEVLLRNLLALGADFV-----NRDNDAWRA 237
Cdd:cd08186 161 CIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTK-----VSSPYVITLAKEAIRLIAEYLpralaNPKDLEARY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 238 NLMWTAnqalngLIGtGVPQDWA----THMIGHELTALW-HVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKN-VFGLPQ 311
Cdd:cd08186 236 WLLYAS------MIA-GIAIDNGllhlTHALEHPLSGLKpELPHGLGLALLGPAVVKYIYKAVPETLADILRPiVPGLKG 308
|
330
....*....|....*
gi 447083498 312 SDDLAEKTIAAIEAF 326
Cdd:cd08186 309 TPDEAEKAARGVEEF 323
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
3-381 |
4.16e-32 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 124.58 E-value: 4.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 3 FSYVNPTMIHFGQGQIASIRRDIPKDH--KVLVLYGGGsIKRNGVYDQVVEALSEHQWVE--FSGVEPNPTKETLDKAVH 78
Cdd:cd14865 1 FEFFNPTKIVSGAGALENLPAELARLGarRPLIVTDKG-LAAAGLLKKVEDALGDAIEIVgvFDDVPPDSSVAVVNEAAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 79 IVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQA-TPIGAILTLPATGSESNTGAVITKAETQDKL 157
Cdd:cd14865 80 RAREAGADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTRPlKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 158 AFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAMvQEGYA----EVLLRNLLALGADfvNRDND 233
Cdd:cd14865 160 LFVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSLQKNPI-SDALAlqaiRLISENLPKAVKN--GKDLE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 234 AwRANLMWTANQA----LNGLIGtgvpqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKN-VFG 308
Cdd:cd14865 237 A-RLALAIAATMAgiafSNSMVG-------LVHAIAHAVGAVAGVPHGLANSILLPHVMRYNLDAAAERYAELALAlAYG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 309 LPQSDDLAEKTIAAIEAFYHQLNVATQFGEHgmAKEAAVDAvlQQLTAHGMHKLGEqGTI-------DLQESRKILENAL 381
Cdd:cd14865 309 VTPAGRRAEEAIEAAIDLVRRLHELCGLPTR--LRDVGVPE--EQLEAIAELALND-GAIlfnprevDPEDILAILEAAY 383
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-344 |
1.30e-31 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 123.00 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPK-DHKVLVLYGGGSIkRNGVYDQVVEALSEH--QWVEFSGVEpNPTKETLDKAVHIVKNQH 84
Cdd:cd08183 1 PPRIVFGRGSLQELGELAAElGKRALLVTGRSSL-RSGRLARLLEALEAAgiEVALFSVSG-EPTVETVDAAVALAREAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 85 IDFILAVGGGSVIDGSKYVAAAAFYEGDGWDIL----TGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFL 160
Cdd:cd08183 79 CDVVIAIGGGSVIDAAKAIAALLTNEGSVLDYLevvgKGRPLTEPPLPFIAIPTTAGTGSEVTKNAVLSSPEHGVKVSLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 161 SPAVQPRFAVLDPDVMKSLPERQLV-NGLvDAWVHVCEQYL----TLPTQAMVQEGyAEVLLRNLLALgadFVNRDNDAW 235
Cdd:cd08183 159 SPSMLPDVALVDPELTLSLPPEVTAaSGL-DALTQLIEPYVsrkaNPLTDALAREG-LRLAARSLRRA---YEDGEDLEA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 236 RANLMWTAnqALNGLI----GTGvpqdwATHMIGHELTALWHVDH----ARSLAIVQPWLL-----RNQLKHKKAKLEQM 302
Cdd:cd08183 234 REDMALAS--LLGGLAlanaGLG-----AVHGLAGPLGGMFGAPHgaicAALLPPVLEANLralreREPDSPALARYREL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 447083498 303 GKNVFGLPqsDDLAEKTIAAIEAFYHQLNVATqFGEHGMAKE 344
Cdd:cd08183 307 AGILTGDP--DAAAEDGVEWLEELCEELGIPR-LSEYGLTEE 345
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
3-350 |
1.89e-31 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 122.66 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 3 FSYVNPTMIHFGQGQIASIRRDIPKDH--KVLVLYGGGSIKrNGVYDQVVEALSEHQ--WVEFSGVEPNPTKETLDKAVH 78
Cdd:cd08176 1 NRFVLNPTSYFGWGAIEEIGEEAKKRGfkKALIVTDKGLVK-FGIVDKVTDVLKEAGiaYTVFDEVKPNPTIENVMAGVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 79 IVKNQHIDFILAVGGGSVIDGSKyvAAAAFYEGDGWDI--LTGQH-TVKQATPIGAILTLPATGSESNTGAVITKAETQD 155
Cdd:cd08176 80 AYKESGADGIIAVGGGSSIDTAK--AIGIIVANPGADVrsLEGVApTKNPAVPIIAVPTTAGTGSEVTINYVITDTEKKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 156 KLAFLSPAVQPRFAVLDPDVMKSLPeRQLV--NGLvDAWVHVCEQYLTLPTQAMvQEGYA----EVLLRNLLALGAdfvN 229
Cdd:cd08176 158 KFVCVDPHDIPTVAIVDPDLMSSMP-KGLTaaTGM-DALTHAIEGYITKGAWEL-SDMLAlkaiELIAKNLRKAVA---N 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 230 RDNDAWRANLMW---TANQALNGlIGTGVpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKnV 306
Cdd:cd08176 232 PNNVEARENMALaqyIAGMAFSN-VGLGI-----VHSMAHPLSAFYDTPHGVANAILLPYVMEFNAPATGEKYRDIAR-A 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 447083498 307 FGLP---QSDDLA-EKTIAAIEAFYHQLNVATQFGEHGMaKEAAVDAV 350
Cdd:cd08176 305 MGVDttgMSDEEAaEAAVDAVKKLSKDVGIPQKLSELGV-KEEDIEAL 351
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
8-350 |
2.13e-31 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 122.24 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPKD--HKVLVLYGGGsIKRNGVYDQVVEALSE--HQWVEFSGVEPNPTKETLDKAVHIVKNQ 83
Cdd:cd14861 3 PTRIRFGAGAIAELPEELKALgiRRPLLVTDPG-LAALGIVDRVLEALGAagLSPAVFSDVPPNPTEADVEAGVAAYREG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 84 HIDFILAVGGGSVIDGSKYVAAAAFYEGDGWD--ILTGQHTVKQAT--PIGAILTLPATGSESNTGAVITKAETQDKLAF 159
Cdd:cd14861 82 GCDGIIALGGGSAIDAAKAIALMATHPGPLWDyeDGEGGPAAITPAvpPLIAIPTTAGTGSEVGRAAVITDDDTGRKKII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 160 LSPAVQPRFAVLDPDVMKSLPERqlvngL-----VDAWVHVCEQYLTLPTQAMVqEGYA-EVLLRNLLALGADFVNRDND 233
Cdd:cd14861 162 FSPKLLPKVAICDPELTLGLPPR-----LtaatgMDALTHCIEAYLSPGFHPMA-DGIAlEGLRLISEWLPRAVADGSDL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 234 AWRANLMwtaNQALNGLI----GTGvpqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNV-FG 308
Cdd:cd14861 236 EARGEMM---MAALMGAVafqkGLG-----AVHALAHALGALYGLHHGLLNAILLPYVLRFNRPAVEDKLARLARALgLG 307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 447083498 309 LPQSDDLaektIAAIEAFYHQLNVATQFGEHG----MAKEAAVDAV 350
Cdd:cd14861 308 LGGFDDF----IAWVEDLNERLGLPATLSELGvtedDLDELAELAL 349
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
3-352 |
2.21e-29 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 116.85 E-value: 2.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 3 FSYVNPTMIHFGQGQIASIRRDIpKDH---KVLVLYGGGSIKrNGVYDQVVEALSEHQ--WVEFSGVEPNPTKETLDKAV 77
Cdd:cd08188 1 FRFYIPPVNLFGPGCLKEIGDEL-KKLggkKALIVTDKGLVK-LGLVKKVTDVLEEAGieYVIFDGVQPNPTVTNVNEGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 78 HIVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDiLTGQHTV-KQATPIGAILTLPATGSESNTGAVITKAETQDK 156
Cdd:cd08188 79 ELFKENGCDFIISVGGGSAHDCAKAIGILATNGGEIED-YEGVDKSkKPGLPLIAINTTAGTASEVTRFAVITDEERHVK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 157 LAFLSPAVQPRFAVLDPDVMKSLPErqlvnGL-----VDAWVHVCEQYLTL---P-TQAMVQEGyAEVLLRNL---LALG 224
Cdd:cd08188 158 MVIVDWNVTPTIAVNDPELMLGMPP-----SLtaatgMDALTHAIEAYVSTgatPlTDALALEA-IRLIAENLpkaVANG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 225 ADFVNRDNDAWrANLMwtANQALN----GLIgtgvpqdwatHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKL- 299
Cdd:cd08188 232 KDLEARENMAY-AQFL--AGMAFNnaglGYV----------HAMAHQLGGFYNLPHGVCNAILLPHVMEFNLPACPERFa 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447083498 300 ---EQMGKNVFGLPqSDDLAEKTIAAIEAFYHQLNVATQFGEHG--------MAKEAAVDAVLQ 352
Cdd:cd08188 299 diaRALGENTEGLS-DEEAAEAAIEAIRKLSRRVGIPSGLKELGvkeedfplLAENALKDACGP 361
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-337 |
2.13e-27 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 111.47 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQG---QIASIRRDIPKDHKVLVlyGGGSIKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKN 82
Cdd:cd08194 1 PRTIIIGGGaleELGEEAASLGGKRALIV--TDKVMVKLGLVDKVTQLLAEAgiAYAVFDDVVSEPTDEMVEEGLALYKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 83 QHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSP 162
Cdd:cd08194 79 GGCDFIVALGGGSPIDTAKAIAVLATNGGPIRDYMGPRKVDKPGLPLIAIPTTAGTGSEVTRFTVITDTETDVKMLLKGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 163 AVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYL---------TLPTQAMvqegyaEVLLRNLLALgadFVNRDND 233
Cdd:cd08194 159 ALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAYVsrkaqpltdTLALSAI------KLIGRNLRRA---YADGDDL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 234 AWRANLMWTANQAlnG---------LIgtgvpqdwatH-M---IGheltALWHVDHARSLAIVQPWLLRNQLKHKKAKLE 300
Cdd:cd08194 230 EAREAMMLAALEA--GiafsnssvaLV----------HgMsrpIG----ALFHVPHGLSNAMLLPAVTEFSLPGAPERYA 293
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 447083498 301 Q----MGKNVFGLPQsDDLAEKTIAAIEAFYHQLNVAT--QFG 337
Cdd:cd08194 294 EiaraMGIATEGDSD-EEAAEKLVEALERLCADLEIPTlrEYG 335
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
8-344 |
4.60e-24 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 102.31 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQiasiRRDIPkdhkvLVLYGGGS---------IKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKA 76
Cdd:cd08191 4 PSRLLFGPGA----RRALG-----RVAARLGSrvlivtdprLASTPLVAELLAALTAAgvAVEVFDGGQPELPVSTVADA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 77 VHIVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGD-----GWDILTGQhtvkqATPIGAILTLPATGSESNTGAVITKA 151
Cdd:cd08191 75 AAAARAFDPDVVIGLGGGSNMDLAKVVALLLAHGGDprdyyGEDRVPGP-----VLPLIAVPTTAGTGSEVTPVAVLTDP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 152 ETQDKLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLPTQAM-------VQEG-------YAEVLL 217
Cdd:cd08191 150 ARGMKVGVSSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARDFPPFprldpdpVYVGknpltdlLALEAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 218 RnLLA--LGADFVNRDNDAWRANLMWTANQAlnGL-IGT-GVPqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLK 293
Cdd:cd08191 230 R-LIGrhLPRAVRDGDDLEARSGMALAALLA--GLaFGTaGTA---AAHALQYPIGALTHTSHGVGNGLLLPYVMRFNRP 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 447083498 294 HKKAKLEQMGKnVFGLP---QSDDLAEKTIAAIEAFYHQLNVATQFGEHGMAKE 344
Cdd:cd08191 304 ARAAELAEIAR-ALGVTtagTSEEAADRAIERVEELLARIGIPTTLADLGVTEA 356
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
8-285 |
4.64e-23 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 98.33 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRrDIpKDHKVLVLyGGGSIKRNGVYDQVVEALSEH-QWVEFSGVEPNPTKETLDKAVHIVKNQHID 86
Cdd:cd08180 4 KTKIYSGEDSLERLK-EL-KGKRVFIV-TDPFMVKSGMVDKVTDELDKSnEVEIFSDVVPDPSIEVVAKGLAKILEFKPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 87 FILAVGGGSVIDGSKyvAAAAFYegdgwdiLTGQHTVKQATPIgAILTLPATGSESNTGAVITKAETQDKLAFLSPAVQP 166
Cdd:cd08180 81 TIIALGGGSAIDAAK--AIIYFA-------LKQKGNIKKPLFI-AIPTTSGTGSEVTSFAVITDPEKGIKYPLVDDSMLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 167 RFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYL----TLPTQAMVQEGyAEVLLRNLLALgadFVNRDNDAWRANlMWT 242
Cdd:cd08180 151 DIAILDPELVKSVPPKVTADTGMDVLTHALEAYVstnaNDFTDALAEKA-IKLVFENLPRA---YRDGDDLEAREK-MHN 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 447083498 243 A--------NQAlnGLigtGVpqdwaTHMIGHELTALWHVDHARSLAIVQP 285
Cdd:cd08180 226 AscmagiafNNA--GL---GI-----NHSLAHALGGRFHIPHGRANAILLP 266
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
11-380 |
5.18e-23 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 99.24 E-value: 5.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 11 IHFGQGQIASIRRDIPKDH--KVLVLYGGgSIKRN-GVYDQVVEALSEHQWVEFSGVEPNPTKETLDKAVHIVKNQHIDF 87
Cdd:cd08192 4 VSYGPGAVEALLHELATLGasRVFIVTSK-SLATKtDVIKRLEEALGDRHVGVFSGVRQHTPREDVLEAARAVREAGADL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 88 ILAVGGGSVIDGSKYVA------AAAFYEGDGWDILTGQHTVKQATPIGAIlTLPAT--GSESNTGAVITKAETQDKLAF 159
Cdd:cd08192 83 LVSLGGGSPIDAAKAVAlalaedVTDVDQLDALEDGKRIDPNVTGPTLPHI-AIPTTlsGAEFTAGAGATDDDTGHKQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 160 LSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTL----PTQAMVQEGYaEVLLRNLLALGADfvNRDNDAw 235
Cdd:cd08192 162 AHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETLCSPqatpFVDALALKAL-RLLFEGLPRSKAD--PEDLEA- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 236 RANLM---WTANQALNGLIGTGvpqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLPQS 312
Cdd:cd08192 238 RLKCQlaaWLSLFGLGSGVPMG-----ASHAIGHQLGPLYGVPHGITSCIMLPAVLRFNAPVNAERQRLIARALGLVTGG 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447083498 313 DDLAEKTIA-AIEAFYHQLNVATQFGEHGMAKEaAVDAVLQQLTAHGMHKLGEQGTIDLQESRKILENA 380
Cdd:cd08192 313 LGREAADAAdAIDALIRELGLPRTLRDVGVGRD-QLEKIAENALTDVWCRTNPRPITDKDDVLEILESA 380
|
|
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
30-381 |
1.97e-21 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 94.92 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 30 KVLVLYGGGsIKRNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKyvaAAA 107
Cdd:cd08190 25 KVLVVTDPG-LAKLGLVERVLESLEKAgiEVVVYDGVRVEPTDESFEEAIEFAKEGDFDAFVAVGGGSVIDTAK---AAN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 108 FYEGDGWDIL--------TGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSPAVQPRFAVLDPDVMKSL 179
Cdd:cd08190 101 LYATHPGDFLdyvnapigKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTGISSRYLRPTLAIVDPLLTLTL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 180 PERQLVNGLVDAWVHVCEQYLTLPTQAM----------VQEG---YAEVLLRNLLALGADFV-----NRDNDAWRANLMW 241
Cdd:cd08190 181 PPRVTASSGFDVLCHALESYTARPYNARprpanpderpAYQGsnpISDVWAEKAIELIGKYLrravnDGDDLEARSNMLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 242 TANQA------------------LNGLIGTGVPQDWAThmiGHEltalwHVDHARSLAIVQPWLLR-----NQLKHKKAk 298
Cdd:cd08190 261 ASTLAgigfgnagvhlphamaypIAGLVKDYRPPGYPV---DHP-----HVPHGLSVALTAPAVFRftapaCPERHLEA- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 299 LEQMGKNVFGLPqSDDLAEKTIAAIEAFYHQLNVATQFGEHGMAKE---AAVDAVLQQ--LTAHGMHKLGEQgtiDLqes 373
Cdd:cd08190 332 AELLGADTSGAS-DRDAGEVLADALIKLMRDIGIPNGLSALGYSEDdipALVEGTLPQqrLLKLNPRPVTEE---DL--- 404
|
....*...
gi 447083498 374 RKILENAL 381
Cdd:cd08190 405 EEIFEDAL 412
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-334 |
3.31e-21 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 93.90 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 5 YVNPTMIHFGQGQIASIRRDIPKDHKVLVLYGGGSIKRNGVYDQVVEALSEHQwVE---FSGVEPNPTKETLDKAVHIVK 81
Cdd:cd14864 1 FKIPPNIVFGADSLERIGEEVKEYGSRFLLITDPVLKESGLADKIVSSLEKAG-ISvivFDEIPASATSDTIDEAAELAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 82 NQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGA-VITKAETQDKLAFl 160
Cdd:cd14864 80 KAGADGIIAVGGGKVLDTAKAVAILANNDGGAYDFLEGAKPKKKPLPLIAVPTTPRSGFEFSDRFpVVDSRSREVKLLK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 161 SPAVQPRFAVLDPDVMKSLPE----RQLVNGLVDAWVHVCEQYLTLPTQAMVQEGyAEVLLRNLLALGADFVNRDNdawR 236
Cdd:cd14864 159 AQPGLPKAVIVDPNLMASLTGnqtaAMALAALALAVEAYLSKKSNFFSDALALKA-IELVSENLDGALADPKNTPA---E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 237 ANLMWTAnqALNGL-IGTGVPQdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGLPQSDDL 315
Cdd:cd14864 235 ELLAQAG--CLAGLaASSSSPG--LATALALAVNSRYKVSKSLVASILLPHVIEYAATSAPDKYAKIARALGEDVEGASP 310
|
330 340
....*....|....*....|..
gi 447083498 316 AEKTIAAIEA---FYHQLNVAT 334
Cdd:cd14864 311 EEAAIAAVEGvrrLIAQLNLPT 332
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
8-367 |
1.09e-20 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 92.63 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPKDHKVLVLYGGGSIKrNGVYDQVVEALSEHQwVE---FSGVEPNPTKETLDKAVHIVKNQH 84
Cdd:cd08178 3 PPKIYFEPGCLPYLLLELPGVKRAFIVTDRVLYK-LGYVDKVLDVLEARG-VEtevFSDVEPDPTLSTVRKGLEAMNAFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 85 IDFILAVGGGSVIDGSKyvAAAAFYEGDG--WDILTGQH------------TVKQATPIgAILTLPATGSESNTGAVITK 150
Cdd:cd08178 81 PDVIIALGGGSAMDAAK--IMWLFYEHPEtkFEDLAQRFmdirkrvykfpkLGKKAKLV-AIPTTSGTGSEVTPFAVITD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 151 AETQDKLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTLP----TQAMVQEGyAEVLLRNLlalgAD 226
Cdd:cd08178 158 DKTGKKYPLADYALTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYVSVMasdyTDGLALQA-IKLIFEYL----PR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 227 FVNRDND-AWRANL--------MWTANqALNGLigtgvpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLR-N------ 290
Cdd:cd08178 233 SYNNGNDiEAREKMhnaatiagMAFAN-AFLGI----------CHSLAHKLGAAFHIPHGRANAILLPHVIRyNatdppt 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 291 ------QLKHKKAK-----LEQMGKnvFGLPQSDDLAEKTIAAIEAFYHQLNVATQFGEHGmAKEAAVDAVLQQLtahGM 359
Cdd:cd08178 302 kqaafpQYKYYVAKeryaeIADLLG--LGGKTPEEKVESLIKAIEDLKKDLGIPTSIREAG-IDEADFLAAVDKL---AE 375
|
....*...
gi 447083498 360 HKLGEQGT 367
Cdd:cd08178 376 DAFDDQCT 383
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
7-344 |
9.46e-19 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 86.59 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 7 NPTMiHFGQGQIASIRRDIPKD--HKVLVLYGGGSIKrNGVYDQVVEALSEHQ--WVEFSGVEPNPTKETLDKAVHIVKN 82
Cdd:PRK10624 8 NETA-YFGRGAIGALTDEVKRRgfKKALIVTDKTLVK-CGVVAKVTDVLDAAGlaYEIYDGVKPNPTIEVVKEGVEVFKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 83 QHIDFILAVGGGSVIDGSK----YVAAAAFYegdgwDI--LTG-QHTVKQATPIGAILTLPATGSESNTGAVITKAETQD 155
Cdd:PRK10624 86 SGADYLIAIGGGSPQDTCKaigiISNNPEFA-----DVrsLEGvAPTKKPSVPIIAIPTTAGTAAEVTINYVITDEEKRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 156 KLAFLSPAVQPRFAVLDPDVMKSLPerqlvNGL-----VDAWVHVCEQYLT---------LPTQAMvqegyaEVLLRNLl 221
Cdd:PRK10624 161 KFVCVDPHDIPQVAFVDADMMDSMP-----PGLkaatgVDALTHAIEGYITrgawaltdmLHLKAI------EIIAGAL- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 222 algADFVNRDNDAWRAnlMWTAnQALNGL----IGTGVpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRnqlKHKKA 297
Cdd:PRK10624 229 ---RGAVAGDKEAGEG--MALG-QYIAGMgfsnVGLGL-----VHGMAHPLGAFYNTPHGVANAILLPHVME---YNADF 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 447083498 298 KLEQ-------MGKNVFGLPQsDDLAEKTIAAIEAFYHQLNVATQFGEHGMAKE 344
Cdd:PRK10624 295 TGEKyrdiaraMGVKVEGMSL-EEARNAAVEAVKALNRDVGIPPHLRDVGVKEE 347
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
44-332 |
1.46e-18 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 86.16 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 44 GVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQH 121
Cdd:PRK09860 46 GMAGDVQKALEERniFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDYEGVDR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 122 TVKQATPIGAILTLPATGSESNTGAVITKAETQDKLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLT 201
Cdd:PRK09860 126 SAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 202 LP----TQAMVQEGYAeVLLRNL---LALGADFVNRDNDAWRANLMWTA-NQALNGLIgtgvpqdwatHMIGHELTALWH 273
Cdd:PRK09860 206 IAatpiTDACALKAVT-MIAENLplaVEDGSNAKAREAMAYAQFLAGMAfNNASLGYV----------HAMAHQLGGFYN 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447083498 274 VDHARSLAIVQPWLLRNQLKHKKAKL----EQMGKNVFGLPQSDDlAEKTIAAIEAFYHQLNV 332
Cdd:PRK09860 275 LPHGVCNAVLLPHVQVFNSKVAAARLrdcaAAMGVNVTGKNDAEG-AEACINAIRELAKKVDI 336
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
30-351 |
9.16e-17 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 80.67 E-value: 9.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 30 KVLVLYGGGSIKrNGVYDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAAAA 107
Cdd:cd17814 28 KVLVVTDPGVIK-AGWVDEVLDSLEAEglEYVVFSDVTPNPRDFEVMEGAELYREEGCDGIVAVGGGSPIDCAKGIGIVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 108 F-------YEGdgwdiltgqhtVKQAT----PIGAILTLPATGSESNTGAVITKAETQDKLAFLSPAVQPRFAVLDPDVM 176
Cdd:cd17814 107 SngghildYEG-----------VDKVRrplpPLICIPTTAGSSADVSQFAIITDTERRVKMAIISKTLVPDVSLIDPETL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 177 KSLPERQLVNGLVDAWVHVCEQYLTLPTQAMVqEGYA----EVLLRNLLALGADfvnRDNDAWRANLMWTANQA----LN 248
Cdd:cd17814 176 TTMDPELTACTGMDALTHAIEAYVSNASSPLT-DLHAleaiRLISENLPKAVAD---PDDLEAREKMMLASLQAglafSN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 249 GLIGtgvpqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKL----EQMGKNVFGLPqSDDLAEKTIAAIE 324
Cdd:cd17814 252 ASLG-------AVHAMAHSLGGLLDLPHGECNALLLPHVIRFNFPAAPERYrkiaEAMGLDVDGLD-DEEVAERLIEAIR 323
|
330 340 350
....*....|....*....|....*....|....*
gi 447083498 325 AFYHQLNVATQFGEHG--------MAKEAAVDAVL 351
Cdd:cd17814 324 DLREDLGIPETLSELGvdeedipeLAKRAMKDPCL 358
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
11-360 |
2.12e-16 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 79.97 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 11 IHFGQGQIASIRRDIpKDH---KVLVLyGGGSIKRNG-VYDQVVEALSEHQWVEFSGVEPNPTKETLDKAVHIVKNQHID 86
Cdd:cd14866 8 LFSGRGALARLGREL-DRLgarRALVV-CGSSVGANPdLMDPVRAALGDRLAGVFDGVRPHSPLETVEAAAEALREADAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 87 FILAVGGGSVIDGSKyVAAAAFYEGDGWDILTGQHTVKQA----------TPIGAILTLPATGSESnTGAVITKAETQDK 156
Cdd:cd14866 86 AVVAVGGGSAIVTAR-AASILLAEDRDVRELCTRRAEDGLmvsprldapkLPIFVVPTTPTTADVK-AGSAVTDPPAGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 157 LAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQyLTLPTQAMVQEGYAEVLLRNLLALGADFVNRDNDAWR 236
Cdd:cd14866 164 LALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEG-LYSRHADPLADATLMHALRLLADGLPRLADDDDPAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 237 ANLMWTANQALNGLIGTGVPqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGkNVFGLPQS--DD 314
Cdd:cd14866 243 ADLVLAAVLAGYGTDHTGGG---VIHALGHAIGARYGVQNGVVHAILLPHVLRFNAPATDGRLDRLA-EALGVADAgdEA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 447083498 315 LAEKTIAAIEAFYHQLNVATQFGEHGMAKEAavdavLQQLTAHGMH 360
Cdd:cd14866 319 SAAAVVDAVEALLDALGVPTRLRDLGVSRED-----LPAIAEAAMD 359
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
29-271 |
5.55e-12 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 66.34 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 29 HKVLVLYGGGSIKRNGvyDQVVEALSEH----QWVEFSGvepNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVa 104
Cdd:COG0371 28 KRALIITGPTALKAAG--DRLEESLEDAgievEVEVFGG---ECSEEEIERLAEEAKEQGADVIIGVGGGKALDTAKAV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 105 aaAFYEGdgwdiltgqhtvkqaTPIGAILTLPATGSESNTGAVITKAETqdklAFLSPAVQPR--FAVL-DPDVMKSLPE 181
Cdd:COG0371 102 --AYRLG---------------LPVVSVPTIASTDAPASPLSVIYTEDG----AFDGYSFLAKnpDLVLvDTDIIAKAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 182 RQLVNGLVDA---W--VHVCEQ--------YLTLPTQAMVQEGYaEVLLRN-LLALGADFVNRDNDAWRANLMwtANQAL 247
Cdd:COG0371 161 RLLAAGIGDAlakWyeARDWSLahrdlageYYTEAAVALARLCA-ETLLEYgEAAIKAVEAGVVTPALERVVE--ANLLL 237
|
250 260 270
....*....|....*....|....*....|..
gi 447083498 248 NGLI--------GTGvpqdwATHMIGHELTAL 271
Cdd:COG0371 238 SGLAmgigssrpGSG-----AAHAIHNGLTAL 264
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
11-354 |
5.78e-12 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 66.38 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 11 IHFGQG---QIASIRRDIPKdHKVLVLYGGGsIKRNGVYDQVVEALSE--HQWVEFSGVEPNPTKETLDKAVHIVKNQHI 85
Cdd:cd08193 7 IICGAGaaaRLGELLRELGA-RRVLLVTDPG-LVKAGLADPALAALEAagIAVTVFDDVVADPPEAVVEAAVEQAREAGA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 86 DFILAVGGGSVIDGSKYVAAAAFYEGD-----GWDILTGQHTvkqatPIGAILTLPATGSESNTGAVITKAETQdKLAFL 160
Cdd:cd08193 85 DGVIGFGGGSSMDVAKLVALLAGSDQPlddiyGVGKATGPRL-----PLILVPTTAGTGSEVTPISIVTTGETE-KKGVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 161 SPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLT----------LPTQAMvqegyaEVLLRNLLALGADFVNR 230
Cdd:cd08193 159 SPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYTSrhkknpisdaLAREAL------RLLGANLRRAVEDGSDL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 231 DNdawRANLMW---TANQAL-NGLIGtgvpqdwATHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNV 306
Cdd:cd08193 233 EA---REAMLLgsmLAGQAFaNAPVA-------AVHALAYPLGGHFHVPHGLSNALVLPHVLRFNLPAAEALYAELARAL 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 447083498 307 F-GLPQSDDL--AEKTIAAIEAFYHQLNVATQFGEHGMAKE----AAVDAVLQQL 354
Cdd:cd08193 303 LpGLAFGSDAaaAEAFIDALEELVEASGLPTRLRDVGVTEEdlpmLAEDAMKQTR 357
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
68-228 |
1.24e-11 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 65.32 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 68 PTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAAAafYEGDGWDILTGQHTVKQATPIGAILTLPATGSE-SNTGA 146
Cdd:cd14860 62 PSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAKLLALK--GISPVLDLFDGKIPLIKEKELIIVPTTCGTGSEvTNISI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 147 V-ITKAETQDKLAflSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYL----TLPTQA-------MVQEGYAE 214
Cdd:cd14860 140 VeLTSLGTKKGLA--VDELYADKAVLIPELLKGLPYKVFATSSIDALIHAIESYLspkaTPYTEMfsykaieMILEGYQE 217
|
170
....*....|....*..
gi 447083498 215 VLLRNLLALGA---DFV 228
Cdd:cd14860 218 IAEKGEEARFPllgDFL 234
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
76-344 |
2.77e-11 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 64.28 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 76 AVHIVKNQHIDFILAVGGGSVIDGSKYVAAAAFYEGDGWDILTGQHTVKQATPIGAILTLPATGSESNTGAVITKAETQD 155
Cdd:PRK15454 98 AVAQLRESGCDGVIAFGGGSVLDAAKAVALLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 156 KLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLTL---PTQAMVQEGYAEVLLRNL---LALGADFVN 229
Cdd:PRK15454 178 KQVLAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALnatPFTDSLAIGAIAMIGKSLpkaVGYGHDLAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 230 RDNdAWRANLMwtANQALNGlIGTGVpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGl 309
Cdd:PRK15454 258 RES-MLLASCM--AGMAFSS-AGLGL-----CHAMAHQPGAALHIPHGLANAMLLPTVMEFNRMVCRERFSQIGRALRT- 327
|
250 260 270
....*....|....*....|....*....|....*
gi 447083498 310 PQSDDLaeKTIAAIEAFYHQLNVATQFGEHGMAKE 344
Cdd:PRK15454 328 KKSDDR--DAINAVSELIAEVGIGKRLGDVGATSA 360
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
8-355 |
8.88e-11 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 63.67 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPKDHKVLVLYGGGSIKrNGVYDQVVEALS-EHQWVE---FSGVEPNPTKETLDKAVHIVKNQ 83
Cdd:PRK13805 460 PKKIYFERGSLPYLLDELDGKKRAFIVTDRFMVE-LGYVDKVTDVLKkRENGVEyevFSEVEPDPTLSTVRKGAELMRSF 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 84 HIDFILAVGGGSVIDGSKyvAAAAFYEGDG----------WDIltgQHTVKQATPIG------AILTLPATGSESNTGAV 147
Cdd:PRK13805 539 KPDTIIALGGGSPMDAAK--IMWLFYEHPEtdfedlaqkfMDI---RKRIYKFPKLGkkaklvAIPTTSGTGSEVTPFAV 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 148 ITKAETQDKLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQYLT---------LPTQAMvqegyaEVLLR 218
Cdd:PRK13805 614 ITDDKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSvmasdytdgLALQAI------KLVFE 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 219 NL---LALGA-DFVNRDNDAWRANL--MWTANQALngligtGVpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLR-N- 290
Cdd:PRK13805 688 YLprsYKNGAkDPEAREKMHNASTIagMAFANAFL------GI-----CHSMAHKLGAEFHIPHGRANAILLPHVIRyNa 756
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447083498 291 ----------QLKHKKA--KLEQMGKNVfGLPQSDD--LAEKTIAAIEAFYHQLNVATQFGEHGMaKEAAVDAVLQQLT 355
Cdd:PRK13805 757 tdppkqaafpQYEYPRAdeRYAEIARHL-GLPGSTTeeKVESLIKAIEELKAELGIPMSIKEAGV-DEADFLAKLDELA 833
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
8-352 |
5.32e-10 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 60.21 E-value: 5.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPKD--HKVLVLYGGGsikRNGVYDQVVEALSEHQWVEFSGVEPNPTKETLDKAVHIVKNQHI 85
Cdd:cd08177 1 PQRVVFGAGTLAELAEELERLgaRRALVLSTPR---QRALAERVAALLGDRVAGVFDGAVMHVPVEVAERALAAAREAGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 86 DFILAVGGGSVIDGSKYVAAaafyegdgwdiltgqHTvkqATPIGAIltlPAT--GSE--SNTGavITKAETqdKLAFLS 161
Cdd:cd08177 78 DGLVAIGGGSAIGLAKAIAL---------------RT---GLPIVAV---PTTyaGSEmtPIWG--ETEDGV--KTTGRD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 162 PAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCEQyLTLP-----TQAMVQEGyAEVLLRNLLALGADFvnRDNDAwR 236
Cdd:cd08177 133 PRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEA-LYAPdanpiTSLLAEEG-IRALARALPRLVADP--SDLEA-R 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 237 ANLM---WTANQALnGLIGTGVpqdwaTHMIGHELTALWHVDHARSLAIVQPWLLRNQLKHKKAKLEQMGKNVFGlpqsD 313
Cdd:cd08177 208 SDALygaWLAGVVL-GSVGMGL-----HHKLCHVLGGTFDLPHAETHAVVLPHVLAYNAPAAPDAMARLARALGG----G 277
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 447083498 314 DLAektiAAIEAFYHQLNVATQFGEHGMAKE---AAVDAVLQ 352
Cdd:cd08177 278 DAA----GGLYDLARRLGAPTSLRDLGMPEDdidRAADLALA 315
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
30-271 |
2.18e-09 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 58.32 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 30 KVLVLYGGGSIKRngVYDQVVEALSEH----QWVEFSGVepnPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAA 105
Cdd:cd08550 24 KALIIGGKTALEA--VGEKLEKSLEEAgidyEVEVFGGE---CTEENIERLAEKAKEEGADVIIGIGGGKVLDTAKAVAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 106 AAfyegdgwDIltgqhtvkqatPIGAILTLPATGSESNTGAVI-TKAETQDKLAFLSPAvqPRFAVLDPDVMKSLPERQL 184
Cdd:cd08550 99 RL-------GL-----------PVVTVPTIAATCAAWSALSVLyDEEGEFLGYSLLKRS--PDLVLVDTDIIAAAPVRYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 185 VNGLVDA---W--VHVCEQYL--TLPTQAMVQegYAEVLLRNLLALGADFVnRDNDAWRANLMWT----ANQALNGLIGT 253
Cdd:cd08550 159 AAGIGDTlakWyeARPSSRGGpdDLALQAAVQ--LAKLAYDLLLEYGVQAV-EDVRQGKVTPALEdvvdAIILLAGLVGS 235
|
250 260
....*....|....*....|.
gi 447083498 254 ---GVPQDWATHMIGHELTAL 271
Cdd:cd08550 236 lggGGCRTAAAHAIHNGLTKL 256
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
29-268 |
1.28e-08 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 55.39 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 29 HKVLVLYGGGSIKRNGvyDQVVEALSEH--QWVEFSGVEPNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAAa 106
Cdd:pfam13685 20 RRVALVADANTYAAAG--RKVAESLKRAgiEVETRLEVAGNADMETAEKLVGALRERDADAVVGVGGGTVIDLAKYAAF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 107 afyegdgwdiltgqhtvKQATPIGAILTLPATGSESNTGAVITKaeTQDKLAFlsPAVQPrFAVL-DPDVMKSLPERQLV 185
Cdd:pfam13685 97 -----------------KLGKPFISVPTAASNDGFASPGASLTV--DGKKRSI--PAAAP-FGVIaDTDVIAAAPRRLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 186 NG----------LVDAWVHVCEQY---LTLPTQAMVQEGYAEVL--LRNLLALGAdfvnrdndAWRANLMwtanqalnGL 250
Cdd:pfam13685 155 SGvgdllakitaVADWELAHAEEVaapLALLSAAMVMNFADRPLrdPGDIEALAE--------LLSALAM--------GG 218
|
250
....*....|....*...
gi 447083498 251 IGTGVPQDWATHMIGHEL 268
Cdd:pfam13685 219 AGSSRPASGSEHLISHAL 236
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
8-104 |
1.48e-08 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 55.64 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPKDH---KVLVLYGGGSIKRNG--VYDQVVEALSEHQWVEFSGVEpnpTKETLDKAVHIVKN 82
Cdd:cd08173 2 PRNVVVGHGAINKIGEVLKKLLlgkRALIITGPNTYKIAGkrVEDLLESSGVEVVIVDIATIE---EAAEVEKVKKLIKE 78
|
90 100
....*....|....*....|..
gi 447083498 83 QHIDFILAVGGGSVIDGSKYVA 104
Cdd:cd08173 79 SKADFIIGVGGGKVIDVAKYAA 100
|
|
| egsA |
PRK00843 |
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed |
1-104 |
2.90e-08 |
|
NAD(P)-dependent glycerol-1-phosphate dehydrogenase; Reviewed
Pssm-ID: 179139 Cd Length: 350 Bit Score: 54.90 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 1 MQFsyvnPTMIHFGQG---QIASIRRDIPKDHKVLVLYGGGSIKRNGvyDQVVEALSEHQWVEFSGVEpNPTKETLDKAV 77
Cdd:PRK00843 8 IQL----PRDVVVGHGvldDIGDVCSDLKLTGRALIVTGPTTKKIAG--DRVEENLEDAGDVEVVIVD-EATMEEVEKVE 80
|
90 100
....*....|....*....|....*..
gi 447083498 78 HIVKNQHIDFILAVGGGSVIDGSKYVA 104
Cdd:PRK00843 81 EKAKDVNAGFLIGVGGGKVIDVAKLAA 107
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
59-197 |
1.03e-06 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 49.96 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 59 VEFSGVEPNPTKETLDKAVHIVKNQHI---DFILAVGGGSVIDGSKYVA-------AAAFYEgdGWDIltgqhtVK-QAT 127
Cdd:cd08184 54 LIFVDTTDEPKTDQIDALRAQIRAENDklpAAVVGIGGGSTMDIAKAVSnmltnpgSAADYQ--GWDL------VKnPGI 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 128 PIGAILTLPATGSESNTGAVITKAETqdKLAFLSPAVQPRFAVLDPDVMKSLPERQLVNGLVDAWVHVCE 197
Cdd:cd08184 126 YKIGVPTLSGTGAEASRTAVLTGPEK--KLGINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVE 193
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
29-107 |
4.15e-06 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 48.29 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 29 HKVLVLYGGGSIKRngVYDQVVEALSEHQ-WVEFSGVEPNptkeTLDKAVHIV-KNQHIDFILAVGGGSVIDGSKYVAAA 106
Cdd:cd08174 26 GKVAIVTGEGIDEL--LGEDILESLEEAGeIVTVEENTDN----SAEELAEKAfSLPKVDAIVGIGGGKVLDVAKYAAFL 99
|
.
gi 447083498 107 A 107
Cdd:cd08174 100 S 100
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
30-107 |
1.43e-04 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 43.55 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 30 KVLVLYGGGSIKRNGvyDQVVEALSEH----QWVEFSGvEPnpTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAA 105
Cdd:cd08170 24 KALVIADPFVLDLVG--ERLEESLEKAglevVFEVFGG-EC--SREEIERLAAIARANGADVVIGIGGGKTIDTAKAVAD 98
|
..
gi 447083498 106 AA 107
Cdd:cd08170 99 YL 100
|
|
| GlyDH-like |
cd08172 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins ... |
29-105 |
1.10e-03 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins that have yet to be characterized, but show sequence homology with glycerol dehydrogenase. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341451 [Multi-domain] Cd Length: 346 Bit Score: 40.58 E-value: 1.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447083498 29 HKVLVLYGGGSIKrngVYDQVVEALSEHQWVE--FSGvepNPTKETLDKAVHIVKNQHIDFILAVGGGSVIDGSKYVAA 105
Cdd:cd08172 24 KRPLIIHGEKSWQ---AAKPYLPKLFEIEYPVlrYDG---ECSYEEIDRLAEEAKEHQADVIIGIGGGKVLDTAKAVAD 96
|
|
| DHQ-like |
cd08169 |
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose ... |
11-191 |
1.83e-03 |
|
Dehydroquinate synthase-like which includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase; This group contains dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. These proteins exhibit the dehydroquinate synthase structural fold. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. 2-deoxy-scyllo-inosose synthase (DOIS) catalyzes carbocycle formation from D-glucose-6-phosphate to 2-deoxy-scyllo-inosose through a multi-step reaction in the biosynthesis of aminoglycoside antibiotics. 2-deoxystreptamine (DOS)-containing aminoglycoside antibiotics includes neomycin, kanamycin, gentamicin, and ribostamycin. 2-epi-5-epi-valiolone synthases catalyze the cyclization of sedoheptulose 7-phosphate to 2-epi-5-epi-valiolone in the biosynthesis of C(7)N-aminocyclitol-containing products. The cyclization product, 2-epi-5-epi-valiolone ((2S,3S,4S,5R)-5-(hydroxymethyl)cyclohexanon-2,3,4,5-tetrol), is a precursor of the valienamine moiety. The valienamine unit is responsible for their biological activities as various glycosidic hydrolases inhibitors. Two important microbial secondary metabolites, validamycin and acarbose, are used in agricultural and biomedical applications.
Pssm-ID: 341448 [Multi-domain] Cd Length: 328 Bit Score: 40.08 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 11 IHFGQGQIASIRRDIPKDHKVLVLY---GGGSIKRNGVYDQVVEALSEHQWVEFSGVEPNPT----KETLDKAVHIVKNQ 83
Cdd:cd08169 4 VFFGEGVFESVNSYIPRDAFDQCLIivdSGVPDLIVNYLAEYFGYYLEVHVFIIQGGEAYKTfqtvVEELERAAALHLNR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 84 HiDFILAVGGGSVIDGSKYVAAAAFyegdgwdilTGQHTVKQATpigAILTLPATGSESNTGAVITKAETqdklaFLSPA 163
Cdd:cd08169 84 H-SAVVAVGGGATGDVVGFAAATYF---------RGIAFIRVPT---TLLAQSDSSVGIKVGINTRGGKN-----LLGAF 145
|
170 180
....*....|....*....|....*...
gi 447083498 164 VQPRFAVLDPDVMKSLPERQLVNGLVDA 191
Cdd:cd08169 146 YPPRAVFADFSFLKTLPFRQVRAGMAEL 173
|
|
| G1PDH_related |
cd08549 |
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and ... |
8-190 |
2.88e-03 |
|
Glycerol-1-phosphate dehydrogenase and related proteins; This family contains bacterial and archeal glycerol-1-phosphate dehydrogenase-like oxidoreductases. These proteins have similarity with glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion. It also contains archaeal Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) that plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids.
Pssm-ID: 341479 [Multi-domain] Cd Length: 331 Bit Score: 39.47 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 8 PTMIHFGQGQIASIRRDIPK-DHKVLVLYGGGSIKRNgVYDQVVEALSEHQWVEfsgvepnPTKETLDKAVHIVKNQHID 86
Cdd:cd08549 1 PRYTIVGDGAINKIEEILKKlNLKRVLIITGKNTKAK-YCRFFYDQLKTVCDIV-------YYDNIDNLEDELKKYTFYD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 87 FILAVGGGSVIDGSKYVAaaafyegdgwdiltgqhtVKQATPIGAILTLPATGSESNTGAVITkaETQDKLAFLSPAvqP 166
Cdd:cd08549 73 CVIGIGGGRSIDTGKYLA------------------YKLKIPFISVPTSASNDGIASPIVSLR--IPGVKKTFMADA--P 130
|
170 180
....*....|....*....|....
gi 447083498 167 RFAVLDPDVMKSLPERQLVNGLVD 190
Cdd:cd08549 131 IAIIADTEIIKKSPRRLLSAGIGD 154
|
|
| AroB |
COG0337 |
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase ... |
11-188 |
6.34e-03 |
|
3-dehydroquinate synthetase [Amino acid transport and metabolism]; 3-dehydroquinate synthetase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440106 Cd Length: 355 Bit Score: 38.15 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 11 IHFGQG---QIASIRRDIPKDHKVLV--------LYGggsikrngvyDQVVEALSEHQW----VEFSGVEPNPTKETLDK 75
Cdd:COG0337 15 IRIGRGlldELGELLAELLKGRRVLVvtdenvapLYG----------ERLRAALEAAGFevhlLVLPDGEASKTLETLER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447083498 76 AVHIVKNQHI---DFILAVGGGSVID--GskyVAAAAFYEGdgwdI--------LTGQH----TVKQA--TP-----IGA 131
Cdd:COG0337 85 ILDALLEAGLdrdDLVVALGGGVVGDlaG---FAAATYLRG----VpfiqvpttLLAQVdssvGGKTGvnHPggknlIGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447083498 132 ILtlpatgsesntgavitkaetqdklaflspavQPRFAVLDPDVMKSLPERQLVNGL 188
Cdd:COG0337 158 FH-------------------------------QPRAVLIDLDFLKTLPERELRAGL 183
|
|
| |
