NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1215925580|ref|WP_089109987|]
View 

MULTISPECIES: FAD-dependent oxidoreductase [Lactobacillaceae]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 1562436)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Pyr_redox_2 super family cl39093
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 5-446 6.54e-104

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


The actual alignment was detected with superfamily member PRK09564:

Pssm-ID: 476868 [Multi-domain]  Cd Length: 444  Bit Score: 316.60  E-value: 6.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   5 KVIVVGASHGGHQSVLELTHKYSDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPADLEKLGTEVYANHEVTK 84
Cdd:PRK09564    2 KIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  85 INPENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDPNVKNITVIGAGYIG 164
Cdd:PRK09564   82 VDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGFIG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 165 IEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQA 244
Cdd:PRK09564  162 LEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 245 AGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDMPIALATVARREARYVAEHIFENtpSI 323
Cdd:PRK09564  242 TGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGR--HV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 324 PFSGVVGSSALSVFDYHFATSGLNMTTAQKADIEIHTSFYKDTLRPAYVPmekGNTEVYVELDYNPNTHQLLGGAVLSTY 403
Cdd:PRK09564  320 SFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYP---GQEDLYVKLIYEADTKVILGGQIIGKK 396

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1215925580 404 DITAQGNVISLAIQQGLKLEDLAEADFFFQPGFDRQWSLLNLA 446
Cdd:PRK09564  397 GAVLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVA 439
 
Name Accession Description Interval E-value
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 5-446 6.54e-104

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 316.60  E-value: 6.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   5 KVIVVGASHGGHQSVLELTHKYSDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPADLEKLGTEVYANHEVTK 84
Cdd:PRK09564    2 KIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  85 INPENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDPNVKNITVIGAGYIG 164
Cdd:PRK09564   82 VDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGFIG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 165 IEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQA 244
Cdd:PRK09564  162 LEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 245 AGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDMPIALATVARREARYVAEHIFENtpSI 323
Cdd:PRK09564  242 TGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGR--HV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 324 PFSGVVGSSALSVFDYHFATSGLNMTTAQKADIEIHTSFYKDTLRPAYVPmekGNTEVYVELDYNPNTHQLLGGAVLSTY 403
Cdd:PRK09564  320 SFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYP---GQEDLYVKLIYEADTKVILGGQIIGKK 396

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1215925580 404 DITAQGNVISLAIQQGLKLEDLAEADFFFQPGFDRQWSLLNLA 446
Cdd:PRK09564  397 GAVLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVA 439
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 25-345 1.06e-102

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 309.05  E-value: 1.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  25 KYSDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPADLEKLGTEVYANHEVTKINPENKQVIVKDlksGkiQS 104
Cdd:COG0446     2 LGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRD---G--ET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 105 YDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDPNVKNITVIGAGYIGIEAAEASIKAGKNVTLIDMI 184
Cdd:COG0446    77 LSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 185 NRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWLRGT-VELDKR 263
Cdd:COG0446   157 PRLLGVL-DPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAgLALGER 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 264 GWIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDMPIALATVARREARYVAEHIFENTPSIPFsgvVGSSALSVFDYHFAT 343
Cdd:COG0446   236 GWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG---LGTFISKVFDLCIAS 312


                  ..
gi 1215925580 344 SG 345
Cdd:COG0446   313 TG 314
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-309 9.28e-64

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 207.94  E-value: 9.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   4 TKVIVVGASHGGHQSVLELTHKysDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPA--------DLEKLGTE 75
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQL--GGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLykrkeevvKKLNNGIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  76 VYANHEVTKINPENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDpnvKNI 155
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLP---KRV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 156 TVIGAGYIGIEAAEASIKAGKNVTLIDMINRpLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDA- 234
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGt 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215925580 235 EYPSDLIIQAAGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAVLAYsipaqkdmpIALATVARREA 309
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGG---------PELAQNAVAQG 301
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 90-428 3.34e-34

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 133.15  E-value: 3.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  90 KQVIVKDlkSGKIQSYDYDKLILSSGVTPNNLPVP-GHELKNVYSMRGKdwaekikakLSDPNV-KNITVIGAGYIGIEA 167
Cdd:TIGR01350 117 GTVSVTG--ENGEETLEAKNIIIATGSRPRSLPGPfDFDGKVVITSTGA---------LNLEEVpESLVIIGGGVIGIEF 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 168 AEASIKAGKNVTLIDMINRPLGNyLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAE---YPSDLIIQA 244
Cdd:TIGR01350 186 ASIFASLGSKVTVIEMLDRILPG-EDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGEtetLTGEKVLVA 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 245 AGVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATVARREARYVAEHIFENTP 321
Cdd:TIGR01350 265 VGRKPNTEGLgleKLGVELDERGRIVVDEYMRTNVPGIYAIGDVI----------GGPMLAHVASHEGIVAAENIAGKEP 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 322 SIPFSGVVGSSALSvfDYHFATSGLNMTTAQKADIEIHTSFYKDTLRPAYVPMekGNTEVYVELDYNPNTHQLLGGAVL- 400
Cdd:TIGR01350 335 AHIDYDAVPSVIYT--DPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALAL--GETDGFVKIIADKKTGEILGAHIIg 410

                         330       340
                  ....*....|....*....|....*....
gi 1215925580 401 -STYDITAQgnvISLAIQQGLKLEDLAEA 428
Cdd:TIGR01350 411 pHATELISE---AALAMELEGTVEELART 436
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 153-259 2.97e-03

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 39.24  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGA-GYIGIEAAEASIKAGKNVTLIDMINRPLGNYldteltdilSKELTNK-GVQVVT-GAKIESYEGLEAvsAV 229
Cdd:cd05352     9 KVAIVTGGsRGIGLAIARALAEAGADVAIIYNSAPRAEEK---------AEELAKKyGVKTKAyKCDVSSQESVEK--TF 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1215925580 230 KTSDAEY-PSDLIIQAAGVKPNTDWLRGTVE 259
Cdd:cd05352    78 KQIQKDFgKIDILIANAGITVHKPALDYTYE 108
 
Name Accession Description Interval E-value
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 5-446 6.54e-104

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 316.60  E-value: 6.54e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   5 KVIVVGASHGGHQSVLELTHKYSDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPADLEKLGTEVYANHEVTK 84
Cdd:PRK09564    2 KIIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVVK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  85 INPENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDPNVKNITVIGAGYIG 164
Cdd:PRK09564   82 VDAKNKTITVKNLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGFIG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 165 IEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQA 244
Cdd:PRK09564  162 LEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 245 AGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDMPIALATVARREARYVAEHIFENtpSI 323
Cdd:PRK09564  242 TGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGR--HV 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 324 PFSGVVGSSALSVFDYHFATSGLNMTTAQKADIEIHTSFYKDTLRPAYVPmekGNTEVYVELDYNPNTHQLLGGAVLSTY 403
Cdd:PRK09564  320 SFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKDKNHTNYYP---GQEDLYVKLIYEADTKVILGGQIIGKK 396

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1215925580 404 DITAQGNVISLAIQQGLKLEDLAEADFFFQPGFDRQWSLLNLA 446
Cdd:PRK09564  397 GAVLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVA 439
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 25-345 1.06e-102

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 309.05  E-value: 1.06e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  25 KYSDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPADLEKLGTEVYANHEVTKINPENKQVIVKDlksGkiQS 104
Cdd:COG0446     2 LGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRD---G--ET 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 105 YDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDPNVKNITVIGAGYIGIEAAEASIKAGKNVTLIDMI 184
Cdd:COG0446    77 LSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 185 NRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWLRGT-VELDKR 263
Cdd:COG0446   157 PRLLGVL-DPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAgLALGER 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 264 GWIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDMPIALATVARREARYVAEHIFENTPSIPFsgvVGSSALSVFDYHFAT 343
Cdd:COG0446   236 GWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG---LGTFISKVFDLCIAS 312


                  ..
gi 1215925580 344 SG 345
Cdd:COG0446   313 TG 314
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
3-352 5.41e-71

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 230.03  E-value: 5.41e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   3 KTKVIVVGASHGGHQSVLELTHKYSDLDIKLFEAGDFISFMSCGMELYLENSVTnVNDVRNFKPADLEKLGTEVYANHEV 82
Cdd:COG1251     1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETD-EEDLLLRPADFYEENGIDLRLGTRV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  83 TKINPENKQVIvkdLKSGkiQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLsdPNVKNITVIGAGY 162
Cdd:COG1251    80 TAIDRAARTVT---LADG--ETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAAL--APGKRVVVIGGGL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 163 IGIEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAE-YPSDLI 241
Cdd:COG1251   153 IGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEeLPADLV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 242 IQAAGVKPNTDWLRGT-VELDkRGwIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDMpIALATVARREARYVAEHIFENT 320
Cdd:COG1251   233 VVAIGVRPNTELARAAgLAVD-RG-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRV-LELVAPAYEQARVAAANLAGGP 309

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1215925580 321 psIPFSGVVGSSALSVFDYHFATSGLNMTTAQ 352
Cdd:COG1251   310 --AAYEGSVPSTKLKVFGVDVASAGDAEGDEE 339
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 4-309 9.28e-64

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 207.94  E-value: 9.28e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   4 TKVIVVGASHGGHQSVLELTHKysDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPA--------DLEKLGTE 75
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQL--GGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLykrkeevvKKLNNGIE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  76 VYANHEVTKINPENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDpnvKNI 155
Cdd:pfam07992  79 VLLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLP---KRV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 156 TVIGAGYIGIEAAEASIKAGKNVTLIDMINRpLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDA- 234
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGt 234

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215925580 235 EYPSDLIIQAAGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAVLAYsipaqkdmpIALATVARREA 309
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGG---------PELAQNAVAQG 301
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 4-445 1.84e-61

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 206.17  E-value: 1.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   4 TKVIVVGASHGGHQSVLELTHKYSDLDIKLFEAGDFISFMSCGMELYLENSVTNVNDVRNFKPADL-EKLGTEVYANHEV 82
Cdd:PRK13512    2 PKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFyDRKQITVKTYHEV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  83 TKINPENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNnlpVPGHELKNVYSMRGKDWAEKIKAKLSDPNVKNITVIGAGY 162
Cdd:PRK13512   82 IAINDERQTVTVLNRKTNEQFEESYDKLILSPGASAN---SLGFESDITFTLRNLEDTDAIDQFIKANQVDKALVVGAGY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 163 IGIEAAEASIKAGKNVTLI---DMINRplgnYLDTELTDILSKELTNKGVQvvtgakiesYEGLEAVSAVKTSDAEYPS- 238
Cdd:PRK13512  159 ISLEVLENLYERGLHPTLIhrsDKINK----LMDADMNQPILDELDKREIP---------YRLNEEIDAINGNEVTFKSg 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 239 -----DLIIQAAGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAVLAY----SIPAQkdmpIALATVARRE 308
Cdd:PRK13512  226 kvehyDMIIEGVGTHPNSKFIESSnIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHyrhvDLPAS----VPLAWGAHRA 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 309 ARYVAEHIFENTpSIPFSGVVGSSALSVFDYHFATSGLNMTTAQKADIEI--HTSFYKdtlrPAYVPmekGNTEVYVELD 386
Cdd:PRK13512  302 ASIVAEQIAGND-TIEFKGFLGNNIVKFFDYTFASVGVKPNELKQFDYKMveVTQGAH----ANYYP---GNSPLHLRVY 373

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1215925580 387 YNPNTHQLLGGAVLSTYDITAQGNVISLAIQQGLKLEDLAEADFFFQPGFDRQWSLLNL 445
Cdd:PRK13512  374 YDTSNRKILRAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINM 432
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 108-428 4.07e-44

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 160.25  E-value: 4.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 108 DKLILSSGVTPNNLPVPGHELKNVYSmrgkdwaekikaklSD--------PnvKNITVIGAGYIGIEAAEASIKAGKNVT 179
Cdd:COG1249   132 DHIVIATGSRPRVPPIPGLDEVRVLT--------------SDealeleelP--KSLVVIGGGYIGLEFAQIFARLGSEVT 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 180 LIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYE----GLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWL- 254
Cdd:COG1249   196 LVERGDRLLPGE-DPEISEALEKALEKEGIDILTGAKVTSVEktgdGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLg 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 255 --RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATVARREARYVAEHIFENTPsipfsgvvgss 332
Cdd:COG1249   275 leAAGVELDERGGIKVDEYLRTSVPGIYAIGDVT----------GGPQLAHVASAEGRVAAENILGKKP----------- 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 333 alSVFDYHF-----------ATSGLNMTTAQKADIEIHTSFYKdtLRPAYVPMEKGNTEVYVELDYNPNTHQLLGGAVLS 401
Cdd:COG1249   334 --RPVDYRAipsvvftdpeiASVGLTEEEAREAGIDVKVGKFP--FAANGRALALGETEGFVKLIADAETGRILGAHIVG 409

                         330       340
                  ....*....|....*....|....*..
gi 1215925580 402 TyDITAQGNVISLAIQQGLKLEDLAEA 428
Cdd:COG1249   410 P-HAGELIHEAALAMEMGLTVEDLADT 435
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
3-316 3.15e-42

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 153.75  E-value: 3.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   3 KTKVIVVGASHGGHQSVLELTHKY-SDLDIKLFEAGDFISFMscGMeLY--LENSVTNVNDVRNFKPAdLEKLGTEVYAN 79
Cdd:COG1252     1 MKRIVIVGGGFAGLEAARRLRKKLgGDAEVTLIDPNPYHLFQ--PL-LPevAAGTLSPDDIAIPLREL-LRRAGVRFIQG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  80 hEVTKINPENKQVIVKDlksGkiQSYDYDKLILSSGVTPNNLPVPGHElKNVYSMRGKDWAEKIKAKL-------SDPNV 152
Cdd:COG1252    77 -EVTGIDPEARTVTLAD---G--RTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDALALRERLlaaferaERRRL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAA------------EASIKAGK-NVTLIDMINRPLGNyLDTELTDILSKELTNKGVQVVTGAKIES 219
Cdd:COG1252   150 LTIVVVGGGPTGVELAgelaellrkllrYPGIDPDKvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTE 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 220 YEGleavSAVKTSDAE-YPSDLIIQAAGVKPNtDWLRGT-VELDKRGWIKTDKYLRT-NLPDVYAIGDAVlaySIPAQKD 296
Cdd:COG1252   229 VDA----DGVTLEDGEeIPADTVIWAAGVKAP-PLLADLgLPTDRRGRVLVDPTLQVpGHPNVFAIGDCA---AVPDPDG 300

                         330       340
                  ....*....|....*....|.
gi 1215925580 297 MPIA-LATVARREARYVAEHI 316
Cdd:COG1252   301 KPVPkTAQAAVQQAKVLAKNI 321
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 90-428 3.34e-34

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 133.15  E-value: 3.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  90 KQVIVKDlkSGKIQSYDYDKLILSSGVTPNNLPVP-GHELKNVYSMRGKdwaekikakLSDPNV-KNITVIGAGYIGIEA 167
Cdd:TIGR01350 117 GTVSVTG--ENGEETLEAKNIIIATGSRPRSLPGPfDFDGKVVITSTGA---------LNLEEVpESLVIIGGGVIGIEF 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 168 AEASIKAGKNVTLIDMINRPLGNyLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAE---YPSDLIIQA 244
Cdd:TIGR01350 186 ASIFASLGSKVTVIEMLDRILPG-EDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGEtetLTGEKVLVA 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 245 AGVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATVARREARYVAEHIFENTP 321
Cdd:TIGR01350 265 VGRKPNTEGLgleKLGVELDERGRIVVDEYMRTNVPGIYAIGDVI----------GGPMLAHVASHEGIVAAENIAGKEP 334

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 322 SIPFSGVVGSSALSvfDYHFATSGLNMTTAQKADIEIHTSFYKDTLRPAYVPMekGNTEVYVELDYNPNTHQLLGGAVL- 400
Cdd:TIGR01350 335 AHIDYDAVPSVIYT--DPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALAL--GETDGFVKIIADKKTGEILGAHIIg 410

                         330       340
                  ....*....|....*....|....*....
gi 1215925580 401 -STYDITAQgnvISLAIQQGLKLEDLAEA 428
Cdd:TIGR01350 411 pHATELISE---AALAMELEGTVEELART 436
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
75-294 1.49e-33

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 130.04  E-value: 1.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  75 EVYANHEVTKINPENKQVIVKDlksgkiQSYDYDKLILSSGVTPNNLPVPGHELknVYSMRGKDWAEKIKAKLSDpnVKN 154
Cdd:PRK04965   74 RLFPHTWVTDIDAEAQVVKSQG------NQWQYDKLVLATGASAFVPPIPGREL--MLTLNSQQEYRAAETQLRD--AQR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 155 ITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLE-AVSAVKTSD 233
Cdd:PRK04965  144 VLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDsGIRATLDSG 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 234 AEYPSDLIIQAAGVKPNTDWLRG---TVEldkRGwIKTDKYLRTNLPDVYAIGDA------VLAYSIPAQ 294
Cdd:PRK04965  224 RSIEVDAVIAAAGLRPNTALARRaglAVN---RG-IVVDSYLQTSAPDIYALGDCaeingqVLPFLQPIQ 289
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 6-358 1.71e-32

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 131.10  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   6 VIVVGASHGGHQSVLELTHKYSD-LDIKLFEAGDFISFMSCGMELYLENSvTNVNDVRNFKPADLEKLGTEVYANHEVTK 84
Cdd:TIGR02374   1 LVLVGNGMAGHRCIEEVLKLNRHmFEITIFGEEPHPNYNRILLSSVLQGE-ADLDDITLNSKDWYEKHGITLYTGETVIQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  85 INPENKQVIVKdlkSGKIQSYDydKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAklSDPNVKNITVIGAGYIG 164
Cdd:TIGR02374  80 IDTDQKQVITD---AGRTLSYD--KLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMA--MAQRFKKAAVIGGGLLG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 165 IEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSD-AEYPSDLIIQ 243
Cdd:TIGR02374 153 LEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDgSSLEADLIVM 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 244 AAGVKPNTDwLRGTVELDKRGWIKTDKYLRTNLPDVYAIGDavlaysIPAQKDMPIALATVARREARYVAEHIFeNTPSI 323
Cdd:TIGR02374 233 AAGIRPNDE-LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGE------CAEHNGRVYGLVAPLYEQAKVLADHIC-GVECE 304

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1215925580 324 PFSGVVGSSALSVFDYHFATSGLNMTTAQKADIEI 358
Cdd:TIGR02374 305 EYEGSDLSAKLKLLGVDVWSAGDAQETERTTSIKI 339
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 153-427 2.18e-27

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 113.73  E-value: 2.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNyLDTELTDILSKELtNKGVQVVTGAKIESYE---GLEAVSAV 229
Cdd:PRK06292  170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL-EDPEVSKQAQKIL-SKEFKIKLGAKVTSVEksgDEKVEELE 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 230 KTSDAEY-PSDLIIQAAGVKPNTDWLR---GTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqKDMPiaLATVA 305
Cdd:PRK06292  248 KGGKTETiEADYVLVATGRRPNTDGLGlenTGIELDERGRPVVDEHTQTSVPGIYAAGDVN--------GKPP--LLHEA 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 306 RREARYVAEHIFEN---------TPSIPFS----GVVGSS--ALsvfdyhfatsglnmtTAQKADIEIHTSFYKDTLRpA 370
Cdd:PRK06292  318 ADEGRIAAENAAGDvaggvryhpIPSVVFTdpqiASVGLTeeEL---------------KAAGIDYVVGEVPFEAQGR-A 381

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1215925580 371 YVpM--EKGNTEVYVEldynPNTHQLLGGAVLStydITAQ--GNVISLAIQQGLKLEDLAE 427
Cdd:PRK06292  382 RV-MgkNDGFVKVYAD----KKTGRLLGAHIIG---PDAEhlIHLLAWAMQQGLTVEDLLR 434
PRK06370 PRK06370
FAD-containing oxidoreductase;
157-428 1.41e-26

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 111.45  E-value: 1.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEY 236
Cdd:PRK06370  176 IIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDCNGG 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 237 PSDL----IIQAAGVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAvlaysipaqkDMPIALATVARREA 309
Cdd:PRK06370  255 APEItgshILVAVGRVPNTDDLgleAAGVETDARGYIKVDDQLRTTNPGIYAAGDC----------NGRGAFTHTAYNDA 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 310 RYVAEHIFENTPS------IPFsgvvgssalSVF-DYHFATSGLNMTTAQKADIEIhtsfykDTLRpayVPM-------E 375
Cdd:PRK06370  325 RIVAANLLDGGRRkvsdriVPY---------ATYtDPPLARVGMTEAEARKSGRRV------LVGT---RPMtrvgravE 386

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215925580 376 KGNTEVYVELDYNPNTHQLLGGAVLSTYditaqG----NVISLAIQQGLKLEDLAEA 428
Cdd:PRK06370  387 KGETQGFMKVVVDADTDRILGATILGVH-----GdemiHEILDAMYAGAPYTTLSRA 438
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 153-426 5.55e-24

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 104.07  E-value: 5.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYE----GLEAVSA 228
Cdd:PRK06416  173 KSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGE-DKEISKLAERALKKRGIKIKTGAKAKKVEqtddGVTVTLE 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 229 VKTSDAEYPSDLIIQAAGVKPNTDWL----RGtVELDkRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATV 304
Cdd:PRK06416  252 DGGKEETLEADYVLVAVGRRPNTENLgleeLG-VKTD-RGFIEVDEQLRTNVPNIYAIGDIV----------GGPMLAHK 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 305 ARREARYVAEHIFENTPSIPFSGVVGssalSVF-DYHFATSGLNMTTAQKADIEIHTSFYkdtlrpayvPMeKGN----- 378
Cdd:PRK06416  320 ASAEGIIAAEAIAGNPHPIDYRGIPA----VTYtHPEVASVGLTEAKAKEEGFDVKVVKF---------PF-AGNgkala 385

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1215925580 379 ---TEVYVELDYNPNTHQLLG----GAVLStyDITAQgnvISLAIQQGLKLEDLA 426
Cdd:PRK06416  386 lgeTDGFVKLIFDKKDGEVLGahmvGARAS--ELIQE---AQLAINWEATPEDLA 435
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
70-286 3.70e-23

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 99.04  E-value: 3.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  70 EKLGTEVYaNHEVTKINPENKQVIVKDLKSGKIQSydyDKLILSSGVTPNNLPVPGHEL---KNVYS--------MRGKD 138
Cdd:COG0492    68 ERFGAEIL-LEEVTSVDKDDGPFRVTTDDGTEYEA---KAVIIATGAGPRKLGLPGEEEfegRGVSYcatcdgffFRGKD 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 139 waekikaklsdpnvknITVIGAGYIGIEAAEASIKAGKNVTLIdmINRPlgnylDTELTDILSKEL-TNKGVQVVTGAKI 217
Cdd:COG0492   144 ----------------VVVVGGGDSALEEALYLTKFASKVTLI--HRRD-----ELRASKILVERLrANPKIEVLWNTEV 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215925580 218 ESYEGLEAVSAVKTSDA------EYPSDLIIQAAGVKPNTDWLRGT-VELDKRGWIKTDKYLRTNLPDVYAIGDAV 286
Cdd:COG0492   201 TEIEGDGRVEGVTLKNVktgeekELEVDGVFVAIGLKPNTELLKGLgLELDEDGYIVVDEDMETSVPGVFAAGDVR 276
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 69-316 7.53e-23

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 100.21  E-value: 7.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  69 LEKLGTEVYANHEVTKinpenkQVIVKDLKSgkiqsyDYDKLILSSGVT-PNNLPVPGHELKNVYSmrGKDWAEKI-KAK 146
Cdd:COG0493   181 IEALGVEFRTNVEVGK------DITLDELLE------EFDAVFLATGAGkPRDLGIPGEDLKGVHS--AMDFLTAVnLGE 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 147 LSDPNV---KNITVIGAGYIGIEAAEASIKAG-KNVTLIDMinRPLGN--YLDTELTDilSKEltnKGVQVVTGAKIESY 220
Cdd:COG0493   247 APDTILavgKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--RTREEmpASKEEVEE--ALE---EGVEFLFLVAPVEI 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 221 EGLE--AVSAVKT---------------------SDAEYPSDLIIQAAGVKPNTDWLRGT--VELDKRGWIKTDK-YLRT 274
Cdd:COG0493   320 IGDEngRVTGLECvrmelgepdesgrrrpvpiegSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEeTYQT 399

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1215925580 275 NLPDVYAIGDAVLAYSipaqkdmpiaLATVARREARYVAEHI 316
Cdd:COG0493   400 SLPGVFAGGDAVRGPS----------LVVWAIAEGRKAARAI 431
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
153-320 4.61e-21

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 95.22  E-value: 4.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAeaSIKA--GKNVTLIDMINRPLGnYLDTELTDILSKELTNKGVQVVTGAKIESYEGLE-AVSAV 229
Cdd:PRK05249  176 RSLIIYGAGVIGCEYA--SIFAalGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDdGVIVH 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 230 KTSDAEYPSDLIIQAAGVKPNTDWLR----GtVELDKRGWIKTDKYLRTNLPDVYAIGDaVLAYsiPaqkdmpiALATVA 305
Cdd:PRK05249  253 LKSGKKIKADCLLYANGRTGNTDGLNlenaG-LEADSRGQLKVNENYQTAVPHIYAVGD-VIGF--P-------SLASAS 321

                         170
                  ....*....|....*
gi 1215925580 306 RREARYVAEHIFENT 320
Cdd:PRK05249  322 MDQGRIAAQHAVGEA 336
PRK06116 PRK06116
glutathione reductase; Validated
 153-326 1.07e-20

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 94.07  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVS-AVKT 231
Cdd:PRK06116  168 KRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGF-DPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSlTLTL 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 232 SDAE-YPSDLIIQAAGVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVLAysipaqkdmpIALATVARR 307
Cdd:PRK06116  247 EDGEtLTVDCLIWAIGREPNTDGLgleNAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGR----------VELTPVAIA 316

                         170
                  ....*....|....*....
gi 1215925580 308 EARYVAEHIFENTPSIPFS 326
Cdd:PRK06116  317 AGRRLSERLFNNKPDEKLD 335
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 1-287 5.95e-18

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 85.36  E-value: 5.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   1 MSKTKVIVVGASHGGHQSVLELTHKYSDLDIKLFeagdfisfmscGMELYL--ENSVTNVNDVRNFKPADLEKLGTEVYA 78
Cdd:PRK09754    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLF-----------SDERHLpyERPPLSKSMLLEDSPQLQQVLPANWWQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  79 NHE--------VTKINPENKQVIvkdLKSGkiQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIKAKLSDP 150
Cdd:PRK09754   70 ENNvhlhsgvtIKTLGRDTRELV---LTNG--ESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 151 nvKNITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVK 230
Cdd:PRK09754  145 --RSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTL 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1215925580 231 TSDAEYPSDLIIQAAGVKPNtDWLRGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVL 287
Cdd:PRK09754  223 QSGETLQADVVIYGIGISAN-DQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAI 278
PRK07251 PRK07251
FAD-containing oxidoreductase;
108-284 8.10e-18

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 85.19  E-value: 8.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 108 DKLILSSGVTPNNLPVPG-HELKNVYSMRGKDWAEKIKAKLSdpnvknitVIGAGYIGIEAAEASIKAGKNVTLIDMINR 186
Cdd:PRK07251  120 ETIVINTGAVSNVLPIPGlADSKHVYDSTGIQSLETLPERLG--------IIGGGNIGLEFAGLYNKLGSKVTVLDAAST 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 187 PLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWL---RGTVELDKR 263
Cdd:PRK07251  192 ILPRE-EPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLgleNTDIELTER 270

                         170       180
                  ....*....|....*....|.
gi 1215925580 264 GWIKTDKYLRTNLPDVYAIGD 284
Cdd:PRK07251  271 GAIKVDDYCQTSVPGVFAVGD 291
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 1-284 1.07e-17

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 85.94  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   1 MSKTKVIVVGASHGGHQSVLELTHK--YSDLDIKLFEAGDFISFMSCGMELYLenSVTNVNDVRNFKPADLEKLGTEVYA 78
Cdd:PRK14989    1 MSKVRLAIIGNGMVGHRFIEDLLDKadAANFDITVFCEEPRIAYDRVHLSSYF--SHHTAEELSLVREGFYEKHGIKVLV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  79 NHEVTKINPENKQVIvkdlkSGKIQSYDYDKLILSSGVTPNNLPVPGHELKNVYSMRGKDWAEKIK--AKLSdpnvKNIT 156
Cdd:PRK14989   79 GERAITINRQEKVIH-----SSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEacARRS----KRGA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIES--YEGLEAVSAVKTSD- 233
Cdd:PRK14989  150 VVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEivQEGVEARKTMRFADg 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1215925580 234 AEYPSDLIIQAAGVKPNtDWLRGTVELD--KRGWIKTDKYLRTNLPDVYAIGD 284
Cdd:PRK14989  230 SELEVDFIVFSTGIRPQ-DKLATQCGLAvaPRGGIVINDSCQTSDPDIYAIGE 281
PLN02507 PLN02507
glutathione reductase
 100-324 1.63e-16

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 81.79  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 100 GKIQSYDYDKLILSSGVTPNNLPVPGHELknvysmrgkdwaekikAKLSDPNV------KNITVIGAGYIGIEAAeaSIK 173
Cdd:PLN02507  161 GTKLRYTAKHILIATGSRAQRPNIPGKEL----------------AITSDEALsleelpKRAVVLGGGYIAVEFA--SIW 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 174 AGKNVTlIDMINR---PLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDA-EYPSDLIIQAAGVKP 249
Cdd:PLN02507  223 RGMGAT-VDLFFRkelPLRGF-DDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGeEFVADVVLFATGRAP 300

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215925580 250 NTDWLR---GTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATVARREARYVAEHIFENTPSIP 324
Cdd:PLN02507  301 NTKRLNleaVGVELDKAGAVKVDEYSRTNIPSIWAIGDVT----------NRINLTPVALMEGTCFAKTVFGGQPTKP 368
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 77-325 4.20e-16

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 79.81  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  77 YANHEVTKINPENKQVIVKDLKSG-----KIQSYDYDKLILSSGVTPNNLPVPGHElKNVYSMRGKDWAEKIKAKL---- 147
Cdd:PTZ00318   79 YLRAVVYDVDFEEKRVKCGVVSKSnnanvNTFSVPYDKLVVAHGARPNTFNIPGVE-ERAFFLKEVNHARGIRKRIvqci 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 148 ---SDPNVK--------NITVIGAGYIGIE-AAE-------------ASIKAGKNVTLIDMINRPLGNYlDTELTDILSK 202
Cdd:PTZ00318  158 eraSLPTTSveerkrllHFVVVGGGPTGVEfAAEladffrddvrnlnPELVEECKVTVLEAGSEVLGSF-DQALRKYGQR 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 203 ELTNKGVQVVTGAKIEsyEGLEAVSAVKTSDaEYPSDLIIQAAGVKPNTDWLRGTVELDKRGWIKTDKYLRT-NLPDVYA 281
Cdd:PTZ00318  237 RLRRLGVDIRTKTAVK--EVLDKEVVLKDGE-VIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDHLRVkPIPNVFA 313

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1215925580 282 IGDAVLAYSIPaqkdMPiALATVARREARYVAEHI---FENTP-SIPF 325
Cdd:PTZ00318  314 LGDCAANEERP----LP-TLAQVASQQGVYLAKEFnneLKGKPmSKPF 356
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 154-233 6.98e-16

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 72.24  E-value: 6.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 154 NITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLgNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSD 233
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 88-330 8.02e-16

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 79.63  E-value: 8.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  88 ENKQVIV----KDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHEL-----KNVYsmrgkdwaekikakLSDPNVKNITVi 158
Cdd:TIGR01423 129 EDKNVVLvresADPKSAVKERLQAEHILLATGSWPQMLGIPGIEHcissnEAFY--------------LDEPPRRVLTV- 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 159 GAGYIGIEAA---EASIKAGKNVTLI---DMINRPLgnylDTELTDILSKELTNKGVQVVTG---AKIE-SYEGLEAVsa 228
Cdd:TIGR01423 194 GGGFISVEFAgifNAYKPRGGKVTLCyrnNMILRGF----DSTLRKELTKQLRANGINIMTNenpAKVTlNADGSKHV-- 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 229 VKTSDAEYPSDLIIQAAGVKPNTDWLR---GTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATVA 305
Cdd:TIGR01423 268 TFESGKTLDVDVVMMAIGRVPRTQTLQldkVGVELTKKGAIQVDEFSRTNVPNIYAIGDVT----------DRVMLTPVA 337

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1215925580 306 RREARYVAEHIFENTP-------------SIPFSGVVG 330
Cdd:TIGR01423 338 INEGAAFVDTVFGNKPrktdhtrvasavfSIPPIGTCG 375
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 153-328 6.56e-15

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 76.50  E-value: 6.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGnYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTS 232
Cdd:PRK06327  184 KKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLA-AADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYT 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 233 DAE-----YPSDLIIQAAGVKPNTDWLRGT---VELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaQKDMpiaLATV 304
Cdd:PRK06327  263 DADgeaqtLEVDKLIVSIGRVPNTDGLGLEavgLKLDERGFIPVDDHCRTNVPNVYAIGDVV-------RGPM---LAHK 332

                         170       180
                  ....*....|....*....|....
gi 1215925580 305 ARREARYVAEHIFENTPSIPFSGV 328
Cdd:PRK06327  333 AEEEGVAVAERIAGQKGHIDYNTI 356
PTZ00058 PTZ00058
glutathione reductase; Provisional
 146-297 1.18e-14

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 76.19  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 146 KLSDPnvKNITVIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEA 225
Cdd:PTZ00058  233 KIKEA--KRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKF-DETIINELENDMKKNNINIITHANVEEIEKVKE 309

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1215925580 226 ---VSAVKTSDAEYPSDLIIQAAGVKPNTDWL--RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVLAYSIPAQKDM 297
Cdd:PTZ00058  310 knlTIYLSDGRKYEHFDYVIYCVGRSPNTEDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEIEDL 386
PRK07846 PRK07846
mycothione reductase; Reviewed
 157-435 3.93e-14

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 74.22  E-value: 3.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNyLDTELTDILSkELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAE- 235
Cdd:PRK07846  171 IVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRH-LDDDISERFT-ELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSt 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 236 YPSDLIIQAAGVKPNTDWLR---GTVELDKRGWIKTDKYLRTNLPDVYAIGDAvlaySIPAQkdmpiaLATVARREARYV 312
Cdd:PRK07846  249 VEADVLLVATGRVPNGDLLDaaaAGVDVDEDGRVVVDEYQRTSAEGVFALGDV----SSPYQ------LKHVANHEARVV 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 313 AEHIFENTPSIPFSGVVGSSAlsVF-DYHFATSGLNMTTAQKADIEIHTSF--YKDTlrpAY-VPMEkgNTEVYVELDYN 388
Cdd:PRK07846  319 QHNLLHPDDLIASDHRFVPAA--VFtHPQIASVGLTENEARAAGLDITVKVqnYGDV---AYgWAME--DTTGFVKLIAD 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1215925580 389 PNTHQLLGGAVlstydITAQGNVIslaIQQ-------GLKLEDLAEADFFFQPG 435
Cdd:PRK07846  392 RDTGRLLGAHI-----IGPQASTL---IQPliqamsfGLDAREMARGQYWIHPA 437
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 69-286 5.70e-13

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 70.59  E-value: 5.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  69 LEKLGTEVYANHEVTKInpenkqVIVKDLKSGkiqsydYDKLILSSGVT-PNNLPVPGHELKNVYSmrgkdwA-EKIKA- 145
Cdd:PRK11749  200 LLKLGVEIRTNTEVGRD------ITLDELRAG------YDAVFIGTGAGlPRFLGIPGENLGGVYS------AvDFLTRv 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 146 ----KLSDPNV-KNITVIGAGYIGIEAAEASIKAG-KNVTLI------DMINR-------------------PLGnyldt 194
Cdd:PRK11749  262 nqavADYDLPVgKRVVVIGGGNTAMDAARTAKRLGaESVTIVyrrgreEMPASeeevehakeegvefewlaaPVE----- 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 195 eltdILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWLRGT--VELDKRGWIKTD-KY 271
Cdd:PRK11749  337 ----ILGDEGRVTGVEFVRMELGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTpgLELNRWGTIIADdET 412

                         250
                  ....*....|....*
gi 1215925580 272 LRTNLPDVYAIGDAV 286
Cdd:PRK11749  413 GRTSLPGVFAGGDIV 427
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 157-284 5.60e-12

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 67.35  E-value: 5.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTLIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAEY 236
Cdd:PRK08010  163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQL 241

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1215925580 237 PSDLIIQAAGVKPNTDWLR---GTVELDKRGWIKTDKYLRTNLPDVYAIGD 284
Cdd:PRK08010  242 AVDALLIASGRQPATASLHpenAGIAVNERGAIVVDKYLHTTADNIWAMGD 292
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
 84-425 1.09e-11

thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.


Pssm-ID: 273624 [Multi-domain]  Cd Length: 484  Bit Score: 66.41  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  84 KINPEN-------KQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGHElknVYSMRGKDwaekIKAKLSDPNvkNIT 156
Cdd:TIGR01438 114 KVKYENayaefvdKHRIKATNKKGKEKIYSAERFLIATGERPRYPGIPGAK---ELCITSDD----LFSLPYCPG--KTL 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTLidMINRPLGNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDA-- 234
Cdd:TIGR01438 185 VVGASYVALECAGFLAGIGLDVTV--MVRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDStn 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 235 ----EYpsDLIIQAAGVKPNTDWL---RGTVELDKR-GWIKTDKYLRTNLPDVYAIGDAVlaysipaqKDMPiALATVAR 306
Cdd:TIGR01438 263 gieeEY--DTVLLAIGRDACTRKLnleNVGVKINKKtGKIPADEEEQTNVPYIYAVGDIL--------EDKP-ELTPVAI 331

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 307 REARYVAEHIFENTPSI-PFSGVvgssALSVFD-YHFATSGLNMTTA----QKADIEIHTSFYkdTLRPAYVPMEKGNTE 380
Cdd:TIGR01438 332 QAGRLLAQRLFKGSTVIcDYENV----PTTVFTpLEYGACGLSEEKAvekfGEENVEVFHSYF--WPLEWTIPSRDNHNK 405

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1215925580 381 VYVELDYNPNTHQ-LLGGAVL--STYDITaQGnvISLAIQQGLKLEDL 425
Cdd:TIGR01438 406 CYAKLVCNKKENErVVGFHVVgpNAGEVT-QG--FAAALRCGLTKKDL 450
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 68-318 1.90e-11

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 65.01  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  68 DLEKLG------TEVYANHEVTKinpENKQVIVKDLKS-GKIQSyDYDKLILSSGV-TPNNLPVPGHELKNVYSmrGKDW 139
Cdd:PRK12770   77 ELEEAGvvfhtrTKVCCGEPLHE---EEGDEFVERIVSlEELVK-KYDAVLIATGTwKSRKLGIPGEDLPGVYS--ALEY 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 140 AEKIKA---------KLSDPNVKNITVIGAGYIGIEAAEASIKAGknVTLIDMINR------PLGNYldtELtdilsKEL 204
Cdd:PRK12770  151 LFRIRAaklgylpweKVPPVEGKKVVVVGAGLTAVDAALEAVLLG--AEKVYLAYRrtineaPAGKY---EI-----ERL 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 205 TNKGVQ---VVTGAKIESYEGLEAVSAVKT------------------SDAEYPSDLIIQAAGVKPnTDWLRGT---VEL 260
Cdd:PRK12770  221 IARGVEfleLVTPVRIIGEGRVEGVELAKMrlgepdesgrprpvpipgSEFVLEADTVVFAIGEIP-TPPFAKEclgIEL 299

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1215925580 261 DKRGWIKTDKYLRTNLPDVYAIGDAVLAYSIpaqkdmpIALATvarREARYVAEHIFE 318
Cdd:PRK12770  300 NRKGEIVVDEKHMTSREGVFAAGDVVTGPSK-------IGKAI---KSGLRAAQSIHE 347
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 153-285 1.96e-11

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 65.95  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAeasIK-AG--KNVTLIDminrplgnyLDTELT--DILS---KELTNkgVQVVTGAKIESYEG-L 223
Cdd:PRK15317  352 KRVAVIGGGNSGVEAA---IDlAGivKHVTVLE---------FAPELKadQVLQdklRSLPN--VTIITNAQTTEVTGdG 417

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1215925580 224 EAVSAVKTSDAEYPSDLIIQAAGV------KPNTDWLRGTVELDKRGWIKTDKYLRTNLPDVYAIGDA 285
Cdd:PRK15317  418 DKVTGLTYKDRTTGEEHHLELEGVfvqiglVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDC 485
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 69-286 2.30e-11

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 65.57  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  69 LEKLGTEVYANHEVTK-INPEnkqvivkDLKSgkiqsyDYDKLILSSGVT-PNNLPVPGHELKNVY-----------SMR 135
Cdd:PRK12810  203 MEAEGIEFRTNVEVGKdITAE-------ELLA------EYDAVFLGTGAYkPRDLGIPGRDLDGVHfamdfliqntrRVL 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 136 GKDWAEKIKAKlsdpnVKNITVIGAGYIGIEAAEASIKAG-KNVTLIDMINRP--LGNYLDTELTDILSKELTN---KGV 209
Cdd:PRK12810  270 GDETEPFISAK-----GKHVVVIGGGDTGMDCVGTAIRQGaKSVTQRDIMPMPpsRRNKNNPWPYWPMKLEVSNaheEGV 344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 210 QVVTGAKIESYEG----LEAVSAVKT------------SDAEYPSDLIIQAAG-VKPNTDWLR-GTVELDKRGWIK-TDK 270
Cdd:PRK12810  345 EREFNVQTKEFEGengkVTGVKVVRTelgegdfepvegSEFVLPADLVLLAMGfTGPEAGLLAqFGVELDERGRVAaPDN 424

                         250
                  ....*....|....*.
gi 1215925580 271 YLRTNLPDVYAIGDAV 286
Cdd:PRK12810  425 AYQTSNPKVFAAGDMR 440
PRK13748 PRK13748
putative mercuric reductase; Provisional
 88-430 4.46e-11

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 64.79  E-value: 4.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  88 ENKQVIVKDLKSGKIQSYDYDKLILSSGVTPNNLPVPGhelknvysMRGKDWAEKIKAKLSDPNVKNITVIGAGYIGIEA 167
Cdd:PRK13748  214 KDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPG--------LKETPYWTSTEALVSDTIPERLAVIGSSVVALEL 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 168 AEASIKAGKNVTLidMINRPLGNYLDTELTDILSKELTNKGVQVV--TGAKIESYEGLEAVsaVKTSDAEYPSDLIIQAA 245
Cdd:PRK13748  286 AQAFARLGSKVTI--LARSTLFFREDPAIGEAVTAAFRAEGIEVLehTQASQVAHVDGEFV--LTTGHGELRADKLLVAT 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 246 GVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkDMP--IALATVARREAryvaehifent 320
Cdd:PRK13748  362 GRAPNTRSLaldAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCT---------DQPqfVYVAAAAGTRA----------- 421

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 321 pSIPFSGvvGSSALS-------VF-DYHFATSGLNMTTAQKADIEIHTSfykdTLRPAYVPMEKGN--TEVYVELDYNPN 390
Cdd:PRK13748  422 -AINMTG--GDAALDltampavVFtDPQVATVGYSEAEAHHDGIETDSR----TLTLDNVPRALANfdTRGFIKLVIEEG 494

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1215925580 391 THQLLGGAVLStydiTAQGNVI---SLAIQQGLKLEDLAEADF 430
Cdd:PRK13748  495 SGRLIGVQAVA----PEAGELIqtaALAIRNRMTVQELADQLF 533
PLN02546 PLN02546
glutathione reductase
 153-396 6.38e-09

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 57.96  E-value: 6.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGAGYIGIEAAeaSIKAGKNVTLIDMI-NRPLGNYLDTELTDILSKELTNKGVQVVTG----AKIESYEGLEAVS 227
Cdd:PLN02546  253 EKIAIVGGGYIALEFA--GIFNGLKSDVHVFIrQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEespqAIIKSADGSLSLK 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 228 AVKTSDAEYPSdlIIQAAGVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGDAVlaysipaqkdMPIALATV 304
Cdd:PLN02546  331 TNKGTVEGFSH--VMFATGRKPNTKNLgleEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVT----------DRINLTPV 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 305 ARREARYVAEHIFENTPSIPFSGVVGSSALSvfDYHFATSGLNMTTA--QKADIEIHTSFYkdtlRPAYVPMEKGNTEVY 382
Cdd:PLN02546  399 ALMEGGALAKTLFGNEPTKPDYRAVPSAVFS--QPPIGQVGLTEEQAieEYGDVDVFTANF----RPLKATLSGLPDRVF 472

                         250
                  ....*....|....
gi 1215925580 383 VELDYNPNTHQLLG 396
Cdd:PLN02546  473 MKLIVCAKTNKVLG 486
PRK12831 PRK12831
putative oxidoreductase; Provisional
 67-286 1.62e-08

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 56.56  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  67 ADLEKLGTEVYANHEVtkinpeNKQVIVKDLksgkIQSYDYDKLILSSGV-TPNNLPVPGHELKNVYS----------MR 135
Cdd:PRK12831  199 ENIKKLGVKIETNVVV------GKTVTIDEL----LEEEGFDAVFIGSGAgLPKFMGIPGENLNGVFSanefltrvnlMK 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 136 --GKDWAEKIKAKlsdpnvKNITVIGAGYIGIEAAEASIKAGKNVTLI------DMINR--------PLGNYLD--TELT 197
Cdd:PRK12831  269 ayKPEYDTPIKVG------KKVAVVGGGNVAMDAARTALRLGAEVHIVyrrseeELPARveevhhakEEGVIFDllTNPV 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 198 DILSKEltNKGVQVVTGAKIESYE----GLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWLRGT--VELDKRGWIKTDK- 270
Cdd:PRK12831  343 EILGDE--NGWVKGMKCIKMELGEpdasGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTkgLKINKRGCIVADEe 420

                         250
                  ....*....|....*.
gi 1215925580 271 YLRTNLPDVYAIGDAV 286
Cdd:PRK12831  421 TGLTSKEGVFAGGDAV 436
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 93-305 3.53e-08

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 55.64  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  93 IVKDLKSGKIQSYDYDKLILSSGVTPNNLP--VPGHE----LKNVYSMrgkdwaEKIKAKLsdpnvkniTVIGAGYIGIE 166
Cdd:PRK07845  126 VKVTTADGGEETLDADVVLIATGASPRILPtaEPDGEriltWRQLYDL------DELPEHL--------IVVGSGVTGAE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 167 AAEASIKAGKNVTLIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVKTSDAE--YPSDLIIqA 244
Cdd:PRK07845  192 FASAYTELGVKVTLVSSRDRVLPGE-DADAAEVLEEVFARRGMTVLKRSRAESVERTGDGVVVTLTDGRtvEGSHALM-A 269

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1215925580 245 AGVKPNTDWL---RGTVELDKRGWIKTDKYLRTNLPDVYAIGD--AVLaysipaqkdmpiALATVA 305
Cdd:PRK07845  270 VGSVPNTAGLgleEAGVELTPSGHITVDRVSRTSVPGIYAAGDctGVL------------PLASVA 323
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 5-319 2.24e-06

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 50.13  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580   5 KVIVVGASHGGHQSVLELTHKysDLDIKLFEA----GDFISFmscGM-ELYLENSVTNVnDVRNfkpadLEKLGTEVYAN 79
Cdd:PRK12778  433 KVAVIGSGPAGLSFAGDLAKR--GYDVTVFEAlheiGGVLKY---GIpEFRLPKKIVDV-EIEN-----LKKLGVKFETD 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  80 HEVtkinpeNKQVIVKDLKSGKiqsydYDKLILSSGV-TPNNLPVPGHELKNVYS----------MRG--KDWAEKIKAK 146
Cdd:PRK12778  502 VIV------GKTITIEELEEEG-----FKGIFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlMDAasPDSDTPIKFG 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 147 lsdpnvKNITVIGAGYIGIEAAEASIKAG-KNVTLI------DMINRpLGNYLDTELTDILSKELTN--------KG-VQ 210
Cdd:PRK12778  571 ------KKVAVVGGGNTAMDSARTAKRLGaERVTIVyrrseeEMPAR-LEEVKHAKEEGIEFLTLHNpieyladeKGwVK 643

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 211 VVTGAKIESYE----GLEAVSAVKTSDAEYPSDLIIQAAGVKPNTDWLRGT--VELDKRGWIKTDKYLRTNLPDVYAIGD 284
Cdd:PRK12778  644 QVVLQKMELGEpdasGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIpgLELNRKGTIVVDEEMQSSIPGIYAGGD 723

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1215925580 285 AVL--AYSIPAQKDmpialatvARREARYVAEHIFEN 319
Cdd:PRK12778  724 IVRggATVILAMGD--------GKRAAAAIDEYLSSK 752
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
 93-326 3.52e-06

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 49.53  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  93 IVKDLKSGKiqSYDYDKLILSSGVTPNnlpVPGHELKNVYSMRGKDWAEKIkaklsdPNVKN-ITVIGAGYIGIEAAEAS 171
Cdd:PTZ00153  263 TIKSEKSGK--EFKVKNIIIATGSTPN---IPDNIEVDQKSVFTSDTAVKL------EGLQNyMGIVGMGIIGLEFMDIY 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 172 IKAGKNVTLID---------------------MINRPLGNYLDTELTDILSkeltNKGVQVVTGAKIESYEGLEAVSAVK 230
Cdd:PTZ00153  332 TALGSEVVSFEyspqllplldadvakyfervfLKSKPVRVHLNTLIEYVRA----GKGNQPVIIGHSERQTGESDGPKKN 407

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 231 TSDAE--YPSDLIIqAAGVKPNTDWLrGTVELD---KRGWIKTDKYLRTNLPD------VYAIGDA----VLAYSIPAQk 295
Cdd:PTZ00153  408 MNDIKetYVDSCLV-ATGRKPNTNNL-GLDKLKiqmKRGFVSVDEHLRVLREDqevydnIFCIGDAngkqMLAHTASHQ- 484

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1215925580 296 dmpiALATVARREARYVAEH------------IFENTPSIPFS 326
Cdd:PTZ00153  485 ----ALKVVDWIEGKGKENVninvenwaskpiIYKNIPSVCYT 523
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
67-283 4.80e-06

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 47.99  E-value: 4.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580  67 ADLEKLgtEVYANHEVTKINPENKQVIVKDLKsGKIQSydyDKLILSSGV--TPNNLPVPghELKNVYSmRGKDWAekik 144
Cdd:pfam13738  85 ADHFEL--PINLFEEVTSVKKEDDGFVVTTSK-GTYQA---RYVIIATGEfdFPNKLGVP--ELPKHYS-YVKDFH---- 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 145 aklsDPNVKNITVIGAGYIGIEAAEASIKAGKNVTLIDminRplGNYLDTELTD--------ILS--KELTNKG-VQVVT 213
Cdd:pfam13738 152 ----PYAGQKVVVIGGYNSAVDAALELVRKGARVTVLY---R--GSEWEDRDSDpsyslspdTLNrlEELVKNGkIKAHF 222

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1215925580 214 GAKIESYEGLEAVSAVKTSDAEY--PSDLIIQAAGVKPNTDWLR-GTVELDKRGWIK-TDKYLRTNLPDVYAIG 283
Cdd:pfam13738 223 NAEVKEITEVDVSYKVHTEDGRKvtSNDDPILATGYHPDLSFLKkGLFELDEDGRPVlTEETESTNVPGLFLAG 296
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
 336-434 7.53e-06

Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.


Pssm-ID: 427019 [Multi-domain]  Cd Length: 109  Bit Score: 44.85  E-value: 7.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 336 VFDYHFATSGLN--MTTAQKADIEIHTSFYKDTLRPAYVPMEKGntevYVELDYNPNTHQLLGGAVLStYDITAQGNVIS 413
Cdd:pfam02852   6 FTDPEIASVGLTeeEAKEKGGEVKVGKFPFAANGRALAYGDTDG----FVKLVADRETGKILGAHIVG-PNAGELIQEAA 80

                          90       100
                  ....*....|....*....|.
gi 1215925580 414 LAIQQGLKLEDLAEaDFFFQP 434
Cdd:pfam02852  81 LAIKMGATVEDLAN-TIHIHP 100
PRK07819 PRK07819
3-hydroxybutyryl-CoA dehydrogenase; Validated
 157-331 6.65e-04

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181133 [Multi-domain]  Cd Length: 286  Bit Score: 41.51  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTLIDMinrplgnylDTELTDILSKELTNKGVQVVTGAKIESYEGLEAVSAVK-TSDAE 235
Cdd:PRK07819   10 VVGAGQMGAGIAEVCARAGVDVLVFET---------TEELATAGRNRIEKSLERAVSRGKLTERERDAALARLRfTTDLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 236 YPSD--LIIQAAgvkpntdwlrgtVELDKrgwIKTDkyLRTNLPDVYAIGDAVLAY---SIPAQKdmpIALATvaRREAR 310
Cdd:PRK07819   81 DFADrqLVIEAV------------VEDEA---VKTE--IFAELDKVVTDPDAVLASntsSIPIMK---LAAAT--KRPGR 138

                         170       180
                  ....*....|....*....|.
gi 1215925580 311 YVAEHIFENTPSIPFSGVVGS 331
Cdd:PRK07819  139 VLGLHFFNPVPVLPLVELVPT 159
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 157-323 2.36e-03

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 40.19  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 157 VIGAGYIGIEAAEASIKAGKNVTlIDMINRPLGNYlDTELTDILSKELTNKGVQVVTGA---KIESYEGLEAVSAVKTSD 233
Cdd:PTZ00052  187 IVGASYIGLETAGFLNELGFDVT-VAVRSIPLRGF-DRQCSEKVVEYMKEQGTLFLEGVvpiNIEKMDDKIKVLFSDGTT 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 234 AEYpsDLIIQAAGVKPNTDWL---RGTVELDKRGWIKTDKYLrTNLPDVYAIGDAVlaysipaqKDMPiALATVARREAR 310
Cdd:PTZ00052  265 ELF--DTVLYATGRKPDIKGLnlnAIGVHVNKSNKIIAPNDC-TNIPNIFAVGDVV--------EGRP-ELTPVAIKAGI 332

                         170
                  ....*....|...
gi 1215925580 311 YVAEHIFENTPSI 323
Cdd:PTZ00052  333 LLARRLFKQSNEF 345
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 153-259 2.97e-03

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 39.24  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 153 KNITVIGA-GYIGIEAAEASIKAGKNVTLIDMINRPLGNYldteltdilSKELTNK-GVQVVT-GAKIESYEGLEAvsAV 229
Cdd:cd05352     9 KVAIVTGGsRGIGLAIARALAEAGADVAIIYNSAPRAEEK---------AEELAKKyGVKTKAyKCDVSSQESVEK--TF 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1215925580 230 KTSDAEY-PSDLIIQAAGVKPNTDWLRGTVE 259
Cdd:cd05352    78 KQIQKDFgKIDILIANAGITVHKPALDYTYE 108
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 151-245 6.64e-03

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 38.17  E-value: 6.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1215925580 151 NVKNITVIGAGYIGIEAAEASIKAGKNVTLIDM----INRPLgNYLDTELTDILSKELTNKGVQVVTGAKIESYEGLEAV 226
Cdd:COG1250     1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDIspeaLERAR-ARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAAL 79

                          90
                  ....*....|....*....
gi 1215925580 227 SAVktsdaeypsDLIIQAA 245
Cdd:COG1250    80 ADA---------DLVIEAV 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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