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Conserved domains on  [gi|446182249|ref|WP_000260104|]
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MULTISPECIES: dihydrolipoyl dehydrogenase [Bacillus]

Protein Classification

dihydrolipoyl dehydrogenase( domain architecture ID 11482251)

dihydrolipoyl dehydrogenase catalyzes the oxidation of dihydrolipoamide to lipoamide and is often a component of multienzyme 2-oxo-acid dehydrogenase complexes

CATH:  3.50.50.60
EC:  1.8.1.4
Gene Ontology:  GO:0004148|GO:0016491|GO:0050660
PubMed:  8805537|10966480

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
6-468 0e+00

dihydrolipoamide dehydrogenase; Reviewed


:

Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 761.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   6 FPIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDF 85
Cdd:PRK06416   1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TKVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPIEIPGFKYSKRVI- 164
Cdd:PRK06416  81 KKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIILATGSRPRELPGIEIDGRVIw 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 165 NSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGV 244
Cdd:PRK06416 161 TSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRG-IKIKTGAKAKKV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 245 EETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMtDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAH 324
Cdd:PRK06416 240 EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAH 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 325 KASYEGKVAVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTR 404
Cdd:PRK06416 319 KASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIFD 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446182249 405 KEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIHI 468
Cdd:PRK06416 399 KKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
 
Name Accession Description Interval E-value
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
6-468 0e+00

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 761.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   6 FPIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDF 85
Cdd:PRK06416   1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TKVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPIEIPGFKYSKRVI- 164
Cdd:PRK06416  81 KKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIILATGSRPRELPGIEIDGRVIw 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 165 NSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGV 244
Cdd:PRK06416 161 TSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRG-IKIKTGAKAKKV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 245 EETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMtDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAH 324
Cdd:PRK06416 240 EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAH 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 325 KASYEGKVAVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTR 404
Cdd:PRK06416 319 KASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIFD 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446182249 405 KEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIHI 468
Cdd:PRK06416 399 KKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
11-467 0e+00

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: 623.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDFTKVQE 90
Cdd:TIGR01350   3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPIEIPG-FKYS-KRVINSTG 168
Cdd:TIGR01350  83 RKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLPGpFDFDgKVVITSTG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  169 ALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETE 248
Cdd:TIGR01350 163 ALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKG-VKILTNTKVTAVEKND 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  249 TGVKVSFEvKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKASY 328
Cdd:TIGR01350 242 DQVTYENK-GGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  329 EGKVAVEAISG-HASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRKED 407
Cdd:TIGR01350 321 EGIVAAENIAGkEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIADKKT 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  408 GLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIH 467
Cdd:TIGR01350 401 GEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
11-463 0e+00

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: 608.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDFTKVQE 90
Cdd:COG1249    5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWAALMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEdaaQTYTFKNAVLATGSTPIEIPGFKY-SKRVINSTGA 169
Cdd:COG1249   85 RKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGG---ETLTADHIVIATGSRPRVPPIPGLdEVRVLTSDEA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 170 LSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETET 249
Cdd:COG1249  162 LELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEG-IDILTGAKVTSVEKTGD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 250 GVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKASYE 329
Cdd:COG1249  241 GVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 330 GKVAVEAISGHASA-IDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRKEDG 408
Cdd:COG1249  321 GRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIADAETG 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446182249 409 LLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALG 463
Cdd:COG1249  401 RILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
11-330 9.08e-89

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: 273.04  E-value: 9.08e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEkanLGGVCLNVGCIPSKALINAGHRYENAMHsddmgitaenvkvdFTKVQE 90
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASL--------------WADLYK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTlrvmTEDAAQTYTFKNAVLATGSTPI--EIPGFK----YSKRVI 164
Cdd:pfam07992  65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL----VDGDGETITYDRLVIATGARPRlpPIPGVElnvgFLVRTL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  165 NSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGV 244
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNG-VEVRLGTSVKEI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  245 EETETGVKVSFEVKGEIqtvEADYVLVTVGRRPNTQeiGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDI-VPGPPLA 323
Cdd:pfam07992 220 IGDGDGVEVILKDGTEI---DADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGGPELA 294

                  ....*..
gi 446182249  324 HKASYEG 330
Cdd:pfam07992 295 QNAVAQG 301
 
Name Accession Description Interval E-value
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
6-468 0e+00

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 761.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   6 FPIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDF 85
Cdd:PRK06416   1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TKVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPIEIPGFKYSKRVI- 164
Cdd:PRK06416  81 KKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTYTAKNIILATGSRPRELPGIEIDGRVIw 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 165 NSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGV 244
Cdd:PRK06416 161 TSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRG-IKIKTGAKAKKV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 245 EETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMtDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAH 324
Cdd:PRK06416 240 EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAH 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 325 KASYEGKVAVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTR 404
Cdd:PRK06416 319 KASAEGIIAAEAIAGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFDVKVVKFPFAGNGKALALGETDGFVKLIFD 398
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446182249 405 KEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIHI 468
Cdd:PRK06416 399 KKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEALGEAALAAAGKPLHA 462
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
11-467 0e+00

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: 623.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDFTKVQE 90
Cdd:TIGR01350   3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPIEIPG-FKYS-KRVINSTG 168
Cdd:TIGR01350  83 RKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETLEAKNIIIATGSRPRSLPGpFDFDgKVVITSTG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  169 ALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETE 248
Cdd:TIGR01350 163 ALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKG-VKILTNTKVTAVEKND 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  249 TGVKVSFEvKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKASY 328
Cdd:TIGR01350 242 DQVTYENK-GGETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  329 EGKVAVEAISG-HASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRKED 407
Cdd:TIGR01350 321 EGIVAAENIAGkEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVKIIADKKT 400
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  408 GLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIH 467
Cdd:TIGR01350 401 GEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEAIKEAALAALGKPIH 460
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
11-463 0e+00

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: 608.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDFTKVQE 90
Cdd:COG1249    5 DLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWAALMA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEdaaQTYTFKNAVLATGSTPIEIPGFKY-SKRVINSTGA 169
Cdd:COG1249   85 RKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGG---ETLTADHIVIATGSRPRVPPIPGLdEVRVLTSDEA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 170 LSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETET 249
Cdd:COG1249  162 LELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEG-IDILTGAKVTSVEKTGD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 250 GVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKASYE 329
Cdd:COG1249  241 GVTVTLEDGGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 330 GKVAVEAISGHASA-IDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRKEDG 408
Cdd:COG1249  321 GRVAAENILGKKPRpVDYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGFVKLIADAETG 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446182249 409 LLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALG 463
Cdd:COG1249  401 RILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALALLG 455
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
8-468 2.97e-174

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 497.01  E-value: 2.97e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   8 IELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDFTK 87
Cdd:PRK06292   2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFKK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  88 VQEWKNGVVKKLTGGV-EGLLKGNKVEIIRGEAYFVDANTLRVmtedAAQTYTFKNAVLATGSTPIEIPGFKY--SKRVI 164
Cdd:PRK06292  82 VMARVRRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTVEV----NGERIEAKNIVIATGSRVPPIPGVWLilGDRLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 165 NSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKgnVNIHTKAMAKGV 244
Cdd:PRK06292 158 TSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE--FKIKLGAKVTSV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 245 EETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAH 324
Cdd:PRK06292 236 EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLH 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 325 KASYEGKVAVE-AISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVT 403
Cdd:PRK06292 316 EAADEGRIAAEnAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGRARVMGKNDGFVKVYA 395
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446182249 404 RKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIHI 468
Cdd:PRK06292 396 DKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRTALRDLFSKLIHG 460
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
9-468 3.81e-168

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 482.12  E-value: 3.81e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIE-------KANLGGVCLNVGCIPSKALINAGHRYENAMHS-DDMGITAEN 80
Cdd:PRK06327   4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  81 VKVDFTKVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFV----DANTLRVMTEDAaQTYTFKNAVLATGSTPIEIPG 156
Cdd:PRK06327  84 VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDE-TVITAKHVIIATGSEPRHLPG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 157 FKYS-KRVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNI 235
Cdd:PRK06327 163 VPFDnKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG-LDI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 236 HTKAMAKGVEETETGVKVSF-EVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIG 314
Cdd:PRK06327 242 HLGVKIGEIKTGGKGVSVAYtDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 315 DIVPGPPLAHKASYEGKVAVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNS 394
Cdd:PRK06327 322 DVVRGPMLAHKAEEEGVAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMANGRALAMGE 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446182249 395 TDGFLQLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIHI 468
Cdd:PRK06327 402 PDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEVWHEAALAVDKRPLHF 475
PRK06370 PRK06370
FAD-containing oxidoreductase;
11-452 4.89e-131

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 386.87  E-value: 4.89e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGIT-AENVKVDFTKVQ 89
Cdd:PRK06370   7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSvGGPVSVDFKAVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  90 EWKNGVVKKLTGGVEGLLKG-NKVEIIRGEAYFVDANTLRVmtedAAQTYTFKNAVLATGSTPI--EIPGFKySKRVINS 166
Cdd:PRK06370  87 ARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRV----GGETLRAKRIFINTGARAAipPIPGLD-EVGYLTN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 167 TGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEE 246
Cdd:PRK06370 162 ETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREG-IDVRLNAECIRVER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 247 TETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKA 326
Cdd:PRK06370 241 DGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 327 SYEGKVAVEAI--SGHASAIDYIgIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTR 404
Cdd:PRK06370 321 YNDARIVAANLldGGRRKVSDRI-VPYATYTDPPLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMKVVVD 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 446182249 405 KEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE 452
Cdd:PRK06370 400 ADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
10-452 1.89e-116

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 349.80  E-value: 1.89e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   10 LDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAEnVKVDFTKVQ 89
Cdd:TIGR02053   1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAAT-VAVDFGELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   90 EWKNGVVKKL-TGGVEGLLKGNKVEIIRGEAYFVDANTLRVmtEDAAQTYTFKNAVLATGSTPI--EIPGFKYSKrVINS 166
Cdd:TIGR02053  80 EGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGREVRGAKRFLIATGARPAipPIPGLKEAG-YLTS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  167 TGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEE 246
Cdd:TIGR02053 157 EEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEG-IEVVTSAQVKAVSV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  247 TETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKA 326
Cdd:TIGR02053 236 RGGGKIITVEKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  327 SYEGKVAVEAISGHASA-IDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRK 405
Cdd:TIGR02053 316 AKEGVVAAENALGGANAkLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVAEP 395
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 446182249  406 EDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE 452
Cdd:TIGR02053 396 GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
PRK06116 PRK06116
glutathione reductase; Validated
11-455 3.52e-93

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 289.36  E-value: 3.52e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHrYENAMH--SDDMGITAENVKVDFTKV 88
Cdd:PRK06116   6 DLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQ-IAEAFHdyAPGYGFDVTENKFDWAKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  89 QEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVmtedAAQTYTFKNAVLATGSTPI--EIPGFKYskrVINS 166
Cdd:PRK06116  85 IANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEV----NGERYTADHILIATGGRPSipDIPGAEY---GITS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 167 TGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEE 246
Cdd:PRK06116 158 DGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKG-IRLHTNAVPKAVEK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 247 TETG-VKVSFEvKGEIQTVeaDYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHK 325
Cdd:PRK06116 237 NADGsLTLTLE-DGETLTV--DCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPV 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 326 ASYEGKVAVEAISGH--ASAIDYIGIPAVCFTDPELASVGYTKKQAEEAG--MTVTVSKFPFAANGRALSLNSTDGFLQL 401
Cdd:PRK06116 314 AIAAGRRLSERLFNNkpDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYgeDNVKVYRSSFTPMYTALTGHRQPCLMKL 393
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446182249 402 VTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE--ITM 455
Cdd:PRK06116 394 VVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEefVTM 449
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
7-452 5.09e-90

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 281.66  E-value: 5.09e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   7 PIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEK-ANLGGVCLNVGCIPSKALINA-----GHRyENAMHSDDmgitaeN 80
Cdd:PRK05249   3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGGCTHTGTIPSKALREAvlrliGFN-QNPLYSSY------R 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  81 VKVDFT--KVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTED-AAQTYTFKNAVLATGSTPIEIPGF 157
Cdd:PRK05249  76 VKLRITfaDLLARADHVINKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECPDgEVETLTADKIVIATGSRPYRPPDV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 158 KYS-KRVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIH 236
Cdd:PRK05249 156 DFDhPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSG-VTIR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 237 TKAMAKGVEETETGVKVSFEVKGEIqtvEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDI 316
Cdd:PRK05249 235 HNEEVEKVEGGDDGVIVHLKSGKKI---KADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 317 VPGPPLAhKASYE-GKVAVEAISGHASA--IDYI--GIpavcFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALS 391
Cdd:PRK05249 312 IGFPSLA-SASMDqGRIAAQHAVGEATAhlIEDIptGI----YTIPEISSVGKTEQELTAAKVPYEVGRARFKELARAQI 386
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446182249 392 LNSTDGFLQLVTRKEDGLLVGAQVAGAGASDIIsEIGLAI-EAGMTAEDIAQTIHAHPTLGE 452
Cdd:PRK05249 387 AGDNVGMLKILFHRETLEILGVHCFGERATEII-HIGQAImEQKGTIEYFVNTTFNYPTMAE 447
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
11-330 9.08e-89

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: 273.04  E-value: 9.08e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEkanLGGVCLNVGCIPSKALINAGHRYENAMHsddmgitaenvkvdFTKVQE 90
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIASL--------------WADLYK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTlrvmTEDAAQTYTFKNAVLATGSTPI--EIPGFK----YSKRVI 164
Cdd:pfam07992  65 RKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL----VDGDGETITYDRLVIATGARPRlpPIPGVElnvgFLVRTL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  165 NSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGV 244
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNG-VEVRLGTSVKEI 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  245 EETETGVKVSFEVKGEIqtvEADYVLVTVGRRPNTQeiGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDI-VPGPPLA 323
Cdd:pfam07992 220 IGDGDGVEVILKDGTEI---DADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGGPELA 294

                  ....*..
gi 446182249  324 HKASYEG 330
Cdd:pfam07992 295 QNAVAQG 301
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
13-458 9.13e-84

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 265.57  E-value: 9.13e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  13 VVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGIT---AENVKVDFTKVq 89
Cdd:PRK07845   5 VIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRfidDGEARVDLPAV- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  90 ewkNGVVKKLT----GGVEGLLKGNKVEIIRGEAYFVDA----NTLRVMTEDAAQTYTFKNAVL-ATGSTPIEIPGFKYS 160
Cdd:PRK07845  84 ---NARVKALAaaqsADIRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLiATGASPRILPTAEPD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 161 -KRVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKA 239
Cdd:PRK07845 161 gERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRG-MTVLKRS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 240 MAKGVEETETGVKVSFEvkgEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPG 319
Cdd:PRK07845 240 RAESVERTGDGVVVTLT---DGRTVEGSHALMAVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGV 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 320 PPLAHKASYEGKVAVEAISGHA-SAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGF 398
Cdd:PRK07845 317 LPLASVAAMQGRIAMYHALGEAvSPLRLKTVASNVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKMSGLRDGF 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446182249 399 LQLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTL-GEITmEAA 458
Cdd:PRK07845 397 VKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLsGSIT-EAA 456
PRK13748 PRK13748
putative mercuric reductase; Provisional
10-452 2.93e-82

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 264.71  E-value: 2.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  10 LDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGH----RYENAMhsdDMGITAENVKVDF 85
Cdd:PRK13748  99 LHVAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHiahlRRESPF---DGGIAATVPTIDR 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TKVQEWKNGVVKKLT-GGVEGLLKGN-KVEIIRGEAYFVDANTLRV-MTEDAAQTYTFKNAVLATGSTPI--EIPGFKYS 160
Cdd:PRK13748 176 SRLLAQQQARVDELRhAKYEGILDGNpAITVLHGEARFKDDQTLIVrLNDGGERVVAFDRCLIATGASPAvpPIPGLKET 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 161 KrVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVeAGDEILAGFEKAMSSVVKRALQKKG-NVNIHTKA 239
Cdd:PRK13748 256 P-YWTSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTIL-ARSTLFFREDPAIGEAVTAAFRAEGiEVLEHTQA 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 240 MAKGVEETEtgvkvsFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPG 319
Cdd:PRK13748 334 SQVAHVDGE------FVLTTGHGELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQ 407
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 320 PPLAHKASYEGKVAVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGM-----TVTVSKFPfaangRALSLNS 394
Cdd:PRK13748 408 PQFVYVAAAAGTRAAINMTGGDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIetdsrTLTLDNVP-----RALANFD 482
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446182249 395 TDGFLQLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE 452
Cdd:PRK13748 483 TRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVE 540
PRK07251 PRK07251
FAD-containing oxidoreductase;
11-452 9.44e-80

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 254.29  E-value: 9.44e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIE--KANLGGVCLNVGCIPSKALINAghryenamhsddmgitAENvKVDFTKV 88
Cdd:PRK07251   5 DLIVIGFGKAGKTLAAKLASAGKKVALVEesKAMYGGTCINIGCIPTKTLLVA----------------AEK-NLSFEQV 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  89 QEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATG--STPIEIPGFKYSKRVINS 166
Cdd:PRK07251  68 MATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIELTAETIVINTGavSNVLPIPGLADSKHVYDS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 167 TGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEE 246
Cdd:PRK07251 148 TGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDG-ITFLLNAHTTEVKN 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 247 TETGVKVSFEVkgeiQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKA 326
Cdd:PRK07251 227 DGDQVLVVTED----ETYRFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYIS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 327 SYEGKVAVEAISGHAS--AIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTR 404
Cdd:PRK07251 303 LDDFRIVFGYLTGDGSytLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVN 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 446182249 405 KEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE 452
Cdd:PRK07251 383 TETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
9-467 5.57e-79

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 258.69  E-value: 5.57e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAII--EKANLGGVCLNVGCIPSKALINAGHRY---ENAMHSDDMGI------- 76
Cdd:PTZ00153 116 EYDVGIIGCGVGGHAAAINAMERGLKVIIFtgDDDSIGGTCVNVGCIPSKALLYATGKYrelKNLAKLYTYGIytnafkn 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  77 -----------TAENVKVDFTKVQEWKNGVVKKLTGGVEGLLKGNK-------VEIIRGEAYFVDANTLRvmTEDAAQTY 138
Cdd:PTZ00153 196 gkndpvernqlVADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIK--SEKSGKEF 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 139 TFKNAVLATGSTP-----IEIPGFKyskrVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILA 213
Cdd:PTZ00153 274 KVKNIIIATGSTPnipdnIEVDQKS----VFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 214 GFEKAMSSVVKRALQKKGNVNIHTKAMAKGVEETETGVKVSF--------EVKGEIQT------VEADYVLVTVGRRPNT 279
Cdd:PTZ00153 350 LLDADVAKYFERVFLKSKPVRVHLNTLIEYVRAGKGNQPVIIghserqtgESDGPKKNmndikeTYVDSCLVATGRKPNT 429
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 280 QEIGLEQVGVKMtDRGIIEIDEQCRTN------VPNIYAIGDIVPGPPLAHKASYEGKVAVEAISGHASA---------- 343
Cdd:PTZ00153 430 NNLGLDKLKIQM-KRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKEnvninvenwa 508
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 344 ---IDYIGIPAVCFTDPELASVGYTKKQAEEAGM--TVTVSKFPFAANGRALSLNS----------------------TD 396
Cdd:PTZ00153 509 skpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPpdNVGVEISFYKANSKVLCENNisfpnnsknnsynkgkyntvdnTE 588
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446182249 397 GFLQLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITMEAAEVALGMPIH 467
Cdd:PTZ00153 589 GMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAFKAIAGVRTH 659
PRK07846 PRK07846
mycothione reductase; Reviewed
11-457 1.58e-74

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 241.01  E-value: 1.58e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAqlGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVKVDFTKVQE 90
Cdd:PRK07846   3 DLIIIGTGSGNSILDERFA--DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDGVRWPDIVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  91 WKNGVVKKL-TGGVEGLLKGN-KVEIIRGEAYFVDANTLRVmteDAAQTYTFKNAVLATGSTPIeIPGFKYSKRVINSTG 168
Cdd:PRK07846  81 RVFGRIDPIaAGGEEYRGRDTpNIDVYRGHARFIGPKTLRT---GDGEEITADQVVIAAGSRPV-IPPVIADSGVRYHTS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 169 A--LSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGNVNIHTKAMakGVEE 246
Cdd:PRK07846 157 DtiMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKRWDVRLGRNVV--GVSQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 247 TETGVKVSFEVKgeiQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKA 326
Cdd:PRK07846 235 DGSGVTLRLDDG---STVEADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVA 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 327 SYEGKVaVEAISGHASAI---DYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFA--ANGRALSlnSTDGFLQL 401
Cdd:PRK07846 312 NHEARV-VQHNLLHPDDLiasDHRFVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGdvAYGWAME--DTTGFVKL 388
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446182249 402 VTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIH-AHPTLGEITMEA 457
Cdd:PRK07846 389 IADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQYwIHPALPEVVENA 445
PLN02507 PLN02507
glutathione reductase
9-458 6.11e-69

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 228.16  E-value: 6.11e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIE----------KANLGGVCLNVGCIPSKALI---NAGHRYENAmhsDDMG 75
Cdd:PLN02507  25 DFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVygaTFGGEFEDA---KNYG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  76 ITAeNVKVDFtkvqEWKNGVVKK------LTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAA-QTYTFKNAVLATG 148
Cdd:PLN02507 102 WEI-NEKVDF----NWKKLLQKKtdeilrLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTkLRYTAKHILIATG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 149 S--TPIEIPGFKYSkrvINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRA 226
Cdd:PLN02507 177 SraQRPNIPGKELA---ITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARN 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 227 LQKKGnVNIHTKAMAKGVEETETGVKVSFEVKGEIqtvEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTN 306
Cdd:PLN02507 254 LEGRG-INLHPRTNLTQLTKTEGGIKVITDHGEEF---VADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTN 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 307 VPNIYAIGDIVPGPPLAHKASYEGK-VAVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQA-EEAGMTVTVSKFPFA 384
Cdd:PLN02507 330 IPSIWAIGDVTNRINLTPVALMEGTcFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAvEQAKGDILVFTSSFN 409
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446182249 385 ANGRALSLNSTDGFLQLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE--ITMEAA 458
Cdd:PLN02507 410 PMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEefVTMRSV 485
PLN02546 PLN02546
glutathione reductase
9-458 1.45e-68

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 228.61  E-value: 1.45e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIE----------KANLGGVCLNVGCIPSKALINA---GHRYENamhSDDMG 75
Cdd:PLN02546  79 DFDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKKLLVYAskySHEFEE---SRGFG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  76 ITAE-NVKVDFTKVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVmtedAAQTYTFKNAVLATGSTPI-- 152
Cdd:PLN02546 156 WKYEtEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDV----DGKLYTARNILIAVGGRPFip 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 153 EIPGFKYskrVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGn 232
Cdd:PLN02546 232 DIPGIEH---AIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRG- 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 233 VNIHTKAMAKGVEETETGvkvSFEVKGEIQTVEA-DYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIY 311
Cdd:PLN02546 308 IEFHTEESPQAIIKSADG---SLSLKTNKGTVEGfSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIW 384
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 312 AIGDIVPGPPLAHKASYEGKVAVEAISGH-ASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRAL 390
Cdd:PLN02546 385 AVGDVTDRINLTPVALMEGGALAKTLFGNePTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGDVDVFTANFRPLKATL 464
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 391 SLNSTDGFLQLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE--ITMEAA 458
Cdd:PLN02546 465 SGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEefVTMRTP 534
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
13-452 3.54e-66

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 219.11  E-value: 3.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  13 VVVGAGPGGYVAAIRAAQLGQKVAIIEKAN--LGGVCLNVGCIPSKALINAGHRYenamhsddmgitaenvkVDFTKVQE 90
Cdd:PRK08010   7 VIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQQH-----------------TDFVRAIQ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  91 WKNGVVKKLTG-GVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPI--EIPGFKYSKRVINST 167
Cdd:PRK08010  70 RKNEVVNFLRNkNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQTVvpPIPGITTTPGVYDST 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 168 GALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEET 247
Cdd:PRK08010 150 GLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQG-VDIILNAHVERISHH 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 248 ETGVkvsfEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLAHKAS 327
Cdd:PRK08010 229 ENQV----QVHSEHAQLAVDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISL 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 328 YEGKVAVEAI--SGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRK 405
Cdd:PRK08010 305 DDYRIVRDELlgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDN 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 446182249 406 EDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE 452
Cdd:PRK08010 385 KTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
11-455 1.03e-65

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: 218.95  E-value: 1.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIE---------KANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAEN- 80
Cdd:TIGR01438   4 DLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEEt 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   81 VKVDFTKVQEWKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQ-TYTFKNAVLATGSTP--IEIPGF 157
Cdd:TIGR01438  84 VKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEkIYSAERFLIATGERPryPGIPGA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  158 KysKRVINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVeAGDEILAGFEKAMSSVVKRALQKKGnVNIHT 237
Cdd:TIGR01438 164 K--ELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDCANKVGEHMEEHG-VKFKR 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  238 KAMAKGVEETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDR-GIIEIDEQCRTNVPNIYAIGDI 316
Cdd:TIGR01438 240 QFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAVGDI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  317 VPG-PPLAHKASYEGKV-AVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQA----EEAGMTVTVSKF-PF--AANG 387
Cdd:TIGR01438 320 LEDkPELTPVAIQAGRLlAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAvekfGEENVEVFHSYFwPLewTIPS 399
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446182249  388 RAlslNSTDGFLQLV-TRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGEITM 455
Cdd:TIGR01438 400 RD---NHNKCYAKLVcNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFT 465
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
11-452 3.80e-62

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: 209.83  E-value: 3.80e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQL-GQKVAIIE---------KANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMG--ITA 78
Cdd:TIGR01423   5 DLVVIGAGSGGLEAGWNAATLyKKRVAVVDvqthhgppfYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGweFDR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   79 ENVKVDFTKVQEWKNGVVKKLTGGVEGLLKGNK-VEIIRGEAYFVDANTLrVMTEDA------AQTYTFKNAVLATGSTP 151
Cdd:TIGR01423  85 SSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVV-LVRESAdpksavKERLQAEHILLATGSWP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  152 --IEIPGFKYskrVINSTGALSLPEIPKKLVVIGGGYIGMELG---TAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRA 226
Cdd:TIGR01423 164 qmLGIPGIEH---CISSNEAFYLDEPPRRVLTVGGGFISVEFAgifNAYKPRGGKVTLCYRNNMILRGFDSTLRKELTKQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  227 LQKKGnVNIHTKAMAKGVEETETGVK-VSFEVKgeiQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCRT 305
Cdd:TIGR01423 241 LRANG-INIMTNENPAKVTLNADGSKhVTFESG---KTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  306 NVPNIYAIGDIVPGPPLAHKASYEGKVAVEAISGHA-SAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFA 384
Cdd:TIGR01423 317 NVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKpRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEKVAVYESSFT 396
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446182249  385 ANGRALSLNSTDGFL-QLVTRKEDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHPTLGE 452
Cdd:TIGR01423 397 PLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
PTZ00058 PTZ00058
glutathione reductase; Provisional
11-455 8.29e-51

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 181.35  E-value: 8.29e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKALINAGHRYENAMHSDDMGITAENVkVDFTKVQE 90
Cdd:PTZ00058  50 DLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFS-FNLPLLVE 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  91 WKNGVVKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMT-------------------------EDAAQTYTFKNAVL 145
Cdd:PTZ00058 129 RRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesdddevtivsagvsqLDDGQVIEGKNILI 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 146 ATGSTPiEIPGFKYSKRVINSTGALSLPEiPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKR 225
Cdd:PTZ00058 209 AVGNKP-IFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELEN 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 226 ALqKKGNVNIHTKAMAKGVEETE-TGVKVSFEVKGeiQTVEADYVLVTVGRRPNTQEIGLEQVGVKmTDRGIIEIDEQCR 304
Cdd:PTZ00058 287 DM-KKNNINIITHANVEEIEKVKeKNLTIYLSDGR--KYEHFDYVIYCVGRSPNTEDLNLKALNIK-TPKGYIKVDDNQR 362
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 305 TNVPNIYAIGDIV------------------PGPPLAHKASYEGK---------VAVEA-------ISGHASAI-DYIGI 349
Cdd:PTZ00058 363 TSVKHIYAVGDCCmvkknqeiedlnllklynEEPYLKKKENTSGEsyynvqltpVAINAgrlladrLFGPFSRTtNYKLI 442
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 350 PAVCFTDPELASVGYTKKQAEEA----GMTVTVSKFP--FAANGRALSLNSTDGFLQLVTRKEDGLLVGAQVAGAGASDI 423
Cdd:PTZ00058 443 PSVIFSHPPIGTIGLSEQEAIDIygkeNVKIYESRFTnlFFSVYDMDPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEI 522
                        490       500       510
                 ....*....|....*....|....*....|....
gi 446182249 424 ISEIGLAIEAGMTAEDIAQTIHAHPTLGE--ITM 455
Cdd:PTZ00058 523 LQGFAVALKMNATKADFDETIPIHPTAAEefVTM 556
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
11-455 2.79e-49

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 175.78  E-value: 2.79e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIE---------KANLGGVCLNVGCIPSKALINAGHrYENAMHSDdmgitAENV 81
Cdd:PTZ00052   7 DLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAAN-IGSIFHHD-----SQMY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  82 KVDFTKVQEWKNGV------VKKLTGGVEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATG---STPI 152
Cdd:PTZ00052  81 GWKTSSSFNWGKLVttvqnhIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEETITAKYILIATGgrpSIPE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 153 EIPGFK-YSkrvINSTGALSLPEIPKKLVVIGGGYIGMELGTAYANFGTEVTVVeAGDEILAGFEKAMSSVVKRALQKKG 231
Cdd:PTZ00052 161 DVPGAKeYS---ITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVA-VRSIPLRGFDRQCSEKVVEYMKEQG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 232 nVNIHTKAMAKGVEETETGVKVSFEVKgeiQTVEADYVLVTVGRRPNTQEIGLEQVGVKMTDRGIIEIDEQCrTNVPNIY 311
Cdd:PTZ00052 237 -TLFLEGVVPINIEKMDDKIKVLFSDG---TTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-TNIPNIF 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 312 AIGDIVPG-PPLAHKASYEGKV-AVEAISGHASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPF------ 383
Cdd:PTZ00052 312 AVGDVVEGrPELTPVAIKAGILlARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQefntle 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 384 -AANGR-------------ALSLNStdgFLQLVTRK-EDGLLVGAQVAGAGASDIISEIGLAIEAGMTAEDIAQTIHAHP 448
Cdd:PTZ00052 392 iAAVHRekherarkdeydfDVSSNC---LAKLVCVKsEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468

                 ....*..
gi 446182249 449 TLGEITM 455
Cdd:PTZ00052 469 TDAEVFM 475
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
349-457 3.16e-41

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: 142.69  E-value: 3.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  349 IPAVCFTDPELASVGYTKKQAEEAGMTVTVSKFPFAANGRALSLNSTDGFLQLVTRKEDGLLVGAQVAGAGASDIISEIG 428
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
                          90       100
                  ....*....|....*....|....*....
gi 446182249  429 LAIEAGMTAEDIAQTIHAHPTLGEITMEA 457
Cdd:pfam02852  81 LAIKMGATVEDLANTIHIHPTLSEALVEA 109
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
123-363 5.86e-37

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: 138.02  E-value: 5.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 123 DANTLRVMTEdaaQTYTFKNAVLATGSTPI--EIPGfkyskrvINSTGALSL------PEI--------PKKLVVIGGGY 186
Cdd:COG0446   65 EAKTVTLRDG---ETLSYDKLVLATGARPRppPIPG-------LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 187 IGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEEtETGVKVSFEVKGEIqtvEA 266
Cdd:COG0446  135 IGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHG-VELRLGETVVAIDG-DDKVAVTLTDGEEI---PA 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 267 DYVLVTVGRRPNTqEIgLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDI--VPGP--------PLAHKASYEGKVAVEA 336
Cdd:COG0446  210 DLVVVAPGVRPNT-EL-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCaeVPHPvtgktvyiPLASAANKQGRVAAEN 287
                        250       260
                 ....*....|....*....|....*..
gi 446182249 337 ISGHASAIDYIGIPAVCFTDPELASVG 363
Cdd:COG0446  288 ILGGPAPFPGLGTFISKVFDLCIASTG 314
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
11-337 1.05e-32

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 126.00  E-value: 1.05e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIpskalinaghryenamhsddmgitaENVkvdftkvqe 90
Cdd:COG0492    2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEI-------------------------ENY--------- 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  91 wkNGVVKKLTGG--VEGLL---KGNKVEIIRGEAYFVDA--NTLRVMTEDAaQTYTFKNAVLATGSTP--IEIPGF-KYS 160
Cdd:COG0492   48 --PGFPEGISGPelAERLReqaERFGAEILLEEVTSVDKddGPFRVTTDDG-TEYEAKAVIIATGAGPrkLGLPGEeEFE 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 161 KRVINSTGALSLPEIP-KKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAgfEKAMssvVKRaLQKKGNVNIHTKA 239
Cdd:COG0492  125 GRGVSYCATCDGFFFRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA--SKIL---VER-LRANPKIEVLWNT 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 240 MAKGVEETE--TGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQeiGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIV 317
Cdd:COG0492  199 EVTEIEGDGrvEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVR 276
                        330       340
                 ....*....|....*....|.
gi 446182249 318 PGPP-LAHKASYEGKVAVEAI 337
Cdd:COG0492  277 DYKYrQAATAAGEGAIAALSA 297
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
110-371 1.53e-32

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 127.95  E-value: 1.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 110 NKVEIIRGE-AYFVDANTLRVMTEDAaQTYTFKNAVLATGSTPI--EIPGfkyskrvINSTGALSL------------PE 174
Cdd:COG1251   69 NGIDLRLGTrVTAIDRAARTVTLADG-ETLPYDKLVLATGSRPRvpPIPG-------ADLPGVFTLrtlddadalraaLA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 175 IPKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAG-FEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETETGVKV 253
Cdd:COG1251  141 PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRqLDEEAGALLQRLLEALG-VEVRLGTGVTEIEGDDRVTGV 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 254 SFEvKGEiqTVEADYVLVTVGRRPNT---QEIGLEqvgvkmTDRGIIeIDEQCRTNVPNIYAIGDI--VPGPPLAHKAS- 327
Cdd:COG1251  220 RLA-DGE--ELPADLVVVAIGVRPNTelaRAAGLA------VDRGIV-VDDYLRTSDPDIYAAGDCaeHPGPVYGRRVLe 289
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446182249 328 -----YE-GKVAVEAISGHASAidYIGIPAVC---FTDPELASVGYTKKQAEE 371
Cdd:COG1251  290 lvapaYEqARVAAANLAGGPAA--YEGSVPSTklkVFGVDVASAGDAEGDEEV 340
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
122-441 2.62e-30

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 122.07  E-value: 2.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 122 VDANTLRVMTEDAAQTYTFKNA----VLATGSTPIeIPGFK-------YSKRV----INSTGALSLPEIpKKLVVIGGGY 186
Cdd:PRK09564  82 VDAKNKTITVKNLKTGSIFNDTydklMIATGARPI-IPPIKninlenvYTLKSmedgLALKELLKDEEI-KNIVIIGAGF 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 187 IGMELGTAYANFGTEVTVVEAGDEILAG-FEKAMSSVVKRALQKKGnVNIHTKAMAKGV--EETETGVKVSfevKGEIqt 263
Cdd:PRK09564 160 IGLEAVEAAKHLGKNVRIIQLEDRILPDsFDKEITDVMEEELRENG-VELHLNEFVKSLigEDKVEGVVTD---KGEY-- 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 264 vEADYVLVTVGRRPNTQeiGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGD------IVPGP----PLAHKASYEGKVA 333
Cdd:PRK09564 234 -EADVVIVATGVKPNTE--FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiynIVSNKnvyvPLATTANKLGRMV 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 334 VEAISG-HASAIDYIGIPAVCFTDPELASVGYTKKQAEEAGM---TVTVSKfpfaANGRALSLNSTDGFLQLVTRKEDGL 409
Cdd:PRK09564 311 GENLAGrHVSFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIdykTVFIKD----KNHTNYYPGQEDLYVKLIYEADTKV 386
                        330       340       350
                 ....*....|....*....|....*....|...
gi 446182249 410 LVGAQVAGA-GASDIISEIGLAIEAGMTAEDIA 441
Cdd:PRK09564 387 ILGGQIIGKkGAVLRIDALAVAIYAKLTTQELG 419
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
122-332 7.50e-22

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 96.91  E-value: 7.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 122 VDANTLRVMTEDaaQTYTFKNAVLATGSTPIeIPGFKYSKRVI--NSTGALSLPEIP----KKLVVIGGGYIGMELGTAY 195
Cdd:PRK04965  84 IDAEAQVVKSQG--NQWQYDKLVLATGASAF-VPPIPGRELMLtlNSQQEYRAAETQlrdaQRVLVVGGGLIGTELAMDL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 196 ANFGTEVTVVEAGDEILAGFEKA-MSSVVKRALQKKGnVNIHTKAMAKGVEETETGVKVSFeVKGeiQTVEADYVLVTVG 274
Cdd:PRK04965 161 CRAGKAVTLVDNAASLLASLMPPeVSSRLQHRLTEMG-VHLLLKSQLQGLEKTDSGIRATL-DSG--RSIEVDAVIAAAG 236
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446182249 275 RRPNTQ---EIGLeqvgvkMTDRGIIeIDEQCRTNVPNIYAIGDIvpgpplahkASYEGKV 332
Cdd:PRK04965 237 LRPNTAlarRAGL------AVNRGIV-VDSYLQTSAPDIYALGDC---------AEINGQV 281
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
103-337 2.77e-21

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 95.20  E-value: 2.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 103 VEGLLKGNKVEIIRGEAYFVDANTLRVMTEDAaQTYTFKNAVLATGSTP--IEIPGFK------YS--------KRVINS 166
Cdd:COG1252   62 LRELLRRAGVRFIQGEVTGIDPEARTVTLADG-RTLSYDYLVIATGSVTnfFGIPGLAehalplKTledalalrERLLAA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 167 TGALSLPEiPKKLVVIGGGYIGMEL----------GTAYANFGT---EVTVVEAGDEILAGFEKAMSSVVKRALQKKGnV 233
Cdd:COG1252  141 FERAERRR-LLTIVVVGGGPTGVELagelaellrkLLRYPGIDPdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRG-V 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 234 NIHTKAMAKGVEETetgvKVSFEvKGEiqTVEADYVLVTVGRRPN--TQEIGLEQvgvkmTDRGIIEIDEQCRT-NVPNI 310
Cdd:COG1252  219 EVHTGTRVTEVDAD----GVTLE-DGE--EIPADTVIWAAGVKAPplLADLGLPT-----DRRGRVLVDPTLQVpGHPNV 286
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446182249 311 YAIGDI--VPG------PPLAHKASYEGKVAVEAI 337
Cdd:COG1252  287 FAIGDCaaVPDpdgkpvPKTAQAAVQQAKVLAKNI 321
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
14-337 5.89e-19

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: 88.65  E-value: 5.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  14 VVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGGVcLNVGcIPS----KALINaghRYENAMhsDDMGITAE-NVKV--DF 85
Cdd:COG0493  126 VVGSGPAGLAAAYQLARAGHEVTVFEALDkPGGL-LRYG-IPEfrlpKDVLD---REIELI--EALGVEFRtNVEVgkDI 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TkvqewkngvvkkltggVEGLLKGnkveiirgeayfvdantlrvmtedaaqtytFKNAVLATGST---PIEIPG------ 156
Cdd:COG0493  199 T----------------LDELLEE------------------------------FDAVFLATGAGkprDLGIPGedlkgv 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 157 ---FKYSKRVINSTGALSLPEIPKKLVVIGGGYIGME-------LGTAyanfgtEVTVVEAGD---------EILAGFEK 217
Cdd:COG0493  233 hsaMDFLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDcartalrLGAE------SVTIVYRRTreempaskeEVEEALEE 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 218 A-----MSSVVKRALQKKGNVN-IHTKAMAKGvEETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIgLEQVGVKM 291
Cdd:COG0493  307 GveflfLVAPVEIIGDENGRVTgLECVRMELG-EPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGL-EEELGLEL 384
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 446182249 292 TDRGIIEIDEQC-RTNVPNIYAIGDIVPGPPLAHKASYEGKVAVEAI 337
Cdd:COG0493  385 DKRGTIVVDEETyQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
178-256 4.29e-18

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: 78.79  E-value: 4.29e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446182249  178 KLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETETGVKVSFE 256
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNG-IEFLLNTTVEAIEGNGDGVVVVLT 78
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
11-315 8.68e-17

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 82.51  E-value: 8.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAII-EKanLGGVCLnvgcipskalinaghryenamhsDDMGItaENvkvdFTKVQ 89
Cdd:PRK15317 213 DVLVVGGGPAGAAAAIYAARKGIRTGIVaER--FGGQVL-----------------------DTMGI--EN----FISVP 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  90 EwKNGvvKKLTGGVEGLLKGNKVEII---RGEAYFVDANTLRVMTEDAAqTYTFKNAVLATGST--PIEIPG-------- 156
Cdd:PRK15317 262 E-TEG--PKLAAALEEHVKEYDVDIMnlqRASKLEPAAGLIEVELANGA-VLKAKTVILATGARwrNMNVPGedeyrnkg 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 157 -----------FKySKRVinstgalslpeipkklVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAgfekamSSVVKR 225
Cdd:PRK15317 338 vaycphcdgplFK-GKRV----------------AVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKA------DQVLQD 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 226 ALQKKGNVNIHTKAMAKGVEETE---TGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQeiGLEQVgVKMTDRGIIEIDEQ 302
Cdd:PRK15317 395 KLRSLPNVTIITNAQTTEVTGDGdkvTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTE--WLKGT-VELNRRGEIIVDAR 471
                        330
                 ....*....|...
gi 446182249 303 CRTNVPNIYAIGD 315
Cdd:PRK15317 472 GATSVPGVFAAGD 484
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
122-361 3.02e-16

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 81.41  E-value: 3.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  122 VDANTLRVMTeDAAQTYTFKNAVLATGSTP--IEIPGFK----YSKRVINSTGAL-SLPEIPKKLVVIGGGYIGMELGTA 194
Cdd:TIGR02374  80 IDTDQKQVIT-DAGRTLSYDKLILATGSYPfiLPIPGADkkgvYVFRTIEDLDAImAMAQRFKKAAVIGGGLLGLEAAVG 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  195 YANFGTEVTVVEAGDEILA-GFEKAMSSVVKRALQKKGnVNIHTKAMAKGVEETETGVKVSFEVKGEIqtvEADYVLVTV 273
Cdd:TIGR02374 159 LQNLGMDVSVIHHAPGLMAkQLDQTAGRLLQRELEQKG-LTFLLEKDTVEIVGATKADRIRFKDGSSL---EADLIVMAA 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  274 GRRPNTqEIGLeQVGVKMtDRGIIeIDEQCRTNVPNIYAIGDIVpgpplAHKASYEGKVAVEAISGHASAIDYIGIPAVC 353
Cdd:TIGR02374 235 GIRPND-ELAV-SAGIKV-NRGII-VNDSMQTSDPDIYAVGECA-----EHNGRVYGLVAPLYEQAKVLADHICGVECEE 305

                  ....*...
gi 446182249  354 FTDPELAS 361
Cdd:TIGR02374 306 YEGSDLSA 313
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
177-363 1.58e-15

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 78.29  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 177 KKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAGFEKAMSSVVKRALQKKGnvnIHTKAMakgvEETET--GVKVS 254
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKRE---IPYRLN----EEIDAinGNEVT 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 255 FEvKGEIQTVeaDYVLVTVGRRPNTQEIglEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGP----------PLAH 324
Cdd:PRK13512 222 FK-SGKVEHY--DMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHyrhvdlpasvPLAW 296
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446182249 325 KASYEGKVAVEAISGHASAI--DYIGIPAVCFTDPELASVG 363
Cdd:PRK13512 297 GAHRAASIVAEQIAGNDTIEfkGFLGNNIVKFFDYTFASVG 337
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
104-343 7.09e-14

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 74.00  E-value: 7.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 104 EGLLKGNKVEIIRGEAYFVDANTLRVMTEDAAQTYTFKNAVLATGSTPIeIPGFKYSK-------RVINSTGAL-SLPEI 175
Cdd:PRK14989  66 EGFYEKHGIKVLVGERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPW-IPPIKGSEtqdcfvyRTIEDLNAIeACARR 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 176 PKKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILA-GFEKAMSSVVKRALQKKGnVNIHT-KAMAKGVEETETGVKV 253
Cdd:PRK14989 145 SKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAeQLDQMGGEQLRRKIESMG-VRVHTsKNTLEIVQEGVEARKT 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 254 SFEVKGEiqTVEADYVLVTVGRRPntQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGD-----------IVPGPPL 322
Cdd:PRK14989 224 MRFADGS--ELEVDFIVFSTGIRP--QDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGEcaswnnrvfglVAPGYKM 299
                        250       260
                 ....*....|....*....|.
gi 446182249 323 AhkasyegKVAVEAISGHASA 343
Cdd:PRK14989 300 A-------QVAVDHLLGSENA 313
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
115-330 7.02e-13

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 70.18  E-value: 7.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 115 IRGEAYFVDANTLRVMTEDAA-------QTYTFK--NAVLATGSTP--IEIPGFK--------------YSKRVINSTGA 169
Cdd:PTZ00318  80 LRAVVYDVDFEEKRVKCGVVSksnnanvNTFSVPydKLVVAHGARPntFNIPGVEerafflkevnhargIRKRIVQCIER 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 170 LSLPEIP----KKL---VVIGGGYIGMELGTAYANFGTE--------------VTVVEAGDEILAGFEKAMSSVVKRALQ 228
Cdd:PTZ00318 160 ASLPTTSveerKRLlhfVVVGGGPTGVEFAAELADFFRDdvrnlnpelveeckVTVLEAGSEVLGSFDQALRKYGQRRLR 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 229 KKGnVNIHTKAMAKGVEETEtgvkvSFEVKGEIqtVEADYVLVT--VGRRPNTQeigleQVGVKMTDRGIIEIDEQCRT- 305
Cdd:PTZ00318 240 RLG-VDIRTKTAVKEVLDKE-----VVLKDGEV--IPTGLVVWStgVGPGPLTK-----QLKVDKTSRGRISVDDHLRVk 306
                        250       260       270
                 ....*....|....*....|....*....|
gi 446182249 306 NVPNIYAIGDI-----VPGPPLAHKASYEG 330
Cdd:PTZ00318 307 PIPNVFALGDCaaneeRPLPTLAQVASQQG 336
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
14-337 3.72e-12

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 68.36  E-value: 3.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  14 VVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGGVcLNVGcIPS--------KALINaghRYEnamhsdDMGITAE-NVKV 83
Cdd:PRK12771 142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGPkLGGM-MRYG-IPAyrlprevlDAEIQ---RIL------DLGVEVRlGVRV 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  84 dftkvqewkngvvkkltggvegllkGNKVEIIRGEAYFvDANTLrvmtedaaqtytfknAVLATGSTPIEIPGfKYSKRV 163
Cdd:PRK12771 211 -------------------------GEDITLEQLEGEF-DAVFV---------------AIGAQLGKRLPIPG-EDAAGV 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 164 IN------STGALSLPEIPKKLVVIGGGYIGME-------LGtayanfGTEVTVV--------EAGDEilaGFEKAMSSV 222
Cdd:PRK12771 249 LDavdflrAVGEGEPPFLGKRVVVIGGGNTAMDaartarrLG------AEEVTIVyrrtredmPAHDE---EIEEALREG 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 223 VKralqkkgnvnIHTKAMAKGVEETETGVKVSFE----------------VKGEIQTVEADYVLVTVGRRPNTQeiGLEQ 286
Cdd:PRK12771 320 VE----------INWLRTPVEIEGDENGATGLRVitvekmeldedgrpspVTGEEETLEADLVVLAIGQDIDSA--GLES 387
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446182249 287 VGVKMTDRGIIEIDEQCR-TNVPNIYAIGDIVPGPPLAHKASYEGKVAVEAI 337
Cdd:PRK12771 388 VPGVEVGRGVVQVDPNFMmTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNI 439
gltD PRK12810
glutamate synthase subunit beta; Reviewed
14-337 7.12e-12

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 67.11  E-value: 7.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  14 VVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGGvcLNVGCIPS----KALINaghRYENAMhsDDMGI---TAENVKVDF 85
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFERADrIGG--LLRYGIPDfkleKEVID---RRIELM--EAEGIefrTNVEVGKDI 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TKVQEWKN--GVVkkLTGGVEGLLKGNkveiIRGE----AYF-VD---ANTLRVMTEDAAQTytfknaVLATGstpieip 155
Cdd:PRK12810 221 TAEELLAEydAVF--LGTGAYKPRDLG----IPGRdldgVHFaMDfliQNTRRVLGDETEPF------ISAKG------- 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 156 gfkysKRVinstgalslpeipkklVVIGGGYIGME-LGTAYANFGTEVTVVEAG-------DEILAGFEKAMSSVVKRAl 227
Cdd:PRK12810 282 -----KHV----------------VVIGGGDTGMDcVGTAIRQGAKSVTQRDIMpmppsrrNKNNPWPYWPMKLEVSNA- 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 228 QKKGNV---NIHTKAM------AKGVE--ETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQEIgLEQVGVKMTDRGI 296
Cdd:PRK12810 340 HEEGVErefNVQTKEFegengkVTGVKvvRTELGEGDFEPVEGSEFVLPADLVLLAMGFTGPEAGL-LAQFGVELDERGR 418
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 446182249 297 IEIDEQC-RTNVPNIYAIGDIVPGPPLAHKASYEGKVAVEAI 337
Cdd:PRK12810 419 VAAPDNAyQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
177-341 1.76e-10

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 62.64  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 177 KKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDEILAgfeKAMSSVVKRAL----QKKGnVNIHtkaMAKGVEETETGVK 252
Cdd:PRK09754 145 RSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMG---RNAPPPVQRYLlqrhQQAG-VRIL---LNNAIEHVVDGEK 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 253 VSFEVK-GEiqTVEADYVLVTVGRRPNTQ---EIGLEqvgvkmTDRGIIeIDEQCRTNVPNIYAIGDIV----PGPPLAH 324
Cdd:PRK09754 218 VELTLQsGE--TLQADVVIYGIGISANDQlarEANLD------TANGIV-IDEACRTCDPAIFAGGDVAitrlDNGALHR 288
                        170
                 ....*....|....*..
gi 446182249 325 KASYEGKVAVEAISGHA 341
Cdd:PRK09754 289 CESWENANNQAQIAAAA 305
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
14-337 5.10e-10

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 61.35  E-value: 5.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  14 VVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGGVclNVGCIPS----KALINAghRYENAMhsdDMGITAE-NVKV--DF 85
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEARDkAGGL--LRYGIPEfrlpKDIVDR--EVERLL---KLGVEIRtNTEVgrDI 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  86 TkvqewkngvvkkltggVEGLLKGNKveiirgeAYFV-----DANTLRVMTEDAAQTYtfkNAVlatgstpieipgfKYS 160
Cdd:PRK11749 218 T----------------LDELRAGYD-------AVFIgtgagLPRFLGIPGENLGGVY---SAV-------------DFL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 161 KRViNSTGALSLPEIPKKLVVIGGGYIGME-LGTAYANFGTEVTVVEAGDeilagfEKAMS-SVVKRALQKKGNVNIHTK 238
Cdd:PRK11749 259 TRV-NQAVADYDLPVGKRVVVIGGGNTAMDaARTAKRLGAESVTIVYRRG------REEMPaSEEEVEHAKEEGVEFEWL 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 239 AMAKGVEETE---TGVKV--------------SFEVKGEIQTVEADYVLVTVGRRPNTqEIGLEQVGVKMTDRG-IIEID 300
Cdd:PRK11749 332 AAPVEILGDEgrvTGVEFvrmelgepdasgrrRVPIEGSEFTLPADLVIKAIGQTPNP-LILSTTPGLELNRWGtIIADD 410
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 446182249 301 EQCRTNVPNIYAIGDIVPGPPLAHKASYEGKVAVEAI 337
Cdd:PRK11749 411 ETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAI 447
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
244-338 2.70e-09

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 58.46  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 244 VEETETGVKVSFEVKGEIQTVEADYVLVTVGRRPnTQEIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGDIVPGPPLA 323
Cdd:PRK12770 253 GEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKI 331
                         90
                 ....*....|....*
gi 446182249 324 HKASYEGKVAVEAIS 338
Cdd:PRK12770 332 GKAIKSGLRAAQSIH 346
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
177-314 7.77e-09

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 56.85  E-value: 7.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249  177 KKLVVIGGGYIGME--LGTAYAnfGTEVTVVEAGDEILAgFEKAMSSVVK-------RALQKKGNVNIHTKAMAKGVEET 247
Cdd:pfam13738 156 QKVVVIGGYNSAVDaaLELVRK--GARVTVLYRGSEWED-RDSDPSYSLSpdtlnrlEELVKNGKIKAHFNAEVKEITEV 232
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446182249  248 ETGVKVSFEvKGEIQTVEADYVLVTvGRRPNTQEigLEQVGVKMTDRGIIEIDEQ-CRTNVPNIYAIG 314
Cdd:pfam13738 233 DVSYKVHTE-DGRKVTSNDDPILAT-GYHPDLSF--LKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
GIDA pfam01134
Glucose inhibited division protein A;
11-149 4.26e-08

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 55.25  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIekANLGGVCLNVGCIPSKALINAGH--RYENAMHSdDMGITAENVKVDF--- 85
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLI--THNTDTIAELSCNPSIGGIAKGHlvREIDALGG-LMGKAADKTGIQFrml 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446182249   86 ----------TKVQEWKNGVVKKLTggvEGLLKGNKVEIIRGEA--YFVDANTLRVMTEDAAQTYTFKNAVLATGS 149
Cdd:pfam01134  78 ntskgpavraLRAQVDRDLYSKEMT---ETLENHPNLTLIQGEVtdLIPENGKVKGVVTEDGEEYKAKAVVLATGT 150
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
177-343 9.67e-08

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 54.36  E-value: 9.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 177 KKLVVIGGGYIGMELGTAYANFGTE-VTVV--EAGDEILAGFEKamssvVKRALQK-----------------KGNV-NI 235
Cdd:PRK12778 571 KKVAVVGGGNTAMDSARTAKRLGAErVTIVyrRSEEEMPARLEE-----VKHAKEEgiefltlhnpieyladeKGWVkQV 645
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 236 HTKAMAKGvEETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQeIGLEQVGVKMTDRGIIEIDEQCRTNVPNIYAIGD 315
Cdd:PRK12778 646 VLQKMELG-EPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPL-VPSSIPGLELNRKGTIVVDEEMQSSIPGIYAGGD 723
                        170       180
                 ....*....|....*....|....*...
gi 446182249 316 IVPGPPLAHKASYEGKVAVEAISGHASA 343
Cdd:PRK12778 724 IVRGGATVILAMGDGKRAAAAIDEYLSS 751
PRK12831 PRK12831
putative oxidoreductase; Provisional
175-337 1.93e-07

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 53.10  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 175 IPKKLVVIGGGYIGMELGTAYANFGTEVTVV--EAGDEILAGFEK---AMSSVVKRAL---------QKKGNVN-IHTKA 239
Cdd:PRK12831 280 VGKKVAVVGGGNVAMDAARTALRLGAEVHIVyrRSEEELPARVEEvhhAKEEGVIFDLltnpveilgDENGWVKgMKCIK 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 240 MAKGvEETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNtQEIGLEQVGVKMTDRGIIEIDEQC-RTNVPNIYAIGDIVP 318
Cdd:PRK12831 360 MELG-EPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPN-PLISSTTKGLKINKRGCIVADEETgLTSKEGVFAGGDAVT 437
                        170
                 ....*....|....*....
gi 446182249 319 GPPLAHKASYEGKVAVEAI 337
Cdd:PRK12831 438 GAATVILAMGAGKKAAKAI 456
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
11-45 1.07e-06

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 50.69  E-value: 1.07e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGG 45
Cdd:pfam12831   1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGfLGG 36
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
11-45 1.17e-06

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 50.62  E-value: 1.17e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGG 45
Cdd:COG1233    5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDtPGG 40
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
8-45 2.94e-06

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 49.45  E-value: 2.94e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446182249   8 IELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGG 45
Cdd:COG1053    2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
HI0933_like pfam03486
HI0933-like protein;
11-42 4.10e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 48.73  E-value: 4.10e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKAN 42
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGK 33
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
11-41 8.21e-06

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 48.05  E-value: 8.21e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKA 41
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKG 31
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
172-339 1.12e-05

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 47.90  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 172 LPEIP-KKLVVIGGGYIGMELGTAYANFGTEVTVV--EAGDEILA-------GFEKAMSSVVKRALQK-----KGNVNIH 236
Cdd:PRK12779 442 LPEVKgKEVFVIGGGNTAMDAARTAKRLGGNVTIVyrRTKSEMPArveelhhALEEGINLAVLRAPREfigddHTHFVTH 521
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 237 TKAMAKGVEETETGVKVSFEVKGEIQTVEADYVLVTVGRRPNTQeIGLEQVGVKMTDRGIIEIDEQC-RTNVPNIYAIGD 315
Cdd:PRK12779 522 ALLDVNELGEPDKSGRRSPKPTGEIERVPVDLVIMALGNTANPI-MKDAEPGLKTNKWGTIEVEKGSqRTSIKGVYSGGD 600
                        170       180
                 ....*....|....*....|....
gi 446182249 316 IVPGPPLAHKASYEGKVAVEAISG 339
Cdd:PRK12779 601 AARGGSTAIRAAGDGQAAAKEIVG 624
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
173-337 1.15e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 47.80  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 173 PEIPKKLVVIGGGYIGMELGTAYANFGTE-VTVV----------------EAGDEILAGFEKAMSSVVKRAlqkKGNVNI 235
Cdd:PRK12814 320 LHPGKKVVVIGGGNTAIDAARTALRLGAEsVTILyrrtreempanraeieEALAEGVSLRELAAPVSIERS---EGGLEL 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 236 HTKAMAKGvEETETGVKVSFEVKGEIQTVEADYVLVTVGrrpntQEIGL---EQVGVKMTDRGIIEID-EQCRTNVPNIY 311
Cdd:PRK12814 397 TAIKMQQG-EPDESGRRRPVPVEGSEFTLQADTVISAIG-----QQVDPpiaEAAGIGTSRNGTVKVDpETLQTSVAGVF 470
                        170       180
                 ....*....|....*....|....*.
gi 446182249 312 AIGDIVPGPPLAHKASYEGKVAVEAI 337
Cdd:PRK12814 471 AGGDCVTGADIAINAVEQGKRAAHAI 496
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
11-46 5.92e-05

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 45.00  E-value: 5.92e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 446182249   11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGGV 46
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRY 37
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
14-47 1.12e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 40.21  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446182249   14 VVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGGVC 47
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDrLGGNA 35
PRK12839 PRK12839
FAD-dependent oxidoreductase;
7-45 1.42e-04

FAD-dependent oxidoreductase;


Pssm-ID: 237223 [Multi-domain]  Cd Length: 572  Bit Score: 44.43  E-value: 1.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446182249   7 PIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGG 45
Cdd:PRK12839   6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKAStCGG 45
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
9-46 1.56e-04

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 44.08  E-value: 1.56e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKA-NLGGV 46
Cdd:COG2072    6 HVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKAdDVGGT 44
PRK06134 PRK06134
putative FAD-binding dehydrogenase; Reviewed
1-45 1.96e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 180419 [Multi-domain]  Cd Length: 581  Bit Score: 43.94  E-value: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446182249   1 MVVGDFPIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEK-ANLGG 45
Cdd:PRK06134   4 AAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKdPVFGG 49
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
8-41 2.44e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 43.30  E-value: 2.44e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446182249   8 IELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKA 41
Cdd:PRK05329   1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
11-45 2.94e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 43.24  E-value: 2.94e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIE---KANLGG 45
Cdd:COG3573    7 DVIVVGAGLAGLVAAAELADAGRRVLLLDqepEANLGG 44
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
11-47 6.68e-04

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 42.13  E-value: 6.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEKAN-LGGVC 47
Cdd:COG1232    3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGGLI 40
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
11-45 7.86e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 41.81  E-value: 7.86e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446182249  11 DTVVVGAGPGGYVAAIRAAQLGQKVAIIEK---ANLGG 45
Cdd:PRK12834   6 DVIVVGAGLAGLVAAAELADAGKRVLLLDQeneANLGG 43
PRK10262 PRK10262
thioredoxin reductase; Provisional
177-317 1.05e-03

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 41.20  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446182249 177 KKLVVIGGGYIGMELGTAYANFGTEVTVVEAGDeilaGFeKAMSSVVKRALQK--KGNVNIHTKAMAKGVEETETGVK-- 252
Cdd:PRK10262 147 QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD----GF-RAEKILIKRLMDKveNGNIILHTNRTLEEVTGDQMGVTgv 221
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446182249 253 --VSFEVKGEIQTVEADYVLVTVGRRPNTQ----EIGLEQVGVKMTDrGIIeiDEQCRTNVPNIYAIGDIV 317
Cdd:PRK10262 222 rlRDTQNSDNIESLDVAGLFVAIGHSPNTAifegQLELENGYIKVQS-GIH--GNATQTSIPGVFAAGDVM 289
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
9-41 1.07e-03

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 41.56  E-value: 1.07e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKA 41
Cdd:PRK07843   7 EYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKA 39
sdhA PRK07803
succinate dehydrogenase flavoprotein subunit; Reviewed
9-44 1.89e-03

succinate dehydrogenase flavoprotein subunit; Reviewed


Pssm-ID: 236101 [Multi-domain]  Cd Length: 626  Bit Score: 40.79  E-value: 1.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLG 44
Cdd:PRK07803   8 SYDVVVIGAGGAGLRAAIEARERGLRVAVVCKSLFG 43
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
13-41 2.93e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 39.54  E-value: 2.93e-03
                         10        20
                 ....*....|....*....|....*....
gi 446182249  13 VVVGAGPGGYVAAIRAAQLGQKVAIIEKA 41
Cdd:COG0654    7 LIVGGGPAGLALALALARAGIRVTVVERA 35
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
178-214 2.98e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 39.69  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446182249  178 KLVVIGGGYIGmeLGTAY--ANFGTEVTVVEAGDEILAG 214
Cdd:pfam01266   1 DVVVIGGGIVG--LSTAYelARRGLSVTLLERGDDPGSG 37
PRK12843 PRK12843
FAD-dependent oxidoreductase;
9-45 3.74e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 39.72  E-value: 3.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEK-ANLGG 45
Cdd:PRK12843  16 EFDVIVIGAGAAGMSAALFAAIAGLKVLLVERtEYVGG 53
PRK12842 PRK12842
putative succinate dehydrogenase; Reviewed
7-45 4.12e-03

putative succinate dehydrogenase; Reviewed


Pssm-ID: 237224 [Multi-domain]  Cd Length: 574  Bit Score: 39.68  E-value: 4.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446182249   7 PIELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEK-ANLGG 45
Cdd:PRK12842   7 ELTCDVLVIGSGAGGLSAAITARKLGLDVVVLEKePVFGG 46
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
9-45 6.57e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 38.97  E-value: 6.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446182249   9 ELDTVVVGAGPGGYVAAIRAAQLGQKVAIIEKANLGG 45
Cdd:PRK12844   6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVG 42
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
17-58 7.13e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 38.41  E-value: 7.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446182249  17 AGPGGYVAAIRAAQLGQKVAIIEKANLGGVCLNVGCIPSKAL 58
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRAL 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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