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Conserved domains on  [gi|515743447|ref|WP_017176047|]
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MULTISPECIES: hypothiocyanous acid reductase MerA [Staphylococcus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
chlor_oxi_RclA super family cl45835
reactive chlorine resistance oxidoreductase RclA;
1-438 2.33e-171

reactive chlorine resistance oxidoreductase RclA;


The actual alignment was detected with superfamily member NF040477:

Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 487.75  E-value: 2.33e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVVKALNQ 80
Cdd:NF040477   1 MNHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQRKSSVVGFLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 KNYLNLENDENITLLNFKAQFKSNTEVELIDENGKLVqtLTADKILINTGAKSNIPNIEGIDSAQNVYDSKGLLNISYQP 160
Cdd:NF040477  81 KNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQE--LRGEKIFINTGAQSVLPPIPGLTTTPGVYDSTGLLNLTQLP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETSQ 240
Cdd:NF040477 159 ARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSHEGEVQLETAE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 241 GNFTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYISLDDFRILKSELFGDR 319
Cdd:NF040477 239 GVLTVDALLVASGRKPATAgLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGEG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 320 SRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGKG 399
Cdd:NF040477 319 KRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVLKAVVDNKTQRILGVSLLCVD 398
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 515743447 400 SEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:NF040477 399 SHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLF 437
 
Name Accession Description Interval E-value
chlor_oxi_RclA NF040477
reactive chlorine resistance oxidoreductase RclA;
1-438 2.33e-171

reactive chlorine resistance oxidoreductase RclA;


Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 487.75  E-value: 2.33e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVVKALNQ 80
Cdd:NF040477   1 MNHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQRKSSVVGFLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 KNYLNLENDENITLLNFKAQFKSNTEVELIDENGKLVqtLTADKILINTGAKSNIPNIEGIDSAQNVYDSKGLLNISYQP 160
Cdd:NF040477  81 KNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQE--LRGEKIFINTGAQSVLPPIPGLTTTPGVYDSTGLLNLTQLP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETSQ 240
Cdd:NF040477 159 ARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSHEGEVQLETAE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 241 GNFTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYISLDDFRILKSELFGDR 319
Cdd:NF040477 239 GVLTVDALLVASGRKPATAgLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGEG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 320 SRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGKG 399
Cdd:NF040477 319 KRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVLKAVVDNKTQRILGVSLLCVD 398
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 515743447 400 SEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:NF040477 399 SHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLF 437
PRK07251 PRK07251
FAD-containing oxidoreductase;
1-440 8.76e-170

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 483.48  E-value: 8.76e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVVKALNQ 80
Cdd:PRK07251   1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMYGGTCINIGCIPTKTLLVAAEKNLSFEQVMATKNTVTSRLRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 KNYLNLENDEnITLLNFKAQFKSNTEVELidENGKLVQTLTADKILINTGAKSNIPNIEGIDSAQNVYDSKGLLNISYQP 160
Cdd:PRK07251  81 KNYAMLAGSG-VDLYDAEAHFVSNKVIEV--QAGDEKIELTAETIVINTGAVSNVLPIPGLADSKHVYDSTGIQSLETLP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREdQEIVTHMINDFKDK-GVRLITNVETKALKNEGDLTTVETS 239
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE-EPSVAALAKQYMEEdGITFLLNAHTTEVKNDGDQVLVVTE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 240 QGNFTGDAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYISLDDFRILKSELFGD 318
Cdd:PRK07251 237 DETYRFDALLYATGRKPNTePLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 319 RSRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGK 398
Cdd:PRK07251 317 GSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGE 396
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 515743447 399 GSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLFNI 440
Cdd:PRK07251 397 GSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLFNI 438
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
1-438 1.33e-146

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: 425.27  E-value: 1.33e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLV-------------NDGIK----HVD 63
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK--GRLGGTCLNVGCIPSKALLhaaevahearhaaEFGISagapSVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  64 FSTAFSRKKEVVKALNqKNYLNLENDENITLLNFKAQFKSNTEVELIDEngklvQTLTADKILINTGAKSNIPNIEGIDS 143
Cdd:COG1249   79 WAALMARKDKVVDRLR-GGVEELLKKNGVDVIRGRARFVDPHTVEVTGG-----ETLTADHIVIATGSRPRVPPIPGLDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 144 AqNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVE 223
Cdd:COG1249  153 V-RVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 224 TKALKNEGDLTTVETSQGN----FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGL 298
Cdd:COG1249  232 VTSVEKTGDGVTVTLEDGGgeeaVEADKVLVATGRRPNTDgLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 299 QFTYISLDDFRILKSELFGDRSRHTeNRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGL 378
Cdd:COG1249  312 QLAHVASAEGRVAAENILGKKPRPV-DYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 379 FKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:COG1249  391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
3-432 5.82e-90

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: 280.30  E-value: 5.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    3 HYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLVN-----DGIKH------------VDFS 65
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEK--EYLGGTCLNVGCIPTKALLHsaevyDEIKHakdlgievenvsVDWE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   66 TAFSRKKEVVKALNQK-NYLNLENdeNITLLNFKAQFKSNTEVELIDENGKlvQTLTADKILINTGAKSNIPNIEGIDSA 144
Cdd:TIGR01350  79 KMQKRKNKVVKKLVGGvSGLLKKN--KVTVIKGEAKFLDPGTVSVTGENGE--ETLEAKNIIIATGSRPRSLPGPFDFDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  145 QNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVET 224
Cdd:TIGR01350 155 KVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  225 KALKNEGDLTTVETSQGNF---TGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQF 300
Cdd:TIGR01350 235 TAVEKNDDQVTYENKGGETetlTGEKVLVAVGRKPNTEgLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPML 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  301 TYISLDDFRILKSELFGDRSRHTeNRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFK 380
Cdd:TIGR01350 315 AHVASHEGIVAAENIAGKEPAHI-DYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVK 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515743447  381 VVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAE 432
Cdd:TIGR01350 394 IIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
4-297 6.01e-60

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: 197.54  E-value: 6.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQftesyGGTCINHGCIPSKVLVNDGIKHVDFST---AFSRKKEVVKALNQ 80
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-----EGTCPYGGCVLSKALLGAAEAPEIASLwadLYKRKEEVVKKLNN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   81 kNYLNLENDENITLLNFKAQFKSNtevELIDENGklvQTLTADKILINTGAKSNIPNIEGIDSAQN----VYDSKGLLNI 156
Cdd:pfam07992  76 -GIEVLLGTEVVSIDPGAKKVVLE---ELVDGDG---ETITYDRLVIATGARPRLPPIPGVELNVGflvrTLDSAEALRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  157 SYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTV 236
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEV 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743447  237 ETSQGN-FTGDAILLATGRVPNTDLaLNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGG 297
Cdd:pfam07992 229 ILKDGTeIDADLVVVAIGRRPNTEL-LEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVG 289
 
Name Accession Description Interval E-value
chlor_oxi_RclA NF040477
reactive chlorine resistance oxidoreductase RclA;
1-438 2.33e-171

reactive chlorine resistance oxidoreductase RclA;


Pssm-ID: 439704 [Multi-domain]  Cd Length: 441  Bit Score: 487.75  E-value: 2.33e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVVKALNQ 80
Cdd:NF040477   1 MNHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMYGGTCINIGCIPTKTLVHDAEQHQDFSTAMQRKSSVVGFLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 KNYLNLENDENITLLNFKAQFKSNTEVELIDENGKLVqtLTADKILINTGAKSNIPNIEGIDSAQNVYDSKGLLNISYQP 160
Cdd:NF040477  81 KNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQE--LRGEKIFINTGAQSVLPPIPGLTTTPGVYDSTGLLNLTQLP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETSQ 240
Cdd:NF040477 159 ARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSHEGEVQLETAE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 241 GNFTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYISLDDFRILKSELFGDR 319
Cdd:NF040477 239 GVLTVDALLVASGRKPATAgLQLQNAGVAVNERGAIVVDKYLRTTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGEG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 320 SRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGKG 399
Cdd:NF040477 319 KRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVMNDTRGVLKAVVDNKTQRILGVSLLCVD 398
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 515743447 400 SEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:NF040477 399 SHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDLF 437
PRK07251 PRK07251
FAD-containing oxidoreductase;
1-440 8.76e-170

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 483.48  E-value: 8.76e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVVKALNQ 80
Cdd:PRK07251   1 MLTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAMYGGTCINIGCIPTKTLLVAAEKNLSFEQVMATKNTVTSRLRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 KNYLNLENDEnITLLNFKAQFKSNTEVELidENGKLVQTLTADKILINTGAKSNIPNIEGIDSAQNVYDSKGLLNISYQP 160
Cdd:PRK07251  81 KNYAMLAGSG-VDLYDAEAHFVSNKVIEV--QAGDEKIELTAETIVINTGAVSNVLPIPGLADSKHVYDSTGIQSLETLP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREdQEIVTHMINDFKDK-GVRLITNVETKALKNEGDLTTVETS 239
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPRE-EPSVAALAKQYMEEdGITFLLNAHTTEVKNDGDQVLVVTE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 240 QGNFTGDAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYISLDDFRILKSELFGD 318
Cdd:PRK07251 237 DETYRFDALLYATGRKPNTePLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 319 RSRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGK 398
Cdd:PRK07251 317 GSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGE 396
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 515743447 399 GSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLFNI 440
Cdd:PRK07251 397 GSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENLNDLFNI 438
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
1-438 1.33e-146

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: 425.27  E-value: 1.33e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLV-------------NDGIK----HVD 63
Cdd:COG1249    1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEK--GRLGGTCLNVGCIPSKALLhaaevahearhaaEFGISagapSVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  64 FSTAFSRKKEVVKALNqKNYLNLENDENITLLNFKAQFKSNTEVELIDEngklvQTLTADKILINTGAKSNIPNIEGIDS 143
Cdd:COG1249   79 WAALMARKDKVVDRLR-GGVEELLKKNGVDVIRGRARFVDPHTVEVTGG-----ETLTADHIVIATGSRPRVPPIPGLDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 144 AqNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVE 223
Cdd:COG1249  153 V-RVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAK 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 224 TKALKNEGDLTTVETSQGN----FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGL 298
Cdd:COG1249  232 VTSVEKTGDGVTVTLEDGGgeeaVEADKVLVATGRRPNTDgLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 299 QFTYISLDDFRILKSELFGDRSRHTeNRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGL 378
Cdd:COG1249  312 QLAHVASAEGRVAAENILGKKPRPV-DYRAIPSVVFTDPEIASVGLTEEEAREAGIDVKVGKFPFAANGRALALGETEGF 390
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 379 FKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:COG1249  391 VKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
1-440 3.04e-146

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 424.04  E-value: 3.04e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVVKALNQ 80
Cdd:PRK08010   1 MNKYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMYGGTCINIGCIPTKTLVHDAQQHTDFVRAIQRKNEVVNFLRN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 KNYLNLENDENITLLNFKAQFKSNTEVELIDENGKLVqtLTADKILINTGAKSNIPNIEGIDSAQNVYDSKGLLNISYQP 160
Cdd:PRK08010  81 KNFHNLADMPNIDVIDGQAEFINNHSLRVHRPEGNLE--IHGEKIFINTGAQTVVPPIPGITTTPGVYDSTGLLNLKELP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETSQ 240
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEH 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 241 GNFTGDAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYISLDDFRILKSELFGDR 319
Cdd:PRK08010 239 AQLAVDALLIASGRQPATaSLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 320 SRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGKG 399
Cdd:PRK08010 319 KRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVD 398
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 515743447 400 SEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLFNI 440
Cdd:PRK08010 399 SHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDLFSL 439
PRK06370 PRK06370
FAD-containing oxidoreductase;
1-438 6.20e-122

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 362.60  E-value: 6.20e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLV-------------NDGIK-----HV 62
Cdd:PRK06370   3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALIER--GLLGGTCVNTGCVPTKTLIasaraahlarraaEYGVSvggpvSV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  63 DFSTAFSRKKEVVKALNQKNYLNLENDENITLLNFKAQFKSNTEVELIDEngklvqTLTADKILINTGAKSNIPNIEGID 142
Cdd:PRK06370  81 DFKAVMARKRRIRARSRHGSEQWLRGLEGVDVFRGHARFESPNTVRVGGE------TLRAKRIFINTGARAAIPPIPGLD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 143 SAqNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNV 222
Cdd:PRK06370 155 EV-GYLTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 223 ETKALKNEGDLTTVETSQGN----FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGG 297
Cdd:PRK06370 234 ECIRVERDGDGIAVGLDCNGgapeITGSHILVAVGRVPNTDdLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGR 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 298 LQFTYISLDDFRILKSELFGDRSRHTENRgIIPYTVFIDPPLSRVGITASEAQQLNYNyventLFINTIPKHKI---NND 374
Cdd:PRK06370 314 GAFTHTAYNDARIVAANLLDGGRRKVSDR-IVPYATYTDPPLARVGMTEAEARKSGRR-----VLVGTRPMTRVgraVEK 387
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515743447 375 G--RGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:PRK06370 388 GetQGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLA 453
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
1-432 8.38e-102

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 310.96  E-value: 8.38e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVL-----------------VNDGIKHVD 63
Cdd:PRK06292   1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEK--GPLGGTCLNVGCIPSKALiaaaeafheakhaeefgIHADGPKID 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  64 FSTAFSRKKEVVKALNQKNYLNLENDENITLLNFKAQFKSNTEVElIDEngklvQTLTADKILINTGAKS-NIPNIEGID 142
Cdd:PRK06292  79 FKKVMARVRRERDRFVGGVVEGLEKKPKIDKIKGTARFVDPNTVE-VNG-----ERIEAKNIVIATGSRVpPIPGVWLIL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 143 SAQnVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKgVRLITNV 222
Cdd:PRK06292 153 GDR-LLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE-FKIKLGA 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 223 ETKALKNEGDLTTVETSQGN----FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGG 297
Cdd:PRK06292 231 KVTSVEKSGDEKVEELEKGGktetIEADYVLVATGRRPNTDgLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGK 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 298 LQFTYISLDDFRILKSELFGDRSRHtENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTL-FINTiPKHKINNDGR 376
Cdd:PRK06292 311 PPLLHEAADEGRIAAENAAGDVAGG-VRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVpFEAQ-GRARVMGKND 388
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515743447 377 GLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAE 432
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
3-432 5.82e-90

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: 280.30  E-value: 5.82e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    3 HYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLVN-----DGIKH------------VDFS 65
Cdd:TIGR01350   1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEK--EYLGGTCLNVGCIPTKALLHsaevyDEIKHakdlgievenvsVDWE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   66 TAFSRKKEVVKALNQK-NYLNLENdeNITLLNFKAQFKSNTEVELIDENGKlvQTLTADKILINTGAKSNIPNIEGIDSA 144
Cdd:TIGR01350  79 KMQKRKNKVVKKLVGGvSGLLKKN--KVTVIKGEAKFLDPGTVSVTGENGE--ETLEAKNIIIATGSRPRSLPGPFDFDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  145 QNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVET 224
Cdd:TIGR01350 155 KVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  225 KALKNEGDLTTVETSQGNF---TGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQF 300
Cdd:TIGR01350 235 TAVEKNDDQVTYENKGGETetlTGEKVLVAVGRKPNTEgLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPML 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  301 TYISLDDFRILKSELFGDRSRHTeNRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFK 380
Cdd:TIGR01350 315 AHVASHEGIVAAENIAGKEPAHI-DYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGKALALGETDGFVK 393
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 515743447  381 VVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAE 432
Cdd:TIGR01350 394 IIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
4-433 2.32e-88

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: 276.61  E-value: 2.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTesYGGTCINHGCIPSKVLVNDG-IKH---------------VDFSTA 67
Cdd:TIGR02053   1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGP--LGGTCVNVGCVPSKMLLRAAeVAHyarkppfgglaatvaVDFGEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   68 FSRKKEVVKALNQKNYLNLENDENITLLNFKAQFKSNTEVELIDENgklvQTLTADKILINTGAKSNIPNIEGIDSAqNV 147
Cdd:TIGR02053  79 LEGKREVVEELRHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDLGR----EVRGAKRFLIATGARPAIPPIPGLKEA-GY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  148 YDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKAL 227
Cdd:TIGR02053 154 LTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  228 K--NEGDLTTVET--SQGNFTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTY 302
Cdd:TIGR02053 234 SvrGGGKIITVEKpgGQGEVEADELLVATGRRPNTDgLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  303 ISLDDFRILKSELFGDRSRhTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVV 382
Cdd:TIGR02053 314 VAAKEGVVAAENALGGANA-KLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLV 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 515743447  383 INKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAES 433
Cdd:TIGR02053 393 AEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEG 443
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
2-432 2.27e-79

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 253.14  E-value: 2.27e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   2 THYNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLVN-----DGIKH------------VDF 64
Cdd:PRK06416   3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEK--EKLGGTCLNRGCIPSKALLHaaeraDEARHsedfgikaenvgIDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  65 STAFSRKKEVVKALNqKNYLNLENDENITLLNFKAQFKSNTEVELIDENGKlvQTLTADKILINTGAKS-NIPNIEgIDs 143
Cdd:PRK06416  81 KKVQEWKNGVVNRLT-GGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGE--QTYTAKNIILATGSRPrELPGIE-ID- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 144 AQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVE 223
Cdd:PRK06416 156 GRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAK 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 224 -TKALKNEGDLT-TVETSQGN--FTGDAILLATGRVPNTD-LALNNTDIELgTHGEIKVNNHLQTSVSHIYAAGDVKGGL 298
Cdd:PRK06416 236 aKKVEQTDDGVTvTLEDGGKEetLEADYVLVAVGRRPNTEnLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 299 QFTYislddfR-----ILKSELFGDRSRHTENRGiIPYTVFIDPPLSRVGITASEAQQLNYNY-VENTLFI-NtiPKHKI 371
Cdd:PRK06416 315 MLAH------KasaegIIAAEAIAGNPHPIDYRG-IPAVTYTHPEVASVGLTEAKAKEEGFDVkVVKFPFAgN--GKALA 385
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743447 372 NNDGRGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAE 432
Cdd:PRK06416 386 LGETDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
PRK06116 PRK06116
glutathione reductase; Validated
1-434 1.29e-72

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 235.05  E-value: 1.29e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFteSYGGTCINHGCIPSKVLV------------------NDGIKHV 62
Cdd:PRK06116   2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAK--RLGGTCVNVGCVPKKLMWygaqiaeafhdyapgygfDVTENKF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  63 DFSTAFSRKKEVVKALNQkNYLNLENDENITLLNFKAQFKSNTEVELideNGKLVqtlTADKILINTGAKSNIPNIEGid 142
Cdd:PRK06116  80 DWAKLIANRDAYIDRLHG-SYRNGLENNGVDLIEGFARFVDAHTVEV---NGERY---TADHILIATGGRPSIPDIPG-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 143 sAQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNV 222
Cdd:PRK06116 151 -AEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 223 ETKAL-KNEGDLTTVETSQGN-FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQ 299
Cdd:PRK06116 230 VPKAVeKNADGSLTLTLEDGEtLTVDCLIWAIGREPNTDgLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 300 FTYISLDDFRILKSELFGDRSRHTENRGIIPYTVFIDPPLSRVGITASEA-QQLNYNYVE--NTLFI---NTIPKHkinn 373
Cdd:PRK06116 310 LTPVAIAAGRRLSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEArEQYGEDNVKvyRSSFTpmyTALTGH---- 385
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515743447 374 DGRGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESF 434
Cdd:PRK06116 386 RQPCLMKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEF 446
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
1-434 6.38e-69

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 225.81  E-value: 6.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQfTESYGGTCINHGCIPSKVL----------------VNDGIK-HVD 63
Cdd:PRK05249   3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIER-YRNVGGGCTHTGTIPSKALreavlrligfnqnplySSYRVKlRIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  64 FSTAFSRKKEVVKAlnQKNYLNLENDEN-ITLLNFKAQFKSNTEVELIDENGKlVQTLTADKILINTGAKSNIPniEGID 142
Cdd:PRK05249  82 FADLLARADHVINK--QVEVRRGQYERNrVDLIQGRARFVDPHTVEVECPDGE-VETLTADKIVIATGSRPYRP--PDVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 143 -SAQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITN 221
Cdd:PRK05249 157 fDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHN 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 222 VETKALKNEGDLTTVETSQGN-FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKG--G 297
Cdd:PRK05249 237 EEVEKVEGGDDGVIVHLKSGKkIKADCLLYANGRTGNTDgLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGfpS 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 298 LQFTyiSLDDFRILKSELFGDRSRHTENrgIIP---YTVfidPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINND 374
Cdd:PRK05249 317 LASA--SMDQGRIAAQHAVGEATAHLIE--DIPtgiYTI---PEISSVGKTEQELTAAKVPYEVGRARFKELARAQIAGD 389
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515743447 375 GRGLFKVVINKDNNEILGATLYGKGSEEIINlIKLAIDQH---IPYQVlrDNIYTHPTIAESF 434
Cdd:PRK05249 390 NVGMLKILFHRETLEILGVHCFGERATEIIH-IGQAIMEQkgtIEYFV--NTTFNYPTMAEAY 449
PRK13748 PRK13748
putative mercuric reductase; Provisional
8-432 8.73e-62

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 209.62  E-value: 8.73e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   8 VIGFGKAGKTLAKYASSQGQQVALIEQFTesYGGTCINHGCIPSKVLV--------------NDGIKH----VDFSTAFS 69
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIERGT--IGGTCVNVGCVPSKIMIraahiahlrrespfDGGIAAtvptIDRSRLLA 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  70 RKKEVVKALNQKNYLN-LENDENITLLNFKAQFK-SNTEVELIDENGKlvQTLTADKILINTGAKSNIPNIEGIDSAQNV 147
Cdd:PRK13748 181 QQQARVDELRHAKYEGiLDGNPAITVLHGEARFKdDQTLIVRLNDGGE--RVVAFDRCLIATGASPAVPPIPGLKETPYW 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 148 YDSKGLLNISYqPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMaREDQEIVTHMINDFKDKGVRLITNVETKAL 227
Cdd:PRK13748 259 TSTEALVSDTI-PERLAVIGSSVVALELAQAFARLGSKVTILARSTLFF-REDPAIGEAVTAAFRAEGIEVLEHTQASQV 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 228 KNEGDLTTVETSQGNFTGDAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQFTYIsld 306
Cdd:PRK13748 337 AHVDGEFVLTTGHGELRADKLLVATGRAPNTrSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYV--- 413
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 307 dfrilkSELFGDRS-------RHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLF 379
Cdd:PRK13748 414 ------AAAAGTRAainmtggDAALDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRALANFDTRGFI 487
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515743447 380 KVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAE 432
Cdd:PRK13748 488 KLVIEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTMVE 540
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
4-297 6.01e-60

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: 197.54  E-value: 6.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQftesyGGTCINHGCIPSKVLVNDGIKHVDFST---AFSRKKEVVKALNQ 80
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED-----EGTCPYGGCVLSKALLGAAEAPEIASLwadLYKRKEEVVKKLNN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   81 kNYLNLENDENITLLNFKAQFKSNtevELIDENGklvQTLTADKILINTGAKSNIPNIEGIDSAQN----VYDSKGLLNI 156
Cdd:pfam07992  76 -GIEVLLGTEVVSIDPGAKKVVLE---ELVDGDG---ETITYDRLVIATGARPRLPPIPGVELNVGflvrTLDSAEALRL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  157 SYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTV 236
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEV 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743447  237 ETSQGN-FTGDAILLATGRVPNTDLaLNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGG 297
Cdd:pfam07992 229 ILKDGTeIDADLVVVAIGRRPNTEL-LEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVG 289
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
1-433 6.79e-60

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 202.46  E-value: 6.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTE-----SYGGTCINHGCIPSKVLVN-----DGIKH--------- 61
Cdd:PRK06327   2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNpkgkpALGGTCLNVGCIPSKALLAsseefENAGHhfadhgihv 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  62 ----VDFSTAFSRKKEVVKALNQK-NYLNLENdeNITLLNFKAQFKSN----TEVELIDENGKlvqTLTADKILINTGAK 132
Cdd:PRK06327  82 dgvkIDVAKMIARKDKVVKKMTGGiEGLFKKN--KITVLKGRGSFVGKtdagYEIKVTGEDET---VITAKHVIIATGSE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 133 S-NIPNIEgIDSaQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDF 211
Cdd:PRK06327 157 PrHLPGVP-FDN-KIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 212 KDKGVRLITNVETKALKNEGDLTTVETSQGN-----FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSV 285
Cdd:PRK06327 235 TKQGLDIHLGVKIGEIKTGGKGVSVAYTDADgeaqtLEVDKLIVSIGRVPNTDgLGLEAVGLKLDERGFIPVDDHCRTNV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 286 SHIYAAGDVKGGLQFTYISLDDfRILKSELFGDRSRHTeNRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINT 365
Cdd:PRK06327 315 PNVYAIGDVVRGPMLAHKAEEE-GVAVAERIAGQKGHI-DYNTIPWVIYTSPEIAWVGKTEQQLKAEGVEYKAGKFPFMA 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743447 366 IPKHKINNDGRGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAES 433
Cdd:PRK06327 393 NGRALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEV 460
PLN02546 PLN02546
glutathione reductase
4-434 4.62e-57

glutathione reductase


Pssm-ID: 215301 [Multi-domain]  Cd Length: 558  Bit Score: 197.02  E-value: 4.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIE--------QFTESYGGTCINHGCIPSKVLVndgikhvdFSTAFSRKKEVV 75
Cdd:PLN02546  80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissDTLGGVGGTCVLRGCVPKKLLV--------YASKYSHEFEES 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  76 KALNQKNYLNLENDENITLLNFKAQFK----------SNTEVELIDENGKLV---------QTLTADKILINTGAKSNIP 136
Cdd:PLN02546 152 RGFGWKYETEPKHDWNTLIANKNAELQrltgiyknilKNAGVTLIEGRGKIVdphtvdvdgKLYTARNILIAVGGRPFIP 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 137 NIEGIdsaQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGV 216
Cdd:PLN02546 232 DIPGI---EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGI 308
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 217 RLITNVETKALKNEGD-LTTVETSQGNFTG-DAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGD 293
Cdd:PLN02546 309 EFHTEESPQAIIKSADgSLSLKTNKGTVEGfSHVMFATGRKPNTkNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGD 388
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 294 VKGGLQFTYISLDDFRILKSELFGDRSRHTENRGiIPYTVFIDPPLSRVGITASEAQQlnyNYVENTLFINTIPKHKINN 373
Cdd:PLN02546 389 VTDRINLTPVALMEGGALAKTLFGNEPTKPDYRA-VPSAVFSQPPIGQVGLTEEQAIE---EYGDVDVFTANFRPLKATL 464
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515743447 374 DG---RGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESF 434
Cdd:PLN02546 465 SGlpdRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEF 528
PRK07846 PRK07846
mycothione reductase; Reviewed
3-397 4.93e-55

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 189.01  E-value: 4.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   3 HYNLIVIGFGkAGKTL--AKYAssqGQQVALIEQFTesYGGTCINHGCIPSKVLVN-----DGIKH-----VDFSTAFSR 70
Cdd:PRK07846   1 HYDLIIIGTG-SGNSIldERFA---DKRIAIVEKGT--FGGTCLNVGCIPTKMFVYaadvaRTIREaarlgVDAELDGVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  71 KKEVVK---------ALNQKNYLNLENDeNITLLNFKAQFKSNTEVELIDENgklvqTLTADKILINTGAKSNIPNIEGI 141
Cdd:PRK07846  75 WPDIVSrvfgridpiAAGGEEYRGRDTP-NIDVYRGHARFIGPKTLRTGDGE-----EITADQVVIAAGSRPVIPPVIAD 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 142 DSAQnVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIvTHMINDFKDKGVRLITN 221
Cdd:PRK07846 149 SGVR-YHTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDI-SERFTELASKRWDVRLG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 222 VETKALKNEGDLTTVETSQGN-FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKGGLQ 299
Cdd:PRK07846 227 RNVVGVSQDGSGVTLRLDDGStVEADVLLVATGRVPNGDlLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQ 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 300 FTYISLDDFRILKSELFGDRSRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNYVEntlfintipkhKINN------ 373
Cdd:PRK07846 307 LKHVANHEARVVQHNLLHPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAAGLDITV-----------KVQNygdvay 375
                        410       420
                 ....*....|....*....|....*....
gi 515743447 374 -----DGRGLFKVVINKDNNEILGATLYG 397
Cdd:PRK07846 376 gwameDTTGFVKLIADRDTGRLLGAHIIG 404
PLN02507 PLN02507
glutathione reductase
4-434 8.08e-53

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 184.25  E-value: 8.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIE--------QFTESYGGTCINHGCIPSKVLVNDGIKHVDFSTAFSRKKEVV 75
Cdd:PLN02507  26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEIN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  76 KAL--NQKNYLNLENDENITLLNFKAQFKSNTEVELIDENGKLV--------------QTLTADKILINTGAKSNIPNIE 139
Cdd:PLN02507 106 EKVdfNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVgpnevevtqldgtkLRYTAKHILIATGSRAQRPNIP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 140 GIDSAqnvYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLeYNKQFMARE-DQEIVTHMINDFKDKGVRL 218
Cdd:PLN02507 186 GKELA---ITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLF-FRKELPLRGfDDEMRAVVARNLEGRGINL 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 219 --ITNVeTKALKNEGDLTTVETSQGNFTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVK 295
Cdd:PLN02507 262 hpRTNL-TQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKrLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVT 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 296 GGLQFTYISLDDFRILKSELFGDRSRHTENRGiIPYTVFIDPPLSRVGItaSEAQQLNYNYVENTLFINTIPKHKINNDG 375
Cdd:PLN02507 341 NRINLTPVALMEGTCFAKTVFGGQPTKPDYEN-VACAVFCIPPLSVVGL--SEEEAVEQAKGDILVFTSSFNPMKNTISG 417
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515743447 376 R---GLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESF 434
Cdd:PLN02507 418 RqekTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEF 479
mycothione_red TIGR03452
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ...
2-432 9.04e-51

mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.


Pssm-ID: 132493 [Multi-domain]  Cd Length: 452  Bit Score: 178.03  E-value: 9.04e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    2 THYNLIVIGFGkAGKTLA--KYAssqGQQVALIEQFTesYGGTCINHGCIPSKVLV-----------------NDGIKHV 62
Cdd:TIGR03452   1 RHYDLIIIGTG-SGNSIPdpRFA---DKRIAIVEKGT--FGGTCLNVGCIPTKMFVyaaevaqsigesarlgiDAEIDSV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   63 DFSTAFSR---KKEVVKALNQKNYLNLENDENITLLNFKAQFKSntEVELIDENGklvQTLTADKILINTGAKSNIPNIE 139
Cdd:TIGR03452  75 RWPDIVSRvfgDRIDPIAAGGEDYRRGDETPNIDVYDGHARFVG--PRTLRTGDG---EEITGDQIVIAAGSRPYIPPAI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  140 gIDSAQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIvTHMINDFKDK--GVR 217
Cdd:TIGR03452 150 -ADSGVRYHTNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKLLRHLDEDI-SDRFTEIAKKkwDIR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  218 LITNVetKALKNEGDLTTVETSQGN-FTGDAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVK 295
Cdd:TIGR03452 228 LGRNV--TAVEQDGDGVTLTLDDGStVTADVLLVATGRVPNGDlLDAEAAGVEVDEDGRIKVDEYGRTSARGVWALGDVS 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  296 GGLQFTYISLDDFRILKSELFGDRSRHTENRGIIPYTVFIDPPLSRVGITASEAQQLNYNyventlfINTipkhKINN-- 373
Cdd:TIGR03452 306 SPYQLKHVANAEARVVKHNLLHPNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHD-------ITV----KIQNyg 374
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743447  374 ---------DGRGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQ-VLRDNIYTHPTIAE 432
Cdd:TIGR03452 375 dvaygwameDTTGFCKLIADRDTGKLLGAHIIGPQASSLIQPLITAMAFGLDAReMARKQYWIHPALPE 443
TGR TIGR01438
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ...
4-438 4.97e-50

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: 176.58  E-value: 4.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTES-------YGGTCINHGCIPSKVL-------------------VND 57
Cdd:TIGR01438   3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTplgtrwgIGGTCVNVGCIPKKLMhqaallgqalkdsrnygwkVEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   58 GIKHvDFSTAFSRKKEVVKALNQkNYLNLENDENITLLNFKAQFKSNTEVELIDENGKlVQTLTADKILINTGAKSNIPN 137
Cdd:TIGR01438  83 TVKH-DWKRLVEAVQNHIGSLNW-GYRVALREKKVKYENAYAEFVDKHRIKATNKKGK-EKIYSAERFLIATGERPRYPG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  138 IEGidSAQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYN---KQFmareDQEIVTHMINDFKDK 214
Cdd:TIGR01438 160 IPG--AKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSillRGF----DQDCANKVGEHMEEH 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  215 GVRLITNVETKALKNEGDLTTVETSQGNFTG----DAILLATGRVPNTD-LALNNTDIELG-THGEIKVNNHLQTSVSHI 288
Cdd:TIGR01438 234 GVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIeeeyDTVLLAIGRDACTRkLNLENVGVKINkKTGKIPADEEEQTNVPYI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  289 YAAGDV-KGGLQFTYISLDDFRILKSELFGDRSRHTENRGiIPYTVFIDPPLSRVGITASEAQQLnynYVENTL------ 361
Cdd:TIGR01438 314 YAVGDIlEDKPELTPVAIQAGRLLAQRLFKGSTVICDYEN-VPTTVFTPLEYGACGLSEEKAVEK---FGEENVevfhsy 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  362 FIN---TIPKHKinNDGRGLFKVVIN-KDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDL 437
Cdd:TIGR01438 390 FWPlewTIPSRD--NHNKCYAKLVCNkKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467

                  .
gi 515743447  438 F 438
Cdd:TIGR01438 468 S 468
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
4-432 6.69e-47

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: 168.23  E-value: 6.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447    4 YNLIVIGFGKAGKTLAKYASS-QGQQVALIE-------QFTESYGGTCINHGCIPSKVLVNdGIKHVD-------FSTAF 68
Cdd:TIGR01423   4 FDLVVIGAGSGGLEAGWNAATlYKKRVAVVDvqthhgpPFYAALGGTCVNVGCVPKKLMVT-GAQYMDtlresagFGWEF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   69 SRK------KEVVKALNQ------KNYLNLEND-ENITL-LNFKAQFKSNTEV--ELIDENGKLVQTLTADKILINTGAK 132
Cdd:TIGR01423  83 DRSsvkanwKALIAAKNKavldinKSYEGMFADtEGLTFfLGWGALEDKNVVLvrESADPKSAVKERLQAEHILLATGSW 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  133 SNIPNIEGIDsaqNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSF---GTNVTVLEYNKQFMAREDQEIVTHMIN 209
Cdd:TIGR01423 163 PQMLGIPGIE---HCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNMILRGFDSTLRKELTK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  210 DFKDKGVRLITNVE-TKALKN-EGDLTTVETSQGNFTGDAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVS 286
Cdd:TIGR01423 240 QLRANGINIMTNENpAKVTLNaDGSKHVTFESGKTLDVDVVMMAIGRVPRTqTLQLDKVGVELTKKGAIQVDEFSRTNVP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  287 HIYAAGDVKGGLQFTYISLDDFRILKSELFGDRSRHTENRGIIPyTVFIDPPLSRVGITASEAQQlNYNYVENTLFINTI 366
Cdd:TIGR01423 320 NIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVAS-AVFSIPPIGTCGLVEEDAAK-KFEKVAVYESSFTP 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743447  367 PKHKINNDGRGLF--KVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAE 432
Cdd:TIGR01423 398 LMHNISGSKYKKFvaKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
93-294 3.54e-43

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: 154.20  E-value: 3.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  93 TLLNFKAQFKSNTEVELIDENGKLV-----QTLTADKILINTGAKSNIPNIEGIDsAQNVYDSKGL---LNI-----SYQ 159
Cdd:COG0446   45 SFERKGIDVRTGTEVTAIDPEAKTVtlrdgETLSYDKLVLATGARPRPPPIPGLD-LPGVFTLRTLddaDALrealkEFK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 160 PKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETS 239
Cdd:COG0446  124 GKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTD 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515743447 240 QGNFTGDAILLATGRVPNTDLAlNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDV 294
Cdd:COG0446  204 GEEIPADLVVVAPGVRPNTELA-KDAGLALGERGWIKVDETLQTSDPDVYAAGDC 257
PTZ00058 PTZ00058
glutathione reductase; Provisional
4-434 7.07e-43

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 158.63  E-value: 7.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLVN--------DGIKHVDFSTAFS------ 69
Cdd:PTZ00058  49 YDLIVIGGGSGGMAAARRAARNKAKVALVEK--DYLGGTCVNVGCVPKKIMFNaasihdilENSRHYGFDTQFSfnlpll 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  70 --RKKEVVKALNQKNYLNLENDeNITLLNFKAQFKSNTEVELI--------------------------DENGklvQTLT 121
Cdd:PTZ00058 127 veRRDKYIRRLNDIYRQNLKKD-NVEYFEGKGSLLSENQVLIKkvsqvdgeadesdddevtivsagvsqLDDG---QVIE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 122 ADKILINTGAKSNIPNIEGIdsaQNVYDSKGLLNISyQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQ 201
Cdd:PTZ00058 203 GKNILIAVGNKPIFPDVKGK---EFTISSDDFFKIK-EAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDE 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 202 EIVTHMINDFKDKGVRLITNVETKAL---KNEGDLTTVETSQGNFTGDAILLATGRVPNTDlALNNTDIELGT-HGEIKV 277
Cdd:PTZ00058 279 TIINELENDMKKNNINIITHANVEEIekvKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTE-DLNLKALNIKTpKGYIKV 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 278 NNHLQTSVSHIYAAGDVKG----------------------------------GLQFTYISLDDFRILKSELFGDRSRhT 323
Cdd:PTZ00058 358 DDNQRTSVKHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRLLADRLFGPFSR-T 436
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 324 ENRGIIPYTVFIDPPLSRVGITasEAQQLNYNYVEN-----TLFIN---TIPKHKINNDGRGLFKVVINKDNNEILGATL 395
Cdd:PTZ00058 437 TNYKLIPSVIFSHPPIGTIGLS--EQEAIDIYGKENvkiyeSRFTNlffSVYDMDPAQKEKTYLKLVCVGKEELIKGLHI 514
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 515743447 396 YGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESF 434
Cdd:PTZ00058 515 VGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEF 553
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
89-294 1.14e-38

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 144.13  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  89 DENITLLnfkaqfkSNTEVELIDENGKLV-----QTLTADKILINTGAKSNIPNIEGIDsAQNVY------DSKGLLNIS 157
Cdd:COG1251   68 ENGIDLR-------LGTRVTAIDRAARTVtladgETLPYDKLVLATGSRPRVPPIPGAD-LPGVFtlrtldDADALRAAL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 158 YQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMARE-DQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTV 236
Cdd:COG1251  140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQlDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGV 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515743447 237 ETSQGN-FTGDAILLATGRVPNTDLAlNNTDIELGtHGeIKVNNHLQTSVSHIYAAGDV 294
Cdd:COG1251  220 RLADGEeLPADLVVVAIGVRPNTELA-RAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDC 275
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
102-411 4.28e-37

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 140.56  E-value: 4.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 102 KSNTEVELIDENGKLVQ----------TLTADKILINTGAKSNIPNIEGIDsAQNVY------DSKGLLNISYQP--KEL 163
Cdd:PRK09564  74 KTEHEVVKVDAKNKTITvknlktgsifNDTYDKLMIATGARPIIPPIKNIN-LENVYtlksmeDGLALKELLKDEeiKNI 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 164 VIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMARE-DQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETSQGN 242
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSfDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGE 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 243 FTGDAILLATGRVPNTDLaLNNTDIELGTHGEIKVNNHLQTSVSHIYAAGD-------VKGglQFTYISLDDF-----RI 310
Cdd:PRK09564 233 YEADVVIVATGVKPNTEF-LEDTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSN--KNVYVPLATTanklgRM 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 311 LKSELFGdrsRHTENRGIIPYTVF--IDPPLSRVGITASEAQQLNYNYveNTLFINTIPKHKINNDGRGLF-KVVINKDN 387
Cdd:PRK09564 310 VGENLAG---RHVSFKGTLGSACIkvLDLEAARTGLTEEEAKKLGIDY--KTVFIKDKNHTNYYPGQEDLYvKLIYEADT 384
                        330       340
                 ....*....|....*....|....*
gi 515743447 388 NEILGATLYGK-GSEEIINLIKLAI 411
Cdd:PRK09564 385 KVILGGQIIGKkGAVLRIDALAVAI 409
PTZ00153 PTZ00153
lipoamide dehydrogenase; Provisional
4-438 9.61e-33

lipoamide dehydrogenase; Provisional


Pssm-ID: 173442 [Multi-domain]  Cd Length: 659  Bit Score: 130.80  E-value: 9.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTESYGGTCINHGCIPSKVLVNDGIKHVD------------FSTAFSRK 71
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDDSIGGTCVNVGCIPSKALLYATGKYRElknlaklytygiYTNAFKNG 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  72 KEVVKALNQknYLNLENDENITLLNFKAQ------------------FKSNTE-VELIDENGKLVQTLTA---------- 122
Cdd:PTZ00153 197 KNDPVERNQ--LVADTVQIDITKLKEYTQsvidklrggienglkskkFCKNSEhVQVIYERGHIVDKNTIkseksgkefk 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 123 -DKILINTGAKSNIPNIEGIDSaQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQ 201
Cdd:PTZ00153 275 vKNIIIATGSTPNIPDNIEVDQ-KSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDA 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 202 EIVTHMINDF-KDKGVRLITNVETKALKNEGDLTTV-----ETSQGNFTG-------------DAILLATGRVPNTD-LA 261
Cdd:PTZ00153 354 DVAKYFERVFlKSKPVRVHLNTLIEYVRAGKGNQPViighsERQTGESDGpkknmndiketyvDSCLVATGRKPNTNnLG 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 262 LNNTDIELgTHGEIKVNNHLQTS------VSHIYAAGDVKGGLQFTY------------ISLDDFRILKSELFGDRSRhT 323
Cdd:PTZ00153 434 LDKLKIQM-KRGFVSVDEHLRVLredqevYDNIFCIGDANGKQMLAHtashqalkvvdwIEGKGKENVNINVENWASK-P 511
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 324 ENRGIIPYTVFIDPPLSRVGITASEAQQLNYN----------------YVENTLFINTIPK--------HKINNDGRGLF 379
Cdd:PTZ00153 512 IIYKNIPSVCYTTPELAFIGLTEKEAKELYPPdnvgveisfykanskvLCENNISFPNNSKnnsynkgkYNTVDNTEGMV 591
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515743447 380 KVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFNDLF 438
Cdd:PTZ00153 592 KIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDAAF 650
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
4-438 1.59e-32

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 128.79  E-value: 1.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIEQFTES-------YGGTCINHGCIPSKVLVNDG----IKHVD-------FS 65
Cdd:PTZ00052   6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPStqgtkwgLGGTCVNVGCVPKKLMHYAAnigsIFHHDsqmygwkTS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  66 TAFSRKKEV------VKALNqKNYLNLENDENITLLNFKAQFKSNTEVELIDENGKlvQTLTADKILINTGAKSNIP-NI 138
Cdd:PTZ00052  86 SSFNWGKLVttvqnhIRSLN-FSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQE--ETITAKYILIATGGRPSIPeDV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 139 EGidSAQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEynKQFMARE-DQEIVTHMINDFKDKGVR 217
Cdd:PTZ00052 163 PG--AKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAV--RSIPLRGfDRQCSEKVVEYMKEQGTL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 218 LITNVETKALKNEGDLTTVETSQGNFTG-DAILLATGRVPNTD-LALNNTDIELGTHGEIKVNNHLqTSVSHIYAAGDVK 295
Cdd:PTZ00052 239 FLEGVVPINIEKMDDKIKVLFSDGTTELfDTVLYATGRKPDIKgLNLNAIGVHVNKSNKIIAPNDC-TNIPNIFAVGDVV 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 296 GGL-QFTYISLDDFRILKSELFGDrSRHTENRGIIPYTVFIDPPLSRVGITASEA-QQLNYNYVE------NTLFINTIP 367
Cdd:PTZ00052 318 EGRpELTPVAIKAGILLARRLFKQ-SNEFIDYTFIPTTIFTPIEYGACGYSSEAAiAKYGEDDIEeylqefNTLEIAAVH 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 368 KHKINNDGRGLFK-----------VVINKDNNEILGATLYGKGSEEIINLIKLAIDQHIPYQVLRDNIYTHPTIAESFND 436
Cdd:PTZ00052 397 REKHERARKDEYDfdvssnclaklVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMN 476

                 ..
gi 515743447 437 LF 438
Cdd:PTZ00052 477 LS 478
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
6-415 1.77e-27

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 113.80  E-value: 1.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   6 LIVIGFGKAGKTLAKYASSQGQQVALIEQftESYGGTCINHGCIPSKVLV--------------------NDGIKHVDFS 65
Cdd:PRK07845   4 IVIIGGGPGGYEAALVAAQLGADVTVIER--DGLGGAAVLTDCVPSKTLIataevrtelrraaelgirfiDDGEARVDLP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  66 TAFSRkkevVKALNQKNYLNLEN---DENITLLNFKAQFKSNT----EVELIDENGKlVQTLTADKILINTGA-----KS 133
Cdd:PRK07845  82 AVNAR----VKALAAAQSADIRArleREGVRVIAGRGRLIDPGlgphRVKVTTADGG-EETLDADVVLIATGAsprilPT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 134 NIPNIEGIDSAQNVYDSKGLlnisyqPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKD 213
Cdd:PRK07845 157 AEPDGERILTWRQLYDLDEL------PEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFAR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 214 KGVRLITNVETKALKNEGDLTTVETSQGN-FTGDAILLATGRVPNT-DLALNNTDIELGTHGEIKVNNHLQTSVSHIYAA 291
Cdd:PRK07845 231 RGMTVLKRSRAESVERTGDGVVVTLTDGRtVEGSHALMAVGSVPNTaGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAA 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 292 GDVKGGLQFTYISLDDFRILKSELFGDRSRHTENRGIIPyTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKI 371
Cdd:PRK07845 311 GDCTGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVAS-NVFTRPEIATVGVSQAAIDSGEVPARTVMLPLATNPRAKM 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 515743447 372 NNDGRGLFKVVINKDNNEILGATLYGKGSEEIINLIKLAIDQHI 415
Cdd:PRK07845 390 SGLRDGFVKLFCRPGTGVVIGGVVVAPRASELILPIALAVQNRL 433
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-294 2.20e-26

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 107.90  E-value: 2.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIE------QFTESyggTCI-NHGCIPSKV----LVNDGIKHVDfstafsrkk 72
Cdd:COG0492    1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEggepggQLATT---KEIeNYPGFPEGIsgpeLAERLREQAE--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  73 evvkalnqknylnlendenitllNFKAQFKsNTEVELID--ENGKLVQT-----LTADKILINTGAKSNIPNIEGIDSaq 145
Cdd:COG0492   69 -----------------------RFGAEIL-LEEVTSVDkdDGPFRVTTddgteYEAKAVIIATGAGPRKLGLPGEEE-- 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 146 nvYDSKGllnISYQP---------KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAreDQEIVTHMindFKDKGV 216
Cdd:COG0492  123 --FEGRG---VSYCAtcdgfffrgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA--SKILVERL---RANPKI 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 217 RLITNVETKALKNEGDLTTVETSQGNfTG-------DAILLATGRVPNTDLaLNNTDIELGTHGEIKVNNHLQTSVSHIY 289
Cdd:COG0492  193 EVLWNTEVTEIEGDGRVEGVTLKNVK-TGeekelevDGVFVAIGLKPNTEL-LKGLGLELDEDGYIVVDEDMETSVPGVF 270

                 ....*
gi 515743447 290 AAGDV 294
Cdd:COG0492  271 AAGDV 275
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
77-401 2.19e-20

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 94.12  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   77 ALNQKNYLNlenDENITLLnfkaqfkSNTEVELIDENGKLV-----QTLTADKILINTGAKSNIPNIEGIDSaQNVY--- 148
Cdd:TIGR02374  57 TLNSKDWYE---KHGITLY-------TGETVIQIDTDQKQVitdagRTLSYDKLILATGSYPFILPIPGADK-KGVYvfr 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  149 ---DSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMARE-DQEIVTHMINDFKDKGVRLITNVET 224
Cdd:TIGR02374 126 tieDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQlDQTAGRLLQRELEQKGLTFLLEKDT 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  225 KALKNEGDLTTVETSQGN-FTGDAILLATGRVPNTDLAlnnTDIELGTHGEIKVNNHLQTSVSHIYAAGDVKG--GLQFT 301
Cdd:TIGR02374 206 VEIVGATKADRIRFKDGSsLEADLIVMAAGIRPNDELA---VSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEhnGRVYG 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  302 YIS--LDDFRILKSELFGdrSRHTENRGIIPYTvfidpPLSRVGITASEAQQLNYNyvENTLFIntipkhKINNDGRGLF 379
Cdd:TIGR02374 283 LVAplYEQAKVLADHICG--VECEEYEGSDLSA-----KLKLLGVDVWSAGDAQET--ERTTSI------KIYDEQKGIY 347
                         330       340
                  ....*....|....*....|..
gi 515743447  380 KVVINKDNNeILGATLYGKGSE 401
Cdd:TIGR02374 348 KKLVLSDDK-LLGAVLFGDTSD 368
Pyr_redox_dim pfam02852
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ...
329-434 3.27e-20

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: 85.30  E-value: 3.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  329 IPYTVFIDPPLSRVGITASEAQQLNYNYVENTLFINTIPKHKINNDGRGLFKVVINKDNNEILGATLYGKGSEEIINLIK 408
Cdd:pfam02852   1 IPSVVFTDPEIASVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQEAA 80
                          90       100
                  ....*....|....*....|....*.
gi 515743447  409 LAIDQHIPYQVLRDNIYTHPTIAESF 434
Cdd:pfam02852  81 LAIKMGATVEDLANTIHIHPTLSEAL 106
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
91-293 3.44e-19

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 88.82  E-value: 3.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  91 NITLLnfkaqfkSNTEVELIDENGKLV----QTLTADKILINTGAKSNIPNIEG------IDSAQNVYDSKGLLNisyQP 160
Cdd:PRK04965  72 NLRLF-------PHTWVTDIDAEAQVVksqgNQWQYDKLVLATGASAFVPPIPGrelmltLNSQQEYRAAETQLR---DA 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAR-EDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETS 239
Cdd:PRK04965 142 QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASlMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLD 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515743447 240 QG-NFTGDAILLATGRVPNTDLALN-NTDIELGthgeIKVNNHLQTSVSHIYAAGD 293
Cdd:PRK04965 222 SGrSIEVDAVIAAAGLRPNTALARRaGLAVNRG----IVVDSYLQTSAPDIYALGD 273
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
163-241 2.72e-17

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: 76.09  E-value: 2.72e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743447  163 LVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVETSQG 241
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
105-294 1.60e-15

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 78.04  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 105 TEVELIDENGklvQTLTADKILINTGAKSN-IPNIEGIdsAQNVY------DSKGLLNISYQPKELVIIGGGYIALEFAS 177
Cdd:PRK09754  87 DTRELVLTNG---ESWHWDQLFIATGAAARpLPLLDAL--GERCFtlrhagDAARLREVLQPERSVVIVGAGTIGLELAA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 178 MFQSFGTNVTVLEYNKQFMAREDQEIVT-HMINDFKDKGVR--LITNVET--KALKNEGDLTTVETSQgnftGDAILLAT 252
Cdd:PRK09754 162 SATQRRCKVTVIELAATVMGRNAPPPVQrYLLQRHQQAGVRilLNNAIEHvvDGEKVELTLQSGETLQ----ADVVIYGI 237
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515743447 253 GRVPNTDLAlnnTDIELGTHGEIKVNNHLQTSVSHIYAAGDV 294
Cdd:PRK09754 238 GISANDQLA---REANLDTANGIVIDEACRTCDPAIFAGGDV 276
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
89-428 4.26e-14

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 73.66  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  89 DENITLLNFKAQFKSNTE---VELIDENGKLVQTLTADKILINTGAKSNIPNIEG--IDSAQNVYDSKGLLNI--SYQPK 161
Cdd:PRK13512  70 RKQITVKTYHEVIAINDErqtVTVLNRKTNEQFEESYDKLILSPGASANSLGFESdiTFTLRNLEDTDAIDQFikANQVD 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 162 ELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALkNEGDLTTVETSQG 241
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAI-NGNEVTFKSGKVE 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 242 NFtgDAILLATGRVPNTDLaLNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDVkggLQFTYISLD-------------DF 308
Cdd:PRK13512 229 HY--DMIIEGVGTHPNSKF-IESSNIKLDDKGFIPVNDKFETNVPNIYAIGDI---ITSHYRHVDlpasvplawgahrAA 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 309 RILKSELFGDRSRHTenRGIIPYTV--FIDPPLSRVGITASEAQQLNYNYVENTlfintiPKHKIN----NDGRGLfKVV 382
Cdd:PRK13512 303 SIVAEQIAGNDTIEF--KGFLGNNIvkFFDYTFASVGVKPNELKQFDYKMVEVT------QGAHANyypgNSPLHL-RVY 373
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515743447 383 INKDNNEILGATLYGK-GSEEIINLIKLA------IDQHIPYQVLRDNIYTHP 428
Cdd:PRK13512 374 YDTSNRKILRAAAVGKeGADKRIDVLSMAmmnqltVDELTEFEVAYAPPYSHP 426
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
118-293 8.53e-13

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 70.53  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 118 QTLTADKILINTGAKSNIPNIEGIDSAQN-VY----DSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYN 192
Cdd:PRK14989  98 RTVFYDKLIMATGSYPWIPPIKGSETQDCfVYrtieDLNAIEACARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 193 KQFMARE-DQEIVTHMINDFKDKGVRLITNVETKALKNEG----------DLTTVETsqgnftgDAILLATGRVPNTDLA 261
Cdd:PRK14989 178 PMLMAEQlDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGvearktmrfaDGSELEV-------DFIVFSTGIRPQDKLA 250
                        170       180       190
                 ....*....|....*....|....*....|..
gi 515743447 262 lNNTDIELGTHGEIKVNNHLQTSVSHIYAAGD 293
Cdd:PRK14989 251 -TQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
106-294 6.42e-12

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 66.69  E-value: 6.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 106 EVELIDENGKLV-----QTLTADKILINTGAKSNIPNIEG----------IDSAQNVYD----------SKGLLNIsyqp 160
Cdd:COG1252   77 EVTGIDPEARTVtladgRTLSYDYLVIATGSVTNFFGIPGlaehalplktLEDALALRErllaaferaeRRRLLTI---- 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 161 kelVIIGGGY----IALEFASMFQSFG---------TNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKAL 227
Cdd:COG1252  153 ---VVVGGGPtgveLAGELAELLRKLLrypgidpdkVRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEV 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515743447 228 KNEGdlttVETSQGN-FTGDAILLATGRVPNTdlALNNTDIELGTHGEIKVNNHLQT-SVSHIYAAGDV 294
Cdd:COG1252  230 DADG----VTLEDGEeIPADTVIWAAGVKAPP--LLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDC 292
PRK13984 PRK13984
putative oxidoreductase; Provisional
8-296 1.24e-11

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 66.71  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   8 VIGFGKAGKTLAKYASSQGQQVALIEqfTESYGGTCINHGcIPSKVLVNDgikhvdfstAFSRKKEVVKALNQKNYLNLE 87
Cdd:PRK13984 288 IVGSGPAGLSAAYFLATMGYEVTVYE--SLSKPGGVMRYG-IPSYRLPDE---------ALDKDIAFIEALGVKIHLNTR 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  88 NDENITLLNFKAQFksntevelidengklvqtltaDKILINTG-AKSNIPNIEGIDSaQNVYDSKGLLNI---------- 156
Cdd:PRK13984 356 VGKDIPLEELREKH---------------------DAVFLSTGfTLGRSTRIPGTDH-PDVIQALPLLREirdylrgegp 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 157 -SYQPKELVIIGGGYIALEFA-SM----FQSFGT-NVTV--LEYNKQFMAREDQEIVTH----------------MINDF 211
Cdd:PRK13984 414 kPKIPRSLVVIGGGNVAMDIArSMarlqKMEYGEvNVKVtsLERTFEEMPADMEEIEEGleegvviypgwgpmevVIEND 493
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 212 KDKGVRLITNVETkaLKNEGDLTTV--ETSQGNFTGDAILLATGRVPNTDLALNNTDIELG-THGEIKVNNHLQTSVSHI 288
Cdd:PRK13984 494 KVKGVKFKKCVEV--FDEEGRFNPKfdESDQIIVEADMVVEAIGQAPDYSYLPEELKSKLEfVRGRILTNEYGQTSIPWL 571

                 ....*....
gi 515743447 289 YAAGD-VKG 296
Cdd:PRK13984 572 FAGGDiVHG 580
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
123-294 3.30e-11

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 64.24  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 123 DKILINTGA-KSNIPNIEGIDsAQNVYDSKGLL------NISYQPKE---------LVIIGGGYIALEFASMFQSFGTNV 186
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGED-LPGVYSALEYLfriraaKLGYLPWEkvppvegkkVVVVGAGLTAVDAALEAVLLGAEK 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 187 TVLEYNKqfmAREDQEIVTHMINDFKDKGVRLITNVETKALKNEGDLTTVE-----TSQGNFTG---------------- 245
Cdd:PRK12770 199 VYLAYRR---TINEAPAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVElakmrLGEPDESGrprpvpipgsefvlea 275
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 515743447 246 DAILLATGRVPNTDLALNNTDIELGTHGEIKVNNHLQTSVSHIYAAGDV 294
Cdd:PRK12770 276 DTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDV 324
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
101-297 1.45e-10

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: 62.84  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 101 FKSNTEVelidenGKlvqTLTADK-------ILINTGA-KSNIPNIEGIDsAQNVYD----------SKGLLNISYQPKE 162
Cdd:COG0493  188 FRTNVEV------GK---DITLDElleefdaVFLATGAgKPRDLGIPGED-LKGVHSamdfltavnlGEAPDTILAVGKR 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 163 LVIIGGGYIALEFAsmfqsfGT-------NVTVLEynkqfmaREDQEivtHM------INDFKDKGVRLITNVETKALkn 229
Cdd:COG0493  258 VVVIGGGNTAMDCA------RTalrlgaeSVTIVY-------RRTRE---EMpaskeeVEEALEEGVEFLFLVAPVEI-- 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 230 EGD-------LTTVETSQGNF-----------TG-------DAILLATGRVPNTDLALNNTDIELGTHGEIKVN-NHLQT 283
Cdd:COG0493  320 IGDengrvtgLECVRMELGEPdesgrrrpvpiEGseftlpaDLVILAIGQTPDPSGLEEELGLELDKRGTIVVDeETYQT 399
                        250
                 ....*....|....
gi 515743447 284 SVSHIYAAGDVKGG 297
Cdd:COG0493  400 SLPGVFAGGDAVRG 413
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
4-294 2.75e-10

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 62.10  E-value: 2.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447   4 YNLIVIGFGKAGKTLAKYASSQGQQVALIeqfTESYGGTcinhgcipskvlVND--GIKHVdFSTAFSRKKEVVKALNQ- 80
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIV---AERFGGQ------------VLDtmGIENF-ISVPETEGPKLAAALEEh 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447  81 -KNY----LNLENDENITllnfkaQFKSNTEVELidENGklvQTLTADKILINTGAKSNIPNIEGidsaQNVYDSKGlln 155
Cdd:PRK15317 276 vKEYdvdiMNLQRASKLE------PAAGLIEVEL--ANG---AVLKAKTVILATGARWRNMNVPG----EDEYRNKG--- 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 156 ISYQP---------KELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMAreD---QEIVTHMINdfkdkgVRLITNVE 223
Cdd:PRK15317 338 VAYCPhcdgplfkgKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKA--DqvlQDKLRSLPN------VTIITNAQ 409
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515743447 224 TKALKNEGDLTTVETSQGNFTGDAILLAT-------GRVPNTDLaLNNTdIELGTHGEIKVNNHLQTSVSHIYAAGDV 294
Cdd:PRK15317 410 TTEVTGDGDKVTGLTYKDRTTGEEHHLELegvfvqiGLVPNTEW-LKGT-VELNRRGEIIVDARGATSVPGVFAAGDC 485
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
100-297 1.37e-08

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 56.73  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 100 QFKSNTEV-------ELIDENgklvqtltaDKILINTGA-KSNIPNIEGIDsAQNVYD----------SKGLLNISyQPK 161
Cdd:PRK11749 206 EIRTNTEVgrditldELRAGY---------DAVFIGTGAgLPRFLGIPGEN-LGGVYSavdfltrvnqAVADYDLP-VGK 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 162 ELVIIGGGYIALEFASMFQSFG-TNVTVLeYnkqfmaREDQEivtHM------INDFKDKGVRLITNVETKALK------ 228
Cdd:PRK11749 275 RVVVIGGGNTAMDAARTAKRLGaESVTIV-Y------RRGRE---EMpaseeeVEHAKEEGVEFEWLAAPVEILgdegrv 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 229 ----------NEGDLT-----TVETSQGNFTGDAILLATGRVPNTDLALNNTDIELGTHGEIKVN-NHLQTSVSHIYAAG 292
Cdd:PRK11749 345 tgvefvrmelGEPDASgrrrvPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADdETGRTSLPGVFAGG 424

                 ....*
gi 515743447 293 DVKGG 297
Cdd:PRK11749 425 DIVTG 429
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
119-293 1.01e-04

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 44.37  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 119 TLTADKILINTGAKSNIPNIEGIDS----------AQNV-------YDSKGLLNISYQPKE----LVIIGGGYIALEFAS 177
Cdd:PTZ00318 111 SVPYDKLVVAHGARPNTFNIPGVEErafflkevnhARGIrkrivqcIERASLPTTSVEERKrllhFVVVGGGPTGVEFAA 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 178 MFQSF--------------GTNVTVLEYNKQFMAREDQEIVTHMINDFKDKGVRLITNVETKALKNEgdltTVETSQGNF 243
Cdd:PTZ00318 191 ELADFfrddvrnlnpelveECKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDK----EVVLKDGEV 266
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515743447 244 --TGdAILLATGRVPNTdlALNNTDIELGTHGEIKVNNHLQTS-VSHIYAAGD 293
Cdd:PTZ00318 267 ipTG-LVVWSTGVGPGP--LTKQLKVDKTSRGRISVDDHLRVKpIPNVFALGD 316
gltD PRK12810
glutamate synthase subunit beta; Reviewed
100-293 2.54e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 43.23  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 100 QFKSNTEVelidenGKLV--QTLTA--DKILINTGA-KSNIPNIEG-------------IDSAQNVYDSKGLLNISYQPK 161
Cdd:PRK12810 209 EFRTNVEV------GKDItaEELLAeyDAVFLGTGAyKPRDLGIPGrdldgvhfamdflIQNTRRVLGDETEPFISAKGK 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 162 ELVIIGGGYIALEfasmfqSFGT-------NVTVLEYNKQFMAREDQEIVTHMINDF------KDKGVRLITNVETKALK 228
Cdd:PRK12810 283 HVVVIGGGDTGMD------CVGTairqgakSVTQRDIMPMPPSRRNKNNPWPYWPMKlevsnaHEEGVEREFNVQTKEFE 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 229 NE-GDLTTVETSQ-----GNFT----------GDAILLATGRVPNTDLALNNTDIELGTHGEIKVN-NHLQTSVSHIYAA 291
Cdd:PRK12810 357 GEnGKVTGVKVVRtelgeGDFEpvegsefvlpADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAPdNAYQTSNPKVFAA 436

                 ..
gi 515743447 292 GD 293
Cdd:PRK12810 437 GD 438
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
204-253 2.00e-03

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 40.27  E-value: 2.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515743447 204 VTHMINDFKDKGVRLITNVETKALKNEGD-LTTVETSQGNFTGDAILLATG 253
Cdd:COG0665  154 VRALARAARAAGVRIREGTPVTGLEREGGrVTGVRTERGTVRADAVVLAAG 204
PRK10262 PRK10262
thioredoxin reductase; Provisional
121-294 3.79e-03

thioredoxin reductase; Provisional


Pssm-ID: 182343 [Multi-domain]  Cd Length: 321  Bit Score: 39.27  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 121 TADKILINTGAKS---NIPNIEGIdSAQNVYDSKGLLNISYQPKELVIIGGGYIALEFASMFQSFGTNVTVLEYNKQFMA 197
Cdd:PRK10262 105 TCDALIIATGASArylGLPSEEAF-KGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRA 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515743447 198 R-----------EDQEIVTHMINDFKD-KGVRL-ITNVETKALKNEGDLTTVETSqgnftgdAILLATGRVPNTDLALNN 264
Cdd:PRK10262 184 EkilikrlmdkvENGNIILHTNRTLEEvTGDQMgVTGVRLRDTQNSDNIESLDVA-------GLFVAIGHSPNTAIFEGQ 256
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 515743447 265 TDIElgtHGEIKVN-----NHLQTSVSHIYAAGDV 294
Cdd:PRK10262 257 LELE---NGYIKVQsgihgNATQTSIPGVFAAGDV 288
solA PRK11259
N-methyl-L-tryptophan oxidase;
1-44 9.33e-03

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 37.89  E-value: 9.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 515743447   1 MTHYNLIVIGFGKAGKTLAKYASSQGQQVALIEQFT------ESYGGTCI 44
Cdd:PRK11259   1 TMRYDVIVIGLGSMGSAAGYYLARRGLRVLGLDRFMpphqqgSSHGDTRI 50
 
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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