|
Name |
Accession |
Description |
Interval |
E-value |
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
14-803 |
0e+00 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 933.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 14 LVVVGNGMAGIRTLEELLAKAPDRYDITVFGAEPHPNYNRIMLSPVLAGEKTFEQIVLNGRDWYEANGIKLLTGDRVEVI 93
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMFEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 94 DRANRTVTAISGLTVPYDKLLIATGSTPLIIQVPGSTLPGVVGFRDLADVDTMLEAAARGGRAVVIGGGLLGLEAANGLK 173
Cdd:TIGR02374 81 DTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 174 VKGMDVTVLHLMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQELPADLVVMAVGIRPNM 253
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 254 ALGKAAGLACGRGIQVDDAMTTSDPAILSVGECVEHRGQTYGLVAPLFEMAKVAAARLAGSTEAAYTGSVTSTKLKVTGV 333
Cdd:TIGR02374 241 ELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECEEYEGSDLSAKLKLLGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 334 DVFSAGDFTGGKDCEDIVFRDAARGVYKRVVVRENRILGAVLYGDTKDGGWYFQMLKDGTEVaPVRDTLIFGQGFGGEga 413
Cdd:TIGR02374 321 DVWSAGDAQETERTTSIKIYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVLKQADI-SEDPAIIKPQISGPE-- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 414 aNPKAAVAALPDSAEICGCNGVCKGTIVTAITEKGLSNLDEVRAHTKASASCGSCTGQVEQLLALTLGDGYAGEAKAkpM 493
Cdd:TIGR02374 398 -AGGPGVEAMPDSEQICSCNTVTKGAIIDAIHTGSCTTVEELKACTKAGTSCGGCKPLVEQLLRAELNSQYTASTPA--L 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 494 CKCTDRTHDEVRRAITALELKSIPDVMQRLEWRTPDGCHHCRPALNYYLLCEWPGEYKDDSRSRYINERVHANIQKDGTY 573
Cdd:TIGR02374 475 CECTDFSRDELFEEIQARGFTTFAEVMNQLGWKTKNGCSTCKPAVQYYLAMLYPGFILDEEATSLSNDHFLANIQKDGTY 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 574 SVVPRMWGGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVRKEDLPAVWADLNAAGMVsgHAYAKGLRTVKTCVGS 653
Cdd:TIGR02374 555 SVIPRMYGGRTNPEQLRTIANIAEAYSIPYVKITGGQRLDLFGAKKDDLPNIWKDLKMPGYE--HAYGKALRTVKTCVGS 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 654 EWCRFGTQDSTGLGVKLERMTWGTWTPHKVKLAVSGCPRNCAEATIKDLGVVCVDSGYELHVGGNGGMHVRACDLLVKVE 733
Cdd:TIGR02374 633 QWCRYGNQDSVQLAIQLERRYEGLRTPHKIKIGVSGCERECAEAAGKDVGVIATEKGWNLYVGGNGGTHPRHGDLLAVDE 712
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 734 TEAEVLEYTGAYMQLYREEARYLERTAPWLERVGLDYLKRRLVDDaEGRAALNARFLFSQSFSQdDPWAE 803
Cdd:TIGR02374 713 DEETLIGYIDRFLQYYRETADYLERTAPWLERLGIDHVREVLFED-DLRAELEESMQRDLSLIK-CPWKE 780
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
13-781 |
0e+00 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 608.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 13 RLVVVGNGMAGIRTLEELLAKA-PDRYDITVFGAEPHPNYNRIMLSPVLAgEKTFEQIVLNGRDWYEANGIKLLTGDRVE 91
Cdd:PRK14989 5 RLAIIGNGMVGHRFIEDLLDKAdAANFDITVFCEEPRIAYDRVHLSSYFS-HHTAEELSLVREGFYEKHGIKVLVGERAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 92 VIDRANRTVTAISGLTVPYDKLLIATGSTPLIIQVPGSTLPGVVGFRDLADVDTMLEAAARGGRAVVIGGGLLGLEAANG 171
Cdd:PRK14989 84 TINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAAGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 172 LKVKGMDVTVLHLMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIV--GSERVSAVRLKNGQELPADLVVMAVGI 249
Cdd:PRK14989 164 LKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADGSELEVDFIVFSTGI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 250 RPNMALGKAAGLACGR--GIQVDDAMTTSDPAILSVGECVEHRGQTYGLVAPLFEMAKVAAARLAGStEAAYTGSVTSTK 327
Cdd:PRK14989 244 RPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGS-ENAFEGADLSAK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 328 LKVTGVDVFSAGDFTG-GKDCEDIVFRDAARGVYKRVVVREN--RILGAVLYGDTKDGGWYFQMLKDGTEVAPVRDTLIF 404
Cdd:PRK14989 323 LKLLGVDVGGIGDAHGrTPGARSYVYLDESKEIYKRLIVSEDnkTLLGAVLVGDTSDYGNLLQLVLNAIELPENPDSLIL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 405 GQGFGGEgaaNPKAAVAALPDSAEICGCNGVCKGTIVTAItEKGLSNLDEVRAHTKASASCGSCTGQVEQLLALTLGDgy 484
Cdd:PRK14989 403 PAHAGSG---KPSIGVDKLPDSAQICSCFDVTKGDLIAAI-NKGCHTVAALKAETKAGTGCGGCIPLVTQVLNAELAK-- 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 485 AGEAKAKPMCKCTDRTHDEVRRAITALELKSIPDVMQRleWRTPDGCHHCRPALNYYLLCEWpGEY---KDDSRSRYINE 561
Cdd:PRK14989 477 QGIEVNNNLCEHFAYSRQELFHLIRVEGIKTFEELLAK--HGKGYGCEVCKPTVGSLLASCW-NEYilkPQHTPLQDTND 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 562 RVHANIQKDGTYSVVPRMWGGLTSAKELRAIADVVDKFAIPTvKVTGGQRIDLFGVRKEDLPAVWADLNAAGMVSGHAYA 641
Cdd:PRK14989 554 NFLANIQKDGTYSVIPRSAGGEITPEGLMAVGRIAREFNLYT-KITGSQRIGLFGAQKDDLPEIWRQLIEAGFETGHAYA 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 642 KGLRTVKTCVGSEWCRFGTQDSTGLGVKLERMTWGTWTPHKVKLAVSGCPRNCAEATIKDLGVVCVDSGYELHVGGNGGM 721
Cdd:PRK14989 633 KALRMAKTCVGSTWCRYGVGDSVGLGVELENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATEKGWNLYVCGNGGM 712
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388779335 722 HVRACDLLVKVETEAEVLEYTGAYMQLYREEARYLERTAPWLERV--GLDYLKRRLVDDAEG 781
Cdd:PRK14989 713 KPRHADLLAADLDRETLIKYLDRFMMFYIRTADKLQRTAVWLENLegGIDYLKAVIIDDKLG 774
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
11-397 |
0e+00 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 532.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 11 RERLVVVGNGMAGIRTLEELLAKAPDrYDITVFGAEPHPNYNRIMLSPVLAGEKTFEQIVLNGRDWYEANGIKLLTGDRV 90
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPD-GEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 91 EVIDRANRTVTAISGLTVPYDKLLIATGSTPLIIQVPGSTLPGVVGFRDLADVDTMLEAAARGGRAVVIGGGLLGLEAAN 170
Cdd:COG1251 80 TAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 171 GLKVKGMDVTVLHLMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQELPADLVVMAVGIR 250
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 251 PNMALGKAAGLACGRGIQVDDAMTTSDPAILSVGECVEHRGQTYG-----LVAPLFEMAKVAAARLAGsTEAAYTGSVTS 325
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAG-GPAAYEGSVPS 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388779335 326 TKLKVTGVDVFSAGDFTGGKdcEDIVFRDAARGVYKRVVVRENRILGAVLYGDTKDGGWYFQMLKDGTEVAP 397
Cdd:COG1251 319 TKLKVFGVDVASAGDAEGDE--EVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPP 388
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
39-325 |
1.02e-75 |
|
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: 248.96 E-value: 1.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 39 DITVFGAEPHPNYNRIMLSP-VLAGEKTFEQIVLNGRDWYEANGIKLLTGDRVEVIDRANRTVTAISGLTVPYDKLLIAT 117
Cdd:COG0446 7 EITVIEKGPHHSYQPCGLPYyVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYDKLVLAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 118 GSTPLIIQVPGSTLPGVVGFRDLADVDTMLEA--AARGGRAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMERqLDR 195
Cdd:COG0446 87 GARPRPPPIPGLDLPGVFTLRTLDDADALREAlkEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV-LDP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 196 SAGALLRHELERRGITVLTGADTAEIVGSERVsAVRLKNGQELPADLVVMAVGIRPNMALGKAAGLACGR--GIQVDDAM 273
Cdd:COG0446 166 EMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgWIKVDETL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1388779335 274 TTSDPAILSVGECVEHRGQTYG------LVAPLFEMAKVAAARLAGsTEAAYTGSVTS 325
Cdd:COG0446 245 QTSDPDVYAAGDCAEVPHPVTGktvyipLASAANKQGRVAAENILG-GPAPFPGLGTF 301
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
13-286 |
9.13e-56 |
|
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: 194.07 E-value: 9.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 13 RLVVVGNGMAGIRTLEELLAKapdRYDITVFGAEPHPNYNRIMLSPVLAGEKTFEQIVLNGRDWYE---------ANGIK 83
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQL---GGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 84 LLTGDRVEVIDRANRTVTAI-----SGLTVPYDKLLIATGSTPLIIQVPGSTLPGVVGFRDLADVDtMLEAAARGGRAVV 158
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAE-ALRLKLLPKRVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 159 IGGGLLGLEAANGLKVKGMDVTVLHLMDTLMeRQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQEL 238
Cdd:pfam07992 158 VGGGYIGVELAAALAKLGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1388779335 239 PADLVVMAVGIRPNMALGKAAGLACGR--GIQVDDAMTTSDPAILSVGEC 286
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDC 286
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
11-321 |
8.70e-41 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 154.52 E-value: 8.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 11 RERLVVVGNGMAGIRTLEELLAKAPDRYDITVFGAEPH----PnynriMLSPVLAGEKTFEQIVLNGRDWYEANGIKLLT 86
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYhlfqP-----LLPEVAAGTLSPDDIAIPLRELLRRAGVRFIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 87 GdRVEVIDRANRTVTAISGLTVPYDKLLIATGSTPLIIQVPGS--------TLPGVVGFRDlaDVDTMLEAAAR--GGRA 156
Cdd:COG1252 76 G-EVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLaehalplkTLEDALALRE--RLLAAFERAERrrLLTI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 157 VVIGGGLLGLEAA-------------NGLKVKGMDVTVLHLMDTLMERqLDRSAGALLRHELERRGITVLTGADTAEIVG 223
Cdd:COG1252 153 VVVGGGPTGVELAgelaellrkllryPGIDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEVDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 224 servSAVRLKNGQELPADLVVMAVGIRPNmALGKAAGLACGRG--IQVDDAM-TTSDPAILSVGECVEHRGQTYGLVAPL 300
Cdd:COG1252 232 ----DGVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLqVPGHPNVFAIGDCAAVPDPDGKPVPKT 306
|
330 340
....*....|....*....|....*....
gi 1388779335 301 ----FEMAKVAA----ARLAGSTEAAYTG 321
Cdd:COG1252 307 aqaaVQQAKVLAkniaALLRGKPLKPFRY 335
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
15-317 |
5.90e-40 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 151.61 E-value: 5.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 15 VVVGNGMAG---IRTLEELLAKAPdrydITVFGAEPHPNYNRIMLSPVLAGEKTFEQ-IVLNGRDWYEANGIKLLTGDRV 90
Cdd:PRK04965 6 VIIGSGFAArqlVKNIRKQDAHIP----ITLITADSGDEYNKPDLSHVFSQGQRADDlTRQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 91 EVIDRANRTVTAiSGLTVPYDKLLIATGSTPLIIQVPGSTLpgVVGFRDLADVDTMLEAAARGGRAVVIGGGLLGLEAAN 170
Cdd:PRK04965 82 TDIDAEAQVVKS-QGNQWQYDKLVLATGASAFVPPIPGREL--MLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 171 GLKVKGMDVTVLHLMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQELPADLVVMAVGIR 250
Cdd:PRK04965 159 DLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLR 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1388779335 251 PNMALGKAAGLACGRGIQVDDAMTTSDPAILSVGECVEHRGQTYGLVAPLFEMAKVAAARLAGSTEA 317
Cdd:PRK04965 239 PNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTP 305
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
13-339 |
5.19e-33 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 132.86 E-value: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 13 RLVVVGNGMAGI-------RTLEELLAKAPDRYDITVFGAEPHPNYNRIML-SPVLAGEKTFEQivlngrdwYEANGIKL 84
Cdd:PRK09564 2 KIIIIGGTAAGMsaaakakRLNKELEITVYEKTDIVSFGACGLPYFVGGFFdDPNTMIARTPEE--------FIKSGIDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 85 LTGDRVEVIDRANRTVTAI-----SGLTVPYDKLLIATGSTPLIIQVPGSTLPGVVGFRDLADVDTMLEAAARGG--RAV 157
Cdd:PRK09564 74 KTEHEVVKVDAKNKTITVKnlktgSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEikNIV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 158 VIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGqE 237
Cdd:PRK09564 154 IIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKG-E 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 238 LPADLVVMAVGIRPNMALGKAAGL--ACGRGIQVDDAMTTSDPAILSVGEC--VEHR---GQTYglvAPLF----EMAKV 306
Cdd:PRK09564 233 YEADVVIVATGVKPNTEFLEDTGLktLKNGAIIVDEYGETSIENIYAAGDCatIYNIvsnKNVY---VPLAttanKLGRM 309
|
330 340 350
....*....|....*....|....*....|...
gi 1388779335 307 AAARLAGsTEAAYTGSVTSTKLKVTGVDVFSAG 339
Cdd:PRK09564 310 VGENLAG-RHVSFKGTLGSACIKVLDLEAARTG 341
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
74-378 |
7.66e-30 |
|
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: 123.66 E-value: 7.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 74 RDWYEANGIKLLTGdRVEVIDraNRTVTAISGLTVPYDKLLIATGSTPLIIQVPGSTLPGVVgfrdlaDVDTMLEAAARG 153
Cdd:COG1249 98 EELLKKNGVDVIRG-RARFVD--PHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVL------TSDEALELEELP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 154 GRAVVIGGGLLGLEAA---NGLkvkGMDVTVLHLMDTLMeRQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAV 230
Cdd:COG1249 169 KSLVVIGGGYIGLEFAqifARL---GSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 231 RLKNG---QELPADLVVMAVGIRPNMA-LG-KAAGLACGR--GIQVDDAMTTSDPAILSVGECVEHRGQTYglVAplFEM 303
Cdd:COG1249 245 TLEDGggeEAVEADKVLVATGRRPNTDgLGlEAAGVELDErgGIKVDEYLRTSVPGIYAIGDVTGGPQLAH--VA--SAE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 304 AKVAAARLAGSTE----------AAYT----GSV--TSTKLKVTGVDV------FSAgdftggkdcediVFR----DAAR 357
Cdd:COG1249 321 GRVAAENILGKKPrpvdyraipsVVFTdpeiASVglTEEEAREAGIDVkvgkfpFAA------------NGRalalGETE 388
|
330 340
....*....|....*....|..
gi 1388779335 358 GVYKRVVVREN-RILGAVLYGD 378
Cdd:COG1249 389 GFVKLIADAETgRILGAHIVGP 410
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
641-773 |
4.91e-29 |
|
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the biosynthetic assimilation of sulphur and nitrogen, respectfully. They are also both important for the dissimilation of oxidized anions for energy transduction.
Pssm-ID: 426031 [Multi-domain] Cd Length: 153 Bit Score: 113.13 E-value: 4.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 641 AKGLRTVKTCVGSEWCRFGTQDSTGLGVKLERM----TWGTWTPHKVKLAVSGCPRNCAEATIKDLGVVCVDS-----GY 711
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEfepdYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKdggeiGF 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388779335 712 ELHVGGNGGMHVRACDLLVKVE--TEAEVLEYTGAYMQLYR----EEARYLERTAPWLERVGLDYLKR 773
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKVVPfvPEEDVLEVIEAILEVYRdhgdRENRKKERLKYLIERLGLEKFRE 148
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
14-290 |
1.05e-26 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 113.48 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 14 LVVVGNGMAGIRTLEELLAKAPDRyDITVFGAEPHPNYNRIMLSPVLAGEKTFEQIVLNGRDWYEANGIKLLTGDRVEVI 93
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTG-ELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 94 DRANRTVTAISGLTVPYDKLLIATGST----PLIIQVPGStlpgVVGFRDLADVDTMLEAAARGGRAVVIGGGLLGLEAA 169
Cdd:PRK09754 85 GRDTRELVLTNGESWHWDQLFIATGAAarplPLLDALGER----CFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 170 NGLKVKGMDVTVLHLMDTLMerqlDRSAGALLRHELERR----GITVLTGADTAEIVGSERVsAVRLKNGQELPADLVVM 245
Cdd:PRK09754 161 ASATQRRCKVTVIELAATVM----GRNAPPPVQRYLLQRhqqaGVRILLNNAIEHVVDGEKV-ELTLQSGETLQADVVIY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1388779335 246 AVGIRPNMALGKAAGLACGRGIQVDDAMTTSDPAILSVGECVEHR 290
Cdd:PRK09754 236 GIGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITR 280
|
|
| NirB_Fer2_BFD-like_1 |
cd19943 |
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
424-476 |
2.13e-26 |
|
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large and a small subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381076 [Multi-domain] Cd Length: 53 Bit Score: 102.31 E-value: 2.13e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1388779335 424 PDSAEICGCNGVCKGTIVTAITEKGLSNLDEVRAHTKASASCGSCTGQVEQLL 476
Cdd:cd19943 1 PDDAEVCGCNGVSKGAIVQAIQEKGLTTLDEVKACTKASTSCGGCTPLVEQLL 53
|
|
| NirB_Fer2_BFD-like_2 |
cd19944 |
second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
491-542 |
6.44e-26 |
|
second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large (NirB) and a small (NirD) subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. Some of the second [2Fe-2S]-binding domains, have one of the Cys residues replaced by a His residue, they may interact with non-Rieske NirD subunits. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381077 [Multi-domain] Cd Length: 52 Bit Score: 100.72 E-value: 6.44e-26
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1388779335 491 KPMCKCTDRTHDEVRRAITALELKSIPDVMQRLEWRTPDGCHHCRPALNYYL 542
Cdd:cd19944 1 KTLCSCTDLSHDEVREAIQEHGLTSFEEVMAALGWKTPDGCEKCRPALNYYL 52
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
547-775 |
3.89e-22 |
|
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 100.96 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 547 PGEYKDDSRSRYINerVHANIQkDGTYSV---VPrmwGGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVRKEDLP 623
Cdd:COG0155 283 PRPLPAFARWDHLG--VHEQKQ-DGLYYVglsVE---NGRITDEQLRALADLAERYGSGEIRLTPNQNLILADVPEEDLP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 624 AVWADLNAAGMvsgHAYAKGLRT-VKTCVGSEWCRFGTQDSTGLGV----KLERMTWGTWTPHKVKLAVSGCPRNCAEAT 698
Cdd:COG0155 357 ALEAALRALGL---ATPPSGLRRdSIACPGLPTCKLAIAESKRLAPaladRLEEDLDGLHDDEPIRIRISGCPNSCGRHY 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 699 IKDLGVVCVD-----SGYELHVGGNGGMHVRACDLLVKVETEAEVLEYTGAYMQLYREEARYLERTAPWLERVGLDYLKR 773
Cdd:COG0155 434 IADIGLVGKAkkgvvEAYQLYLGGGLGGDARLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVGIEPLKE 513
|
..
gi 1388779335 774 RL 775
Cdd:COG0155 514 LL 515
|
|
| Rubredoxin_C |
pfam18267 |
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin ... |
325-393 |
1.75e-21 |
|
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin oxidoreductase present in Clostridium acetobutylicum. The majority of obligatory anaerobes detoxify micro-aerobic environments by consuming O2 via H2O-forming NADH oxidase. This enzyme offers an alternate reaction pathway for scavenging of O2 and reactive oxygen species, wherein the reducing equivalent is obtained from NADH.
Pssm-ID: 408082 [Multi-domain] Cd Length: 70 Bit Score: 88.77 E-value: 1.75e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388779335 325 STKLKVTGVDVFSAGDFTGGKDCEDIVFRDAARGVYKRVVVRENRILGAVLYGDTKDGGWYFQMLKDGT 393
Cdd:pfam18267 2 STILKVFGIDLFSMGDIEENDNAEEIVKVDASNGIYKKLFIRDGKLVGAILIGDTSESPKLKKAIEKKI 70
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
155-235 |
4.01e-19 |
|
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: 82.25 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 155 RAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMeRQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKN 234
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 1388779335 235 G 235
Cdd:pfam00070 80 G 80
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
78-289 |
4.24e-19 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 88.64 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 78 EANGIKLLTgDRVEVIDRANR--TVTAISGLTVPYDKLLIATGSTPLIIQVPGSTLP---GVVGFrdlADVDTMLeaaAR 152
Cdd:COG0492 68 ERFGAEILL-EEVTSVDKDDGpfRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSYC---ATCDGFF---FR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 153 GGRAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLmerqldRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRL 232
Cdd:COG0492 141 GKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDEL------RASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTL 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1388779335 233 KNG-----QELPADLVVMAVGIRPNMALGKAAGLACGRG--IQVDDAMTTSDPAILSVGECVEH 289
Cdd:COG0492 215 KNVktgeeKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVRDY 278
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
83-313 |
4.19e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 84.81 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 83 KLLTGDRVEVI-DRANRTVTAisgltvpyDKLLIATGSTPLiiqvpgsTLPGV-VGFRDLADVDTMLEAAARGGRAVVIG 160
Cdd:PRK06416 115 KLVDPNTVRVMtEDGEQTYTA--------KNIILATGSRPR-------ELPGIeIDGRVIWTSDEALNLDEVPKSLVVIG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 161 GGLLGLEAANGLKVKGMDVTVLHLMDTLM--ErqlDRSAGALLRHELERRGITVLTGAdTAEIV--GSERVSAVRLKNG- 235
Cdd:PRK06416 180 GGYIGVEFASAYASLGAEVTIVEALPRILpgE---DKEISKLAERALKKRGIKIKTGA-KAKKVeqTDDGVTVTLEDGGk 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 236 -QELPADLVVMAVGIRPNMA-LG-KAAGLACGRG-IQVDDAMTTSDPAILSVGECVE-----HRGqtyglvaplFEMAKV 306
Cdd:PRK06416 256 eETLEADYVLVAVGRRPNTEnLGlEELGVKTDRGfIEVDEQLRTNVPNIYAIGDIVGgpmlaHKA---------SAEGII 326
|
....*..
gi 1388779335 307 AAARLAG 313
Cdd:PRK06416 327 AAEAIAG 333
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
13-329 |
6.18e-17 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 84.06 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 13 RLVVVGnGMAGIRTLEELLAKAPDRYDITVFGAEPHPNYNRIMLsPVLAGEktfeqiVLNGRD---------WYEANGIK 83
Cdd:PRK13512 3 KIIVVG-AVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCAL-PYYIGE------VVEDRKyalaytpekFYDRKQIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 84 LLTGDRVEVIDRANRTVTAIS-----GLTVPYDKLLIATGSTPliiQVPGSTLPGVVGFRDLADVDTMLE--AAARGGRA 156
Cdd:PRK13512 75 VKTYHEVIAINDERQTVTVLNrktneQFEESYDKLILSPGASA---NSLGFESDITFTLRNLEDTDAIDQfiKANQVDKA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 157 VVIGGGLLGLEAANGLKVKGMDVTVLHlMDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSErvsaVRLKNGQ 236
Cdd:PRK13512 152 LVVGAGYISLEVLENLYERGLHPTLIH-RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNE----VTFKSGK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 237 ELPADLVVMAVGIRPNMALGKAAGLACGRG--IQVDDAMTTSDPAILSVGECVEHRGQTYGLVA--PL----FEMAKVAA 308
Cdd:PRK13512 227 VEHYDMIIEGVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITSHYRHVDLPAsvPLawgaHRAASIVA 306
|
330 340
....*....|....*....|.
gi 1388779335 309 ARLAGSTEAAYTGSVTSTKLK 329
Cdd:PRK13512 307 EQIAGNDTIEFKGFLGNNIVK 327
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
82-286 |
8.70e-17 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 83.67 E-value: 8.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 82 IKLLTGDRVEVID-RA----NRTVtAISGLTVPYDKLLIATGSTPLIIQVPGSTLpGVvgfrdlaDVDTMLEAAARGGRA 156
Cdd:PRK06116 100 RNGLENNGVDLIEgFArfvdAHTV-EVNGERYTADHILIATGGRPSIPDIPGAEY-GI-------TSDGFFALEELPKRV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 157 VVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMeRQLDRSAGALLRHELERRGITVLTGADTAEIV-GSERVSAVRLKNG 235
Cdd:PRK06116 171 AVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPL-RGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEkNADGSLTLTLEDG 249
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1388779335 236 QELPADLVVMAVGIRPNM-ALG-KAAGLAC-GRG-IQVDDAMTTSDPAILSVGEC 286
Cdd:PRK06116 250 ETLTVDCLIWAIGREPNTdGLGlENAGVKLnEKGyIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
98-286 |
1.00e-16 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 83.71 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 98 RTVTaISGLTVPYDKLLIATGSTPLIIQVPGstlpgvvgfrdLADV-----DTMLEAAARGGRAVVIGGGLLGLEAANGL 172
Cdd:PRK06370 123 NTVR-VGGETLRAKRIFINTGARAAIPPIPG-----------LDEVgyltnETIFSLDELPEHLVIIGGGYIGLEFAQMF 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 173 KVKGMDVTVLHLMDTLMERQlDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLK---NGQELPADLVVMAVGI 249
Cdd:PRK06370 191 RRFGSEVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDcngGAPEITGSHILVAVGR 269
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1388779335 250 RPNM-ALG-KAAGLACGR--GIQVDDAMTTSDPAILSVGEC 286
Cdd:PRK06370 270 VPNTdDLGlEAAGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
568-632 |
1.06e-16 |
|
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key to both biosynthetic assimilation of sulfur and nitrogen and dissimilation of oxidized anions for energy transduction. Two copies of this repeat are found in Nitrite and Sulfite reductases and form a single structural domain.
Pssm-ID: 377044 [Multi-domain] Cd Length: 67 Bit Score: 74.87 E-value: 1.06e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388779335 568 QKDGTYSVVPRMWGGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVRKEDLPAVWADLNAA 632
Cdd:pfam03460 3 QKDGDYMVRVRVPGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELLEELAEA 67
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
78-319 |
8.60e-16 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 80.61 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 78 EANGIKLLTGdRVEVIDraNRTVTaISGLTVPYDKLLIATGSTplIIQVPGSTLPGVVgfrDLADVDTMLEAAARGGRAV 157
Cdd:PRK06292 103 KKPKIDKIKG-TARFVD--PNTVE-VNGERIEAKNIVIATGSR--VPPIPGVWLILGD---RLLTSDDAFELDKLPKSLA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 158 VIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMeRQLDRSAGALLRHELERRgITVLTGADTAEI-VGSERVSAVRLKNG- 235
Cdd:PRK06292 174 VIGGGVIGLELGQALSRLGVKVTVFERGDRIL-PLEDPEVSKQAQKILSKE-FKIKLGAKVTSVeKSGDEKVEELEKGGk 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 236 -QELPADLVVMAVGIRPNM-ALG-KAAGLACG-RG-IQVDDAMTTSDPAILSVGECVehrGQTyglvaPLFEMAK---VA 307
Cdd:PRK06292 252 tETIEADYVLVATGRRPNTdGLGlENTGIELDeRGrPVVDEHTQTSVPGIYAAGDVN---GKP-----PLLHEAAdegRI 323
|
250
....*....|..
gi 1388779335 308 AARLAGSTEAAY 319
Cdd:PRK06292 324 AAENAAGDVAGG 335
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
581-784 |
1.30e-15 |
|
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; Sulfite reductase, beta subunit (hemoprotein) is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439925 [Multi-domain] Cd Length: 519 Bit Score: 80.55 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 581 GGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVRKEDLPAVWADLNAAGMvsgHAYAKG---LRTVKTCVGSEWCR 657
Cdd:COG0155 63 GGVLTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELAEVGL---TTIGACgdvVRNVTASPLAGVDP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 658 FGTQDSTGLGVKLERMTWG----TWTPHKVKLAVSGCPRNCAEATIKDLGVVCVDS-----GYELHVGGNGGMHVRACDL 728
Cdd:COG0155 140 DELFDVRPYAEAISQHLLGhpeyTYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKedglvGFNVLVGGGLGRTPRLADV 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388779335 729 LVKVETEAEVLEYTGAYMQLYREE--------AR--YLertapwLERVGLD---------YLKRRLVDDAEGRAA 784
Cdd:COG0155 220 LGEFVPPEDLLDVAEAVVRVFRDYgdrdnrkkARlkYL------VDDLGVEkfreeveeeYLGFPLEPAPRPLPA 288
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
87-313 |
3.53e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 78.81 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 87 GDRVEVIDRANRTVTAisgltvpyDKLLIATGSTPliiqvpgSTLPGV-VGFRDLADVDTMLEAAARGGRAVVIGGGLLG 165
Cdd:PRK06327 131 GYEIKVTGEDETVITA--------KHVIIATGSEP-------RHLPGVpFDNKIILDNTGALNFTEVPKKLAVIGAGVIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 166 LEAANGLKVKGMDVTVLHLMDTLMERQLDRSAGALLRhELERRGITVLTGADTAEI-VGSERVS-AVRLKNG--QELPAD 241
Cdd:PRK06327 196 LELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAK-AFTKQGLDIHLGVKIGEIkTGGKGVSvAYTDADGeaQTLEVD 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1388779335 242 LVVMAVGIRPNMA-LG-KAAGLACG-RG-IQVDDAMTTSDPAILSVGECVehRGQTYGLVAplFEMAKVAAARLAG 313
Cdd:PRK06327 275 KLIVSIGRVPNTDgLGlEAVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVV--RGPMLAHKA--EEEGVAVAERIAG 346
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
60-285 |
1.52e-12 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 70.61 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 60 LAGEKTFEQIVLNG--RDWYEANGIKLLTGdRVEVIDRANRTVTAISGLTVPY--DKLLIATGSTPLIIQVPGSTLPGVv 135
Cdd:PLN02507 115 LLQKKTDEILRLNGiyKRLLANAGVKLYEG-EGKIVGPNEVEVTQLDGTKLRYtaKHILIATGSRAQRPNIPGKELAIT- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 136 gfrdlADVDTMLEAAARggRAVVIGGGLLGLEAANglKVKGMDVTV-LHLMDTLMERQLDRSAGALLRHELERRGITVLT 214
Cdd:PLN02507 193 -----SDEALSLEELPK--RAVVLGGGYIAVEFAS--IWRGMGATVdLFFRKELPLRGFDDEMRAVVARNLEGRGINLHP 263
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388779335 215 GADTAEIVGSERVSAVRLKNGQELPADLVVMAVGIRPNMA-LG-KAAGLACGR--GIQVDDAMTTSDPAILSVGE 285
Cdd:PLN02507 264 RTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKrLNlEAVGVELDKagAVKVDEYSRTNIPSIWAIGD 338
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
108-317 |
1.59e-12 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 70.95 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 108 VPYDKLLIATGSTPLIIQVPGstlpgvvgfrdLADVD--TMLEAAARGG---RAVVIGGGLLGLEAANGLKVKGMDVTVL 182
Cdd:PRK13748 231 VAFDRCLIATGASPAVPPIPG-----------LKETPywTSTEALVSDTipeRLAVIGSSVVALELAQAFARLGSKVTIL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 183 hLMDTLMERQlDRSAGALLRHELERRGITVLTGADtaeivgserVSAVRLKNGQ--------ELPADLVVMAVGIRPN-- 252
Cdd:PRK13748 300 -ARSTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQ---------ASQVAHVDGEfvlttghgELRADKLLVATGRAPNtr 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1388779335 253 -MALgKAAGLAC-GRG-IQVDDAMTTSDPAILSVGECVEhrgqtyglvAPLFemAKVAAArlAGSTEA 317
Cdd:PRK13748 369 sLAL-DAAGVTVnAQGaIVIDQGMRTSVPHIYAAGDCTD---------QPQF--VYVAAA--AGTRAA 422
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
74-284 |
2.97e-12 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 69.80 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 74 RDWYEANGIKLLTGD---------RVEVIDRANRTVTAisgltvpyDKLLIATGSTPLiiqvpgstLPGVVGFRD--LAD 142
Cdd:PRK05249 101 RGQYERNRVDLIQGRarfvdphtvEVECPDGEVETLTA--------DKIVIATGSRPY--------RPPDVDFDHprIYD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 143 VDTMLEAAARGGRAVVIGGGLLGLEAA---NGLKVKgmdVTVLHLMDTLMERqLDRSAGALLRHELERRGITVLTGADTA 219
Cdd:PRK05249 165 SDSILSLDHLPRSLIIYGAGVIGCEYAsifAALGVK---VTLINTRDRLLSF-LDDEISDALSYHLRDSGVTIRHNEEVE 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388779335 220 EIVGSERVSAVRLKNGQELPADLVVMAVGIRPNM-ALG-KAAGL-ACGRG-IQVDDAMTTSDPAILSVG 284
Cdd:PRK05249 241 KVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTdGLNlENAGLeADSRGqLKVNENYQTAVPHIYAVG 309
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
429-477 |
7.45e-12 |
|
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).
Pssm-ID: 461261 [Multi-domain] Cd Length: 50 Bit Score: 60.62 E-value: 7.45e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1388779335 429 ICGCNGVCKGTIVTAItEKGLSNLDEVRAHTKASASCGSCTGQVEQLLA 477
Cdd:pfam04324 2 VCRCFGVTDGEIRDAI-REGLTTVEEVKRRTKAGTGCGSCRPAIEEILA 49
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
16-292 |
9.82e-12 |
|
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: 67.85 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 16 VVGNGMAGIrTLEELLAKAPdrYDITVFGAEPH---------PNYnRImlspvlagEKTfeqiVLNGR-DWYEANGIKLL 85
Cdd:COG0493 126 VVGSGPAGL-AAAYQLARAG--HEVTVFEALDKpggllrygiPEF-RL--------PKD----VLDREiELIEALGVEFR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 86 TGdrVEVidraNRTVTaISGLTVPYDKLLIATGST-PLIIQVPGSTLPGVVGFRD-LADVDTMLEAA---ARGGRAVVIG 160
Cdd:COG0493 190 TN--VEV----GKDIT-LDELLEEFDAVFLATGAGkPRDLGIPGEDLKGVHSAMDfLTAVNLGEAPDtilAVGKRVVVIG 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 161 GGLLGLEA---ANGLKVKgmDVTVLHLMDtlMERQldrSAGALLRHELERRGITVLTGADTAEIVGSE--RVSAVRL--- 232
Cdd:COG0493 263 GGNTAMDCartALRLGAE--SVTIVYRRT--REEM---PASKEEVEEALEEGVEFLFLVAPVEIIGDEngRVTGLECvrm 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 233 ------KNG-----------QELPADLVVMAVGIRPNMA-LGKAAGLAC-GRG-IQVD-DAMTTSDPAILSVGECVehRG 291
Cdd:COG0493 336 elgepdESGrrrpvpiegseFTLPADLVILAIGQTPDPSgLEEELGLELdKRGtIVVDeETYQTSLPGVFAGGDAV--RG 413
|
.
gi 1388779335 292 Q 292
Cdd:COG0493 414 P 414
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
16-292 |
4.32e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 65.97 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 16 VVGNGMAGIrTLEELLAKAPdrYDITVFGAEPHPN-YNR--ImlspvlAGEKTFEQIVLNGRDWYEANGIKLLTGDRVEv 92
Cdd:PRK11749 145 VIGAGPAGL-TAAHRLARKG--YDVTIFEARDKAGgLLRygI------PEFRLPKDIVDREVERLLKLGVEIRTNTEVG- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 93 idranRTVTaISGLTVPYDKLLIATG-STPLIIQVPGSTLPGVVGFRD-LADVDTMLEAA--ARGGRAVVIGGGLLGLEA 168
Cdd:PRK11749 215 -----RDIT-LDELRAGYDAVFIGTGaGLPRFLGIPGENLGGVYSAVDfLTRVNQAVADYdlPVGKRVVVIGGGNTAMDA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 169 ANGLKVKG-MDVTVLHlmdtlMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSER----VSAVRLKNGQ------- 236
Cdd:PRK11749 289 ARTAKRLGaESVTIVY-----RRGREEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGrvtgVEFVRMELGEpdasgrr 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1388779335 237 ---------ELPADLVVMAVGIRPN---MALGKAAGLACGRGIQVDDA-MTTSDPAILSVGECVehRGQ 292
Cdd:PRK11749 364 rvpiegsefTLPADLVIKAIGQTPNpliLSTTPGLELNRWGTIIADDEtGRTSLPGVFAGGDIV--TGA 430
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
110-287 |
5.50e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.93 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 110 YDKLLIATGS-TPLIIQVPGSTLPGV-------VGFR--DLADVDTMLEAAARGGRAVVIGGGLLGLEAANGLKVKGMDV 179
Cdd:PRK12770 119 YDAVLIATGTwKSRKLGIPGEDLPGVysaleylFRIRaaKLGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEAVLLGAEK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 180 TVLHLMDTLMERqldrSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQ--------------------ELP 239
Cdd:PRK12770 199 VYLAYRRTINEA----PAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVELAKMRlgepdesgrprpvpipgsefVLE 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1388779335 240 ADLVVMAVGIRPNMALGK-AAGLACGRG--IQVDDAMTTSDPAILSVGECV 287
Cdd:PRK12770 275 ADTVVFAIGEIPTPPFAKeCLGIELNRKgeIVVDEKHMTSREGVFAAGDVV 325
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
111-285 |
1.14e-09 |
|
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: 61.53 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 111 DKLLIATGSTPLIIQVPGSTLPGVvgfrdlADVDTMLEAAARggRAVVIGGGLLGLEAA---NGLKVKGMDVTVLHLMDT 187
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGIEHCIS------SNEAFYLDEPPR--RVLTVGGGFISVEFAgifNAYKPRGGKVTLCYRNNM 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 188 LMeRQLDRSAGALLRHELERRGITVLTGADTAEIV----GSERVSavrLKNGQELPADLVVMAVGIRP---NMALGKAA- 259
Cdd:TIGR01423 225 IL-RGFDSTLRKELTKQLRANGINIMTNENPAKVTlnadGSKHVT---FESGKTLDVDVVMMAIGRVPrtqTLQLDKVGv 300
|
170 180
....*....|....*....|....*.
gi 1388779335 260 GLACGRGIQVDDAMTTSDPAILSVGE 285
Cdd:TIGR01423 301 ELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
59-285 |
1.16e-09 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 61.30 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 59 VLAGEK--TFEQIV---------LNGRDWyeangiKLLTGDRVEVIDR-----ANRTVTAISG-----LTVpyDKLLIAT 117
Cdd:PRK07251 55 LVAAEKnlSFEQVMatkntvtsrLRGKNY------AMLAGSGVDLYDAeahfvSNKVIEVQAGdekieLTA--ETIVINT 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 118 GSTPLIIQVPG-STLPGVVgfrdlaDVDTMLEAAARGGRAVVIGGGLLGLEAAnGLKVK-GMDVTVLHLMDTLMERQlDR 195
Cdd:PRK07251 127 GAVSNVLPIPGlADSKHVY------DSTGIQSLETLPERLGIIGGGNIGLEFA-GLYNKlGSKVTVLDAASTILPRE-EP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 196 SAGALLRHELERRGITVLTGADTAEiVGSERVSAVRLKNGQELPADLVVMAVGIRPN---MALGKAAGLACGRG-IQVDD 271
Cdd:PRK07251 199 SVAALAKQYMEEDGITFLLNAHTTE-VKNDGDQVLVVTEDETYRFDALLYATGRKPNtepLGLENTDIELTERGaIKVDD 277
|
250
....*....|....
gi 1388779335 272 AMTTSDPAILSVGE 285
Cdd:PRK07251 278 YCQTSVPGVFAVGD 291
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
78-286 |
1.27e-09 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 61.41 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 78 EANGIKLLTGD-RVEVIDRANRTVTAISG----LTVPYDKLLIATGSTPLIIqvPGSTLPG--VVGFRDLADVDTMLEaa 150
Cdd:PRK07845 103 EREGVRVIAGRgRLIDPGLGPHRVKVTTAdggeETLDADVVLIATGASPRIL--PTAEPDGerILTWRQLYDLDELPE-- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 151 arggRAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMERQlDRSAGALLRHELERRGITVLTG--ADTAEIVGSERVs 228
Cdd:PRK07845 179 ----HLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGE-DADAAEVLEEVFARRGMTVLKRsrAESVERTGDGVV- 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388779335 229 aVRLKNGQELPADLVVMAVGIRPNMA-LG-KAAGLACGRG--IQVDDAMTTSDPAILSVGEC 286
Cdd:PRK07845 253 -VTLTDGRTVEGSHALMAVGSVPNTAgLGlEEAGVELTPSghITVDRVSRTSVPGIYAAGDC 313
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
492-542 |
1.41e-09 |
|
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).
Pssm-ID: 461261 [Multi-domain] Cd Length: 50 Bit Score: 54.07 E-value: 1.41e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1388779335 492 PMCKCTDRTHDEVRRAITAlELKSIPDVMQRleWRTPDGCHHCRPALNYYL 542
Cdd:pfam04324 1 IVCRCFGVTDGEIRDAIRE-GLTTVEEVKRR--TKAGTGCGSCRPAIEEIL 48
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
113-287 |
3.29e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 60.40 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 113 LLIATGSTPLiiqvpgstLPGVVGFRDLADVDTMLEAAaRGGRAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMeRQ 192
Cdd:PTZ00058 206 ILIAVGNKPI--------FPDVKGKEFTISSDDFFKIK-EAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL-RK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 193 LDRSAGALLRHELERRGITVLTGADTAEI--VGSERVSAVRLKNGQELPADLVVMAVGIRPNM-ALG-KAAGLACGRG-I 267
Cdd:PTZ00058 276 FDETIINELENDMKKNNINIITHANVEEIekVKEKNLTIYLSDGRKYEHFDYVIYCVGRSPNTeDLNlKALNIKTPKGyI 355
|
170 180
....*....|....*....|
gi 1388779335 268 QVDDAMTTSDPAILSVGECV 287
Cdd:PTZ00058 356 KVDDNQRTSVKHIYAVGDCC 375
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
89-285 |
4.33e-09 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 59.64 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 89 RVEVIDRAN-RTVTAISGLTVPYDKLLIATGSTPLIIQVPG-STLPGVVgfrdlaDVDTMLEAAARGGRAVVIGGGLLGL 166
Cdd:PRK08010 98 QAEFINNHSlRVHRPEGNLEIHGEKIFINTGAQTVVPPIPGiTTTPGVY------DSTGLLNLKELPGHLGILGGGYIGV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 167 EAANGLKVKGMDVTVLHLMDTLMERQlDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQELpADLVVMA 246
Cdd:PRK08010 172 EFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLA-VDALLIA 249
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1388779335 247 VGIRPNMA--LGKAAGLACGR--GIQVDDAMTTSDPAILSVGE 285
Cdd:PRK08010 250 SGRQPATAslHPENAGIAVNErgAIVVDKYLHTTADNIWAMGD 292
|
|
| nirA |
PRK09567 |
NirA family protein; |
563-717 |
5.03e-09 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 59.64 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 563 VHANIQkDGTYSVVPRMWGGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVRKEDLPAVWADLNAAGMvsgHAYAK 642
Cdd:PRK09567 366 VHPQKQ-PGLNWIGVVLPVGRLTTDQMRGLAKIAARYGDGEIRLTVWQNLLISGVPDADVAAVEAAIEALGL---TTEAS 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 643 GLRT-VKTCVGSEWCRFGTQDSTGLGVKLermtwGTWTPHKVKL------AVSGCPRNCAEATIKDLGV----VCVDS-- 709
Cdd:PRK09567 442 SIRAgLVACTGNAGCKFAAADTKGHALAI-----ADYCEPRVALdqpvniHLTGCHHSCAQHYIGDIGLigakVAVSEgd 516
|
170
....*....|.
gi 1388779335 710 ---GYELHVGG 717
Cdd:PRK09567 517 tveGYHIVVGG 527
|
|
| NifU_Fer2_BFD-like |
cd19947 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation ... |
425-477 |
7.98e-08 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation protein NifU and similar proteins; This family includes the BFD-like [2Fe-2S]-binding domain of Azotobacter vinelandii and Klebsiella pneumoniae nitrogen fixation protein NifU. NifU binds one Fe cation per subunit and one [2Fe-2S] cluster per subunit, and is involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381080 [Multi-domain] Cd Length: 55 Bit Score: 49.59 E-value: 7.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1388779335 425 DSAEICGCNGVCKGTIVTAITEKGLSNLDEVRAHTKASASCGSCTGQVEQLLA 477
Cdd:cd19947 1 EGAIVCKCFGVTEVMIERAIRENNLTTVEDVTNYTKAGGGCGSCHEKIEDILD 53
|
|
| Bfd |
COG2906 |
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism]; |
429-481 |
1.35e-07 |
|
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
Pssm-ID: 442150 [Multi-domain] Cd Length: 54 Bit Score: 48.66 E-value: 1.35e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1388779335 429 ICGCNGVCKGTIVTAItEKGLSNLDEVRAHTKASASCGSCTGQVEQLLALTLG 481
Cdd:COG2906 3 VCLCNGVTDRQIRAAI-AEGATSLEELRAALGAGTQCGSCVPEARELLAEALA 54
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
107-316 |
1.43e-07 |
|
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: 54.86 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 107 TVPYDKLLIATGSTPLIIQVPGSTLPGVVGfrdladvDTMLEAAARGGRAVVIGGGLLGLEAANGLKVKGMDVTVlhLMD 186
Cdd:TIGR01438 141 IYSAERFLIATGERPRYPGIPGAKELCITS-------DDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 187 TLMERQLDRSAGALLRHELERRGITVLTG--ADTAEIVGSE-RVSAVRLKNGQELPADLVVMAVGIRPNM------ALGK 257
Cdd:TIGR01438 212 SILLRGFDQDCANKVGEHMEEHGVKFKRQfvPIKVEQIEAKvLVEFTDSTNGIEEEYDTVLLAIGRDACTrklnleNVGV 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388779335 258 AAGLACGRgIQVDDAMTTSDPAILSVGECVEHRGQtyglVAPL-FEMAKVAAARL-AGSTE 316
Cdd:TIGR01438 292 KINKKTGK-IPADEEEQTNVPYIYAVGDILEDKPE----LTPVaIQAGRLLAQRLfKGSTV 347
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
98-284 |
4.24e-07 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 53.42 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 98 RTVTAISGLTVPYDKLLIATGSTPLIIQVPGSTlpgVVGFRDladVDTMLEAAARGGRAVVIGGGLLGLEAANGLKVKGM 177
Cdd:PRK07846 117 KTLRTGDGEEITADQVVIAAGSRPVIPPVIADS---GVRYHT---SDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 178 DVTVLhlmdtlmerqlDRSaGALLRH----------ELERRGITVLTGADTAEIVGSERVSAVRLKNGQELPADLVVMAV 247
Cdd:PRK07846 191 RVTVV-----------NRS-GRLLRHldddiserftELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVAT 258
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1388779335 248 GIRPN---MALGkAAGLACGRG--IQVDDAMTTSDPAILSVG 284
Cdd:PRK07846 259 GRVPNgdlLDAA-AAGVDVDEDgrVVVDEYQRTSAEGVFALG 299
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
74-292 |
1.39e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 51.70 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 74 RDWYEANGIKLLTGdrVEVidraNRTVTAiSGLTVPYDKLLIATGST-PLIIQVPGSTLPGV---VGF-----RDLADVD 144
Cdd:PRK12810 200 IELMEAEGIEFRTN--VEV----GKDITA-EELLAEYDAVFLGTGAYkPRDLGIPGRDLDGVhfaMDFliqntRRVLGDE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 145 TMLEAAARGGRAVVIGGGLlgleaanglkvKGMD------------VTVLHLMDTLMERQLDRSAGALLRHELE-----R 207
Cdd:PRK12810 273 TEPFISAKGKHVVVIGGGD-----------TGMDcvgtairqgaksVTQRDIMPMPPSRRNKNNPWPYWPMKLEvsnahE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 208 RGITVLTGADTAEIVGSE------RVSAVRLKNG---------QELPADLVVMAVGIR-PNMALGKAAGLAC---GRGIQ 268
Cdd:PRK12810 342 EGVEREFNVQTKEFEGENgkvtgvKVVRTELGEGdfepvegseFVLPADLVLLAMGFTgPEAGLLAQFGVELderGRVAA 421
|
250 260
....*....|....*....|....
gi 1388779335 269 VDDAMTTSDPAILSVGECVehRGQ 292
Cdd:PRK12810 422 PDNAYQTSNPKVFAAGDMR--RGQ 443
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
42-285 |
3.13e-06 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 50.64 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 42 VFGAEPHPNYNRIMlspvlaGEKTFEQIVLNG--RDWYEANGIKLLTGdRVEVIDraNRTVTaISGLTVPYDKLLIATGS 119
Cdd:PLN02546 157 KYETEPKHDWNTLI------ANKNAELQRLTGiyKNILKNAGVTLIEG-RGKIVD--PHTVD-VDGKLYTARNILIAVGG 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 120 TPLIIQVPGStlpgvvgfRDLADVDTMLEAAARGGRAVVIGGGLLGLEAA---NGLKVkgmDVTVLHLMDTLMeRQLDRS 196
Cdd:PLN02546 227 RPFIPDIPGI--------EHAIDSDAALDLPSKPEKIAIVGGGYIALEFAgifNGLKS---DVHVFIRQKKVL-RGFDEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 197 AGALLRHELERRGITVLTGADTAEIVGSERVSaVRLKNGQELPADL--VVMAVGIRPNMA-LG-KAAGLACGR--GIQVD 270
Cdd:PLN02546 295 VRDFVAEQMSLRGIEFHTEESPQAIIKSADGS-LSLKTNKGTVEGFshVMFATGRKPNTKnLGlEEVGVKMDKngAIEVD 373
|
250
....*....|....*
gi 1388779335 271 DAMTTSDPAILSVGE 285
Cdd:PLN02546 374 EYSRTSVPSIWAVGD 388
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
152-269 |
7.01e-06 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 49.31 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 152 RGGRAVVIGGGLLGLEAANGLKVKGMDVTVlhlMDtlmerqlDRSAGALLRHELERRGITVLTGADTAEIVGServsavr 231
Cdd:COG0771 3 KGKKVLVLGLGKSGLAAARLLAKLGAEVTV---SD-------DRPAPELAAAELEAPGVEVVLGEHPEELLDG------- 65
|
90 100 110
....*....|....*....|....*....|....*...
gi 1388779335 232 lkngqelpADLVVMAVGIRPNMALGKAAgLAcgRGIQV 269
Cdd:COG0771 66 --------ADLVVKSPGIPPDHPLLKAA-RA--AGIPV 92
|
|
| Fer2_BFD-like |
cd19942 |
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ... |
429-475 |
1.05e-05 |
|
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.
Pssm-ID: 381075 [Multi-domain] Cd Length: 49 Bit Score: 43.20 E-value: 1.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1388779335 429 ICGCNGVCKGTIVTAITEKGLSNLDEVRAHTKASASCGSCTGQVEQL 475
Cdd:cd19942 3 VCECFAVTEKELREAIRKGGLKTVEELLTGTGAGGGCGVCHPHVAQL 49
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
107-316 |
1.31e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 48.67 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 107 TVPYDKLLIATGSTPLIIQ-VPGStlpgvvgfRDLA-DVDTMLEAAARGGRAVVIGGGLLGLEAANGLKVKGMDVTVlhL 184
Cdd:PTZ00052 142 TITAKYILIATGGRPSIPEdVPGA--------KEYSiTSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV--A 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 185 MDTLMERQLDRSAGALLRHELERRGITVLTGADTAEIVGSERVSAVRLKNGQELPADLVVMAVGIRPNMALGKAAGLacg 264
Cdd:PTZ00052 212 VRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAI--- 288
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1388779335 265 rGIQVDDAM-------TTSDPAILSVGECVEHRGQtyglVAPLFEMAKVAAAR--LAGSTE 316
Cdd:PTZ00052 289 -GVHVNKSNkiiapndCTNIPNIFAVGDVVEGRPE----LTPVAIKAGILLARrlFKQSNE 344
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
578-787 |
1.37e-05 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 48.46 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 578 RMWGGLTSAKELRAIADVVDKFA-IPTVKVTGGQRIDLFGVRKEDLPAVWADLNAAGMVSGHAyakGLRTVKTCVGSEWC 656
Cdd:PRK09566 71 RVPNGILTSEQLRVLASIVQRYGdDGSADITTRQNLQLRGILLEDLPEILNRLKAVGLTSVQS---GMDNVRNITGSPVA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 657 RFGTQ---DSTGLGVKLERM-TWG-------TWTPHKVKLAVSGCPRNCAEATIKDLGVVCVDS----GYELHVGG--NG 719
Cdd:PRK09566 148 GIDPDeliDTRPLTQKLQDMlTNNgegnpefSNLPRKFNIAIAGGRDNSVHAEINDIAFVPAYKdgvlGFNVLVGGffSS 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1388779335 720 GMHVRACDLLVKVETEaEVLEYTGAYMQLYRE----EARYLERTAPWLERVGLDYLkRRLVDDAEGRAALNA 787
Cdd:PRK09566 228 QRCAYAIPLNAWVKPD-EVVRLCRAILEVYRDnglrANRQKGRLMWLIDEWGIEKF-RAAVEAQFGPPLLTA 297
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
11-321 |
1.45e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 48.22 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 11 RERLVVVGNGMAGIRTLEELlakAPDRYDITVFGAEPHpnynrIMLSPVLAGEKT----FEQIVLNGRDWYEANGIKLLT 86
Cdd:PTZ00318 10 KPNVVVLGTGWAGAYFVRNL---DPKKYNITVISPRNH-----MLFTPLLPQTTTgtleFRSICEPVRPALAKLPNRYLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 87 GDRVEVIDRANRTVTAISGL---------TVPYDKLLIATGSTPLIIQVPGST-----LPGVVGFRDL----------AD 142
Cdd:PTZ00318 82 AVVYDVDFEEKRVKCGVVSKsnnanvntfSVPYDKLVVAHGARPNTFNIPGVEeraffLKEVNHARGIrkrivqcierAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 143 V-DTMLEAAARGGRAVVIGGGLLGLEAANGLK--------------VKGMDVTVLHLMDTLMErQLDRSAGALLRHELER 207
Cdd:PTZ00318 162 LpTTSVEERKRLLHFVVVGGGPTGVEFAAELAdffrddvrnlnpelVEECKVTVLEAGSEVLG-SFDQALRKYGQRRLRR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 208 RGITVLTGADTAEIVGSErvsaVRLKNGQELPADLVVMAVGIRPNmALGKAagLACGRG----IQVDDAMTTSD-PAILS 282
Cdd:PTZ00318 241 LGVDIRTKTAVKEVLDKE----VVLKDGEVIPTGLVVWSTGVGPG-PLTKQ--LKVDKTsrgrISVDDHLRVKPiPNVFA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1388779335 283 VGEC--VEHRgqtyglvaPLFEMAKVAaarlagSTEAAYTG 321
Cdd:PTZ00318 314 LGDCaaNEER--------PLPTLAQVA------SQQGVYLA 340
|
|
| NasA-like_Fer2_BFD-like |
cd19948 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ... |
429-477 |
1.82e-05 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins; The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381081 [Multi-domain] Cd Length: 53 Bit Score: 42.90 E-value: 1.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1388779335 429 ICGCNGVCKGTIVTAITEKGLSNLDEVRAHTKASASCGSCTGQVEQLLA 477
Cdd:cd19948 4 VCACFSVGENTIRRAIADNGLTSVAQVGTCLKAGTNCGSCVPEIQKLLS 52
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
110-287 |
4.61e-05 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 47.04 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 110 YDKLLIATGS-TPLIIQVPGSTLPGV---------VGFRDLA--DVDTMLEAaarGGRAVVIGGGLLGLEAANGLKVKGM 177
Cdd:PRK12778 518 FKGIFIASGAgLPNFMNIPGENSNGVmssneyltrVNLMDAAspDSDTPIKF---GKKVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 178 DVTvlhlmdTLMERQLDRSAGALLR--HELERRGITVLTGADTAEIVGSE--RVSAVRL---KNGQ-------------- 236
Cdd:PRK12778 595 ERV------TIVYRRSEEEMPARLEevKHAKEEGIEFLTLHNPIEYLADEkgWVKQVVLqkmELGEpdasgrrrpvaipg 668
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388779335 237 ---ELPADLVVMAVGIRPNMALGKA-AGLACGR--GIQVDDAMTTSDPAILSVGECV 287
Cdd:PRK12778 669 stfTVDVDLVIVSVGVSPNPLVPSSiPGLELNRkgTIVVDEEMQSSIPGIYAGGDIV 725
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
197-250 |
4.53e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 43.68 E-value: 4.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1388779335 197 AGALLRHeLERRGITVLTGADTAEI-VGSERVSAVRLKNGQELPADLVVMAVGIR 250
Cdd:COG1233 225 ADALARL-AEELGGEIRTGAEVERIlVEGGRATGVRLADGEEIRADAVVSNADPA 278
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
153-286 |
6.12e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.22 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 153 GGRAVVIGGGLLGLEAANGLK--VKgmDVTVLHLMDTLmerqldrSAGALLRHELERRG-ITVLTGADTAEIVG-SERVS 228
Cdd:PRK15317 351 GKRVAVIGGGNSGVEAAIDLAgiVK--HVTVLEFAPEL-------KADQVLQDKLRSLPnVTIITNAQTTEVTGdGDKVT 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1388779335 229 AVRLK---NGQE--LPADLVVMAVGIRPNMA-LGKAAGLAcGRG-IQVDDAMTTSDPAILSVGEC 286
Cdd:PRK15317 422 GLTYKdrtTGEEhhLELEGVFVQIGLVPNTEwLKGTVELN-RRGeIIVDARGATSVPGVFAAGDC 485
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
152-252 |
1.06e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.83 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 152 RGGRAVVIGGGLLGLEAANGLKVKGMDVTVLHLMDTLMERQLDRSAGalLR-------HELERRG-ITVLTGADTAEIVG 223
Cdd:pfam13738 154 AGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYS--LSpdtlnrlEELVKNGkIKAHFNAEVKEITE 231
|
90 100 110
....*....|....*....|....*....|
gi 1388779335 224 SERVSAVRLKNGQELPA-DLVVMAVGIRPN 252
Cdd:pfam13738 232 VDVSYKVHTEDGRKVTSnDDPILATGYHPD 261
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
96-212 |
1.36e-03 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 41.63 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 96 ANRTVTAI---SGLTVpYDKLLIATGSTPLIiqVPGSTLPG----VVGFRDLADVDTMLEAAA---RGGRAVVIGGGLLG 165
Cdd:cd01620 98 TNRGVVEVlmrKKLTA-YALEDLENDFRPRL--APNSNIAGyagvQLGAYELARIQGGRMGGAggvPPAKVLIIGAGVVG 174
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1388779335 166 LEAANGLKVKGMDVTV-------LHLMDTLMERQLDRSAGALLRHELERRGITV 212
Cdd:cd01620 175 LGAAKIAKKLGANVLVydikeekLKGVETLGGSRLRYSQKEELEKELKQTDILI 228
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
124-287 |
1.42e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 42.17 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 124 IQVPGSTLPGVVgfrdlaDVDTMLEAAARGG------RAVVIGGGLLGLEAAN-GLKVKGMDVTVLHLmdtlmeRQLDRS 196
Cdd:PRK12771 238 LPIPGEDAAGVL------DAVDFLRAVGEGEppflgkRVVVIGGGNTAMDAARtARRLGAEEVTIVYR------RTREDM 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 197 AGalLRHELE---RRGITVLTGADTAEIVGSERVSAVRL-----------------KNGQE--LPADLVVMAVGIRPNMA 254
Cdd:PRK12771 306 PA--HDEEIEealREGVEINWLRTPVEIEGDENGATGLRvitvekmeldedgrpspVTGEEetLEADLVVLAIGQDIDSA 383
|
170 180 190
....*....|....*....|....*....|....*.
gi 1388779335 255 -LGKAAGLACGRG-IQVDDA-MTTSDPAILSVGECV 287
Cdd:PRK12771 384 gLESVPGVEVGRGvVQVDPNfMMTGRPGVFAGGDMV 419
|
|
| Fer2_BFD |
cd19945 |
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ... |
429-480 |
1.98e-03 |
|
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes Escherichia coli and Pseudomonas aeruginosa bacterioferritin-associated ferredoxin BFD which binds an [2Fe-2S] cluster and appears to interact with bacterioferritin (E. coli BFR/YheA and P. aeruginosa BfrB), a dynamic regulator of intracellular iron levels. It has been suggested that BFD and bacterioferritin form an electron transfer complex which may participate in the iron storage or iron immobilization functions of bacterioferritin. For Pseudomonas aeruginosa, it has been shown that mobilization of Fe3+ stored in BfrB requires interaction with BFD, which transfers electrons to reduce Fe3+ in the internal cavity of BfrB for subsequent release of Fe2+. The stability of BFD may be aided by an anion-binding site found within this domain. In addition to BFD, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins such as the large subunit of NADH-dependent nitrite reductase and the Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381078 [Multi-domain] Cd Length: 54 Bit Score: 36.79 E-value: 1.98e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1388779335 429 ICGCNGVCKGTIVTAItEKGLSNLDEVRAHTKASASCGSCTGQVEQLLALTL 480
Cdd:cd19945 3 VCLCNGITDKQIRQAV-AQGATSLRELREQLGVGSQCGKCARMARQVLEEEL 53
|
|
| CopZ-like_Fer2_BFD-like |
cd10141 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus ... |
429-475 |
2.65e-03 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus fulgidus CopZ, and similar proteins; Archaeoglobus fulgidus CopZ is a fusion of a redox-active domain (containing a mononuclear metal center and an [2Fe-2S] cluster) with a CXXC-containing copper-binding domain. It is a soluble Cu+ chaperone which delivers cytoplasmic Cu+ to the transmembrane metal-binding sites in the Cu+-ATPase CopA; CopA couples the hydrolysis of ATP to the efflux of cytoplasmic Cu+. In addition to CopZ, the BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), and the large subunit of NADH-dependent nitrite reductase. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381074 [Multi-domain] Cd Length: 58 Bit Score: 36.82 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1388779335 429 ICGCNGVCKGTIVTAITEKGLSNLDEVRAHTKA----------SASCgsCTGQVEQL 475
Cdd:cd10141 4 VCYCFGVTEEDIIEAVAETGATTVEEIRATGKAgrcacevnnpSGRC--CLGNVKKA 58
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
16-287 |
4.81e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 40.52 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 16 VVGNGMAGIrTLEELLAKAPdrYDITVFGAEPHP----NYN--RIMLsPVLAGEKTFEQIvlngrdwyEANGIKLLTGDR 89
Cdd:PRK13984 288 IVGSGPAGL-SAAYFLATMG--YEVTVYESLSKPggvmRYGipSYRL-PDEALDKDIAFI--------EALGVKIHLNTR 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 90 VevidraNRTVTaISGLTVPYDKLLIATG-----STPliiqVPGSTLPGVVGFRDLADvdtMLEAAARG--------GRA 156
Cdd:PRK13984 356 V------GKDIP-LEELREKHDAVFLSTGftlgrSTR----IPGTDHPDVIQALPLLR---EIRDYLRGegpkpkipRSL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 157 VVIGGGLLGLEAANGL------KVKGMDVTVLHLMDTLMERQLDRSAgalLRHELERrGITVLTGADTAEI-VGSERVSA 229
Cdd:PRK13984 422 VVIGGGNVAMDIARSMarlqkmEYGEVNVKVTSLERTFEEMPADMEE---IEEGLEE-GVVIYPGWGPMEVvIENDKVKG 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 230 VRLK--------NGQ-----------ELPADLVVMAVGIRPNMA-----LGKAAGLACGRgIQVDDAMTTSDPAILSVGE 285
Cdd:PRK13984 498 VKFKkcvevfdeEGRfnpkfdesdqiIVEADMVVEAIGQAPDYSylpeeLKSKLEFVRGR-ILTNEYGQTSIPWLFAGGD 576
|
..
gi 1388779335 286 CV 287
Cdd:PRK13984 577 IV 578
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
576-720 |
8.61e-03 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 39.76 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 576 VPrmwGGLTSAKELRAIADVVDKFAIPTVKVTGGQRIDLFGVRKEDLPAVWAD-----------LNAAGMVSghayakgl 644
Cdd:PLN02431 402 VP---VGRLQAADMDELARLADEYGSGELRLTVEQNIIIPNVPNSKVEALLAEpllqrfspnpgLLLKGLVA-------- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1388779335 645 rtvktCVGSEWCRFG----TQDSTGLGVKLERMTWgtwTPHKVKLAVSGCPRNCAEATIKDLGVV-C--------VDSGY 711
Cdd:PLN02431 471 -----CTGNQFCGQAiietKARALKVTEELERLVE---VPRPVRMHWTGCPNSCGQVQVADIGFMgCmardengkAVEGA 542
|
....*....
gi 1388779335 712 ELHVGGNGG 720
Cdd:PLN02431 543 DIFVGGRVG 551
|
|
| |
