|
Name |
Accession |
Description |
Interval |
E-value |
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
6-791 |
0e+00 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 1397.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 6 LVLVGNGMAGVRAIEEILSVAKDEFQITIFGAEPHPNYNRILLSKVLQGDTDIKDITLNDWDWYEENNIQLYTNETVIKV 85
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMFEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 86 DTENKTVITDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAARGLL 165
Cdd:TIGR02374 81 DTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 166 NLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTSIEADLVVMAVGIRPNT 245
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 246 TLGAESGIPVNRGIIVNDYMQTEIPHIYAVGECAEHRGIAYGLVAPLYEQAKVLAKHMCGIETKPYEGSVLSTQLKVSGV 325
Cdd:TIGR02374 241 ELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECEEYEGSDLSAKLKLLGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 326 EVFSAGDFNESEEKKAIKVFDEQDGIYKKIVLRGNQIVGAVLFGDSSEGNRLFSMIQKEADISETSKISILQPLSQEAGT 405
Cdd:TIGR02374 321 DVWSAGDAQETERTTSIKIYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVLKQADISEDPAIIKPQISGPEAGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 406 SITAAMSDDEIICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVEEILQHTLGSDFDasAQKEAICGCT 485
Cdd:TIGR02374 401 PGVEAMPDSEQICSCNTVTKGAIIDAIHTGSCTTVEELKACTKAGTSCGGCKPLVEQLLRAELNSQYT--ASTPALCECT 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 486 TLSRDEVVEEIKAKGLSHTREVMNVLGWKTPEGCSKCRPALNYYLGMINPTKYEDDRTSRFVNERMHANIQKDGTYSVVP 565
Cdd:TIGR02374 479 DFSRDELFEEIQARGFTTFAEVMNQLGWKTKNGCSTCKPAVQYYLAMLYPGFILDEEATSLSNDHFLANIQKDGTYSVIP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 566 RMYGGVTNSTDLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWEDLDMPSG-YAYGKTLRTVKTCVGEQFCRFG 644
Cdd:TIGR02374 559 RMYGGRTNPEQLRTIANIAEAYSIPYVKITGGQRLDLFGAKKDDLPNIWKDLKMPGYeHAYGKALRTVKTCVGSQWCRYG 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 645 TQDSMALGIALEKKFEGLNTPHKVKMAVSACPRNCAESGIKDLGVVGIDGGWELYVGGNGGTHLRAGDLLMKVKTNEEVL 724
Cdd:TIGR02374 639 NQDSVQLAIQLERRYEGLRTPHKIKIGVSGCERECAEAAGKDVGVIATEKGWNLYVGGNGGTHPRHGDLLAVDEDEETLI 718
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835700157 725 EYAGAYLQYYRETANYLERTSAWLERVGLSHVQSVLNDPEKRQELNGRMNETLSVHKDPWKDFLEDK 791
Cdd:TIGR02374 719 GYIDRFLQYYRETADYLERTAPWLERLGIDHVREVLFEDDLRAELEESMQRDLSLIKCPWKETLEDK 785
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
1-795 |
0e+00 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 585.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 1 MGKKQLVLVGNGMAGVRAIEEILSVA-KDEFQITIFGAEPHPNYNRILLSKVLQGDTdIKDITLNDWDWYEENNIQLYTN 79
Cdd:PRK14989 1 MSKVRLAIIGNGMVGHRFIEDLLDKAdAANFDITVFCEEPRIAYDRVHLSSYFSHHT-AEELSLVREGFYEKHGIKVLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 80 ETVIKVDTENKTVITDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQYKKAAVIGGGLLGLE 159
Cdd:PRK14989 80 ERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 160 AARGLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIV--GDDRVEGLRFKDGTSIEADLVVM 237
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADGSELEVDFIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 238 AVGIRPNTTLGAESGIPVNR--GIIVNDYMQTEIPHIYAVGECAEHRGIAYGLVAPLYEQAKVLAKHMCGIETKpYEGSV 315
Cdd:PRK14989 240 STGIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENA-FEGAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 316 LSTQLKVSGVEVFSAGDFN-ESEEKKAIKVFDEQDGIYKKIVLR--GNQIVGAVLFGDSSEGNRLFSMIQKEADISETSK 392
Cdd:PRK14989 319 LSAKLKLLGVDVGGIGDAHgRTPGARSYVYLDESKEIYKRLIVSedNKTLLGAVLVGDTSDYGNLLQLVLNAIELPENPD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 393 ISILQPLSQEAGTSITA-AMSDDEIICGCNGVSKGAIIQAIQeKGCSSTDEIKACTGASRSCGGCKPLVEEILQHTLgsd 471
Cdd:PRK14989 399 SLILPAHAGSGKPSIGVdKLPDSAQICSCFDVTKGDLIAAIN-KGCHTVAALKAETKAGTGCGGCIPLVTQVLNAEL--- 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 472 fdaSAQ----KEAICGCTTLSRDEVVEEIKAKGLSHTREVMNVLGwkTPEGCSKCRPALNYYLG------MINP--TKYE 539
Cdd:PRK14989 475 ---AKQgievNNNLCEHFAYSRQELFHLIRVEGIKTFEELLAKHG--KGYGCEVCKPTVGSLLAscwneyILKPqhTPLQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 540 DdrtsrfVNERMHANIQKDGTYSVVPRMYGGVTNSTDLRKIADVVDKYEIpLVKMTGGQRIDLIGVKKEDLPKVWEDL-- 617
Cdd:PRK14989 550 D------TNDNFLANIQKDGTYSVIPRSAGGEITPEGLMAVGRIAREFNL-YTKITGSQRIGLFGAQKDDLPEIWRQLie 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 618 -DMPSGYAYGKTLRTVKTCVGEQFCRFGTQDSMALGIALEKKFEGLNTPHKVKMAVSACPRNCAESGIKDLGVVGIDGGW 696
Cdd:PRK14989 623 aGFETGHAYAKALRMAKTCVGSTWCRYGVGDSVGLGVELENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATEKGW 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 697 ELYVGGNGGTHLRAGDLLMKVKTNEEVLEYAGAYLQYYRETANYLERTSAWLERV--GLSHVQSVLNDpeKRQELNGRMN 774
Cdd:PRK14989 703 NLYVCGNGGMKPRHADLLAADLDRETLIKYLDRFMMFYIRTADKLQRTAVWLENLegGIDYLKAVIID--DKLGLNAQLE 780
|
810 820
....*....|....*....|....*
gi 1835700157 775 ETLSVHKD----PWKDFLEDKQTSK 795
Cdd:PRK14989 781 EEMARLREavvcEWTETVNTPSAQT 805
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
3-399 |
0e+00 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 544.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 3 KKQLVLVGNGMAGVRAIEEILSVAKDeFQITIFGAEPHPNYNRILLSKVLQGDTDIKDITLNDWDWYEENNIQLYTNETV 82
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPD-GEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 83 IKVDTENKTVITDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAAR 162
Cdd:COG1251 80 TAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 163 GLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTSIEADLVVMAVGIR 242
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 243 PNTTLGAESGIPVNRGIIVNDYMQTEIPHIYAVGECAEHRGIAYG-----LVAPLYEQAKVLAKHMCGIETkPYEGSVLS 317
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPA-AYEGSVPS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 318 TQLKVSGVEVFSAGDFNESEEkkAIKVFDEQDGIYKKIVLRGNQIVGAVLFGDSSEGNRLFSMIQKEADISETSKISILQ 397
Cdd:COG1251 319 TKLKVFGVDVASAGDAEGDEE--VVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAAL 396
|
..
gi 1835700157 398 PL 399
Cdd:COG1251 397 PL 398
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
28-332 |
1.38e-77 |
|
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: 253.58 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 28 DEFQITIFGAEPHPNYNRILLSK-VLQGDTDIKDITLNDWDWYEENNIQLYTNETVIKVDTENKTVITDADRIQPYDELI 106
Cdd:COG0446 4 PDAEITVIEKGPHHSYQPCGLPYyVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYDKLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 107 LATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQY--KKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMERq 184
Cdd:COG0446 84 LATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 185 LDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVeGLRFKDGTSIEADLVVMAVGIRPNTTLGAESGIPVNR--GIIVN 262
Cdd:COG0446 163 LDPEMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgWIKVD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835700157 263 DYMQTEIPHIYAVGECAEHRGIAYG------LVAPLYEQAKVLAKHMCGIETkPYEGsVLSTQLKVSGVEVFSAGD 332
Cdd:COG0446 242 ETLQTSDPDVYAAGDCAEVPHPVTGktvyipLASAANKQGRVAAENILGGPA-PFPG-LGTFISKVFDLCIASTGT 315
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
4-278 |
6.00e-64 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 216.03 E-value: 6.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 4 KQLVLVGNGMAGVRAIEEIlsvAKDEFQITIFGAEPHPNYNRILLSKVLQGDTDIKDITLNDWDWYE---------ENNI 74
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTL---AQLGGKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 75 QLYTNETVIKVDTENKTVI-----TDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQyKKAA 149
Cdd:pfam07992 78 EVLLGTEVVSIDPGAKKVVleelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLP-KRVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 150 VIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMeRQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTS 229
Cdd:pfam07992 157 VVGGGYIGVELAAALAKLGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1835700157 230 IEADLVVMAVGIRPNTTLGAESGIPVNR--GIIVNDYMQTEIPHIYAVGEC 278
Cdd:pfam07992 236 IDADLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDC 286
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
7-309 |
4.90e-47 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 172.02 E-value: 4.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 7 VLVGNGMAgvrAIEEILSVAKDEFQ--ITIFGAEPHPNYNRILLSKVL-QGDTDIKDITLNDWDWYEENNIQLYTNETVI 83
Cdd:PRK04965 6 VIIGSGFA---ARQLVKNIRKQDAHipITLITADSGDEYNKPDLSHVFsQGQRADDLTRQSAGEFAEQFNLRLFPHTWVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 84 KVDTENKTVITDADRIqPYDELILATGSVPFILPIPGaDKKGVT-----AFRDIKdtdtmlAASKQYKKAAVIGGGLLGL 158
Cdd:PRK04965 83 DIDAEAQVVKSQGNQW-QYDKLVLATGASAFVPPIPG-RELMLTlnsqqEYRAAE------TQLRDAQRVLVVGGGLIGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 159 EAARGLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDrvEGLR--FKDGTSIEADLVV 236
Cdd:PRK04965 155 ELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTD--SGIRatLDSGRSIEVDAVI 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835700157 237 MAVGIRPNTTLGAESGIPVNRGIIVNDYMQTEIPHIYAVGECAEHRGIAYGLVAPLYEQAKVLAKHMCGIETK 309
Cdd:PRK04965 233 AAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTP 305
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
67-370 |
8.70e-43 |
|
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: 161.79 E-value: 8.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 67 DWYEENNIQLY------TNETVIKVdtENKTVITdADRIqpydelILATGSVPFILPIPGADKKGvtafrdIKDTDTMLA 140
Cdd:COG1249 99 ELLKKNGVDVIrgrarfVDPHTVEV--TGGETLT-ADHI------VIATGSRPRVPPIPGLDEVR------VLTSDEALE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 141 ASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMeRQLDATAGRLLQNELEKQGMTFLLEKQTEEI-VGDDRV 219
Cdd:COG1249 164 LEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVeKTGDGV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 220 EgLRFKDG---TSIEADLVVMAVGIRPNT-TLGAES-GIPVNR--GIIVNDYMQTEIPHIYAVGECAEHRGIAYglVApl 292
Cdd:COG1249 243 T-VTLEDGggeEAVEADKVLVATGRRPNTdGLGLEAaGVELDErgGIKVDEYLRTSVPGIYAIGDVTGGPQLAH--VA-- 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 293 YEQAKVLAKHMCGIETKPYEGSVlstqlkVSGV-----EVFSAGdFNESEEKKA---IKVF-------------DEQDGI 351
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRA------IPSVvftdpEIASVG-LTEEEAREAgidVKVGkfpfaangralalGETEGF 390
|
330 340
....*....|....*....|
gi 1835700157 352 YKKIVLRGN-QIVGAVLFGD 370
Cdd:COG1249 391 VKLIADAETgRILGAHIVGP 410
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
69-367 |
3.08e-40 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 154.43 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 69 YEENNIQLYTNETVIKVDTENKTVI-----TDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAA-- 141
Cdd:PRK09564 66 FIKSGIDVKTEHEVVKVDAKNKTITvknlkTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELlk 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 142 SKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEG 221
Cdd:PRK09564 146 DEEIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 222 LRFKDGTsIEADLVVMAVGIRPNTTLGAESGIPV--NRGIIVNDYMQTEIPHIYAVGECAE--HRGIAYGLVAPLY---- 293
Cdd:PRK09564 226 VVTDKGE-YEADVVIVATGVKPNTEFLEDTGLKTlkNGAIIVDEYGETSIENIYAAGDCATiyNIVSNKNVYVPLAttan 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 294 EQAKVLAKHMCGIETkPYEGSVLSTQLKVSGVEVFSAGdFNESEEK------KAIKVFDE--------QDGIYKKIV--- 356
Cdd:PRK09564 305 KLGRMVGENLAGRHV-SFKGTLGSACIKVLDLEAARTG-LTEEEAKklgidyKTVFIKDKnhtnyypgQEDLYVKLIyea 382
|
330
....*....|....*...
gi 1835700157 357 ----LRGNQIVG---AVL 367
Cdd:PRK09564 383 dtkvILGGQIIGkkgAVL 400
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
3-318 |
1.42e-38 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 147.97 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 3 KKQLVLVGNGMAGVRAIEEILSVAKDEFQITIFGAEPH----PnynriLLSKVLQGDTDIKDITLNdwdwYEE----NNI 74
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYhlfqP-----LLPEVAAGTLSPDDIAIP----LREllrrAGV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 75 QLYTnETVIKVDTENKTVITDADRIQPYDELILATGSVPFILPIPGADK-----KGVTAFRDIKdtDTMLAASKQYKKA- 148
Cdd:COG1252 72 RFIQ-GEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEhalplKTLEDALALR--ERLLAAFERAERRr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 149 ----AVIGGGLLGLEAA-------------RGLLNLGMDVSVIHLAPFLMERqLDATAGRLLQNELEKQGMTFLLEKQTE 211
Cdd:COG1252 149 lltiVVVGGGPTGVELAgelaellrkllryPGIDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 212 EIVGDdrveGLRFKDGTSIEADLVVMAVGIRPNtTLGAESGIPVNRG--IIVNDYMQTE-IPHIYAVGECAEHRGIAYGL 288
Cdd:COG1252 228 EVDAD----GVTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVPgHPNVFAIGDCAAVPDPDGKP 302
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1835700157 289 VAPL----YEQAKVLAKHMC----GIETKPYE----GSVLST 318
Cdd:COG1252 303 VPKTaqaaVQQAKVLAKNIAallrGKPLKPFRyrdkGCLASL 344
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
626-763 |
1.16e-31 |
|
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: 120.84 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 626 GKTLRTVKTCVGEQFCRFGTQDSMALGIALEK----KFEGLNTPHKVKMAVSACPRNCAESGIKDLGVVGIDG-----GW 696
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDefepDYGFPYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKdggeiGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835700157 697 ELYVGGNGGTHLRAGDLLMKVK--TNEEVLEYAGAYLQYYR----ETANYLERTSAWLERVGLSHVQSVLNDP 763
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKVVPfvPEEDVLEVIEAILEVYRdhgdRENRKKERLKYLIERLGLEKFREEVEER 153
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
1-282 |
4.18e-31 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 126.19 E-value: 4.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 1 MGKKQLVLVGNGMAGVRAIEeilSVAKDEF--QITIFGAEPHPNYNRILLSK--VLQGDTDIKdiTLNDWDWYEENNIQL 76
Cdd:PRK09754 1 MKEKTIIIVGGGQAAAMAAA---SLRQQGFtgELHLFSDERHLPYERPPLSKsmLLEDSPQLQ--QVLPANWWQENNVHL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 77 YTNETVIKV-DTENKTVITDADRIQpYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQYKKAAVIGGGL 155
Cdd:PRK09754 76 HSGVTIKTLgRDTRELVLTNGESWH-WDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 156 LGLEAARGLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEgLRFKDGTSIEADLV 235
Cdd:PRK09754 155 IGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVV 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1835700157 236 VMAVGIRPNTTLGAESGIPVNRGIIVNDYMQTEIPHIYAVGECAEHR 282
Cdd:PRK09754 234 IYGIGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITR 280
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
105-305 |
9.56e-30 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 123.33 E-value: 9.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 105 LILATGSVPFIlpIPGADKKGvtafRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLM--E 182
Cdd:PRK06416 138 IILATGSRPRE--LPGIEIDG----RVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILpgE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 183 rqlDATAGRLLQNELEKQGMTFLLE---KQTEEivGDDRVEGLRFKDG--TSIEADLVVMAVGIRPNTT-LGAES-GIPV 255
Cdd:PRK06416 212 ---DKEISKLAERALKKRGIKIKTGakaKKVEQ--TDDGVTVTLEDGGkeETLEADYVLVAVGRRPNTEnLGLEElGVKT 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835700157 256 NRG-IIVNDYMQTEIPHIYAVGECAE-----HRGiayglvaplYEQAKVLAKHMCG 305
Cdd:PRK06416 287 DRGfIEVDEQLRTNVPNIYAIGDIVGgpmlaHKA---------SAEGIIAAEAIAG 333
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
77-281 |
1.09e-29 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 119.84 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 77 YTNETVIKVDTEN--KTVITD------ADRIqpydelILATGSVPFILPIPGADK---KGVTA--------FRDikdtdt 137
Cdd:COG0492 74 ILLEEVTSVDKDDgpFRVTTDdgteyeAKAV------IIATGAGPRKLGLPGEEEfegRGVSYcatcdgffFRG------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 138 mlaaskqyKKAAVIGGGLLGLEAARGLLNLGMDVSVIHlapflmeRQLDATAGRLLQNELEK-QGMTFLLEKQTEEIVGD 216
Cdd:COG0492 142 --------KDVVVVGGGDSALEEALYLTKFASKVTLIH-------RRDELRASKILVERLRAnPKIEVLWNTEVTEIEGD 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 217 DRVEGLRFKDGTS-----IEADLVVMAVGIRPNTTLGAESGIPVNRG--IIVNDYMQTEIPHIYAVGECAEH 281
Cdd:COG0492 207 GRVEGVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVRDY 278
|
|
| NirB_Fer2_BFD-like_2 |
cd19944 |
second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
479-530 |
8.83e-28 |
|
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: 106.11 E-value: 8.83e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 479 EAICGCTTLSRDEVVEEIKAKGLSHTREVMNVLGWKTPEGCSKCRPALNYYL 530
Cdd:cd19944 1 KTLCSCTDLSHDEVREAIQEHGLTSFEEVMAALGWKTPDGCEKCRPALNYYL 52
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
68-321 |
9.47e-28 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 117.19 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 68 WYEENNIQLYTNETVIKVDTENKTV-----ITDADRIQPYDELILATGSVPFILPIpgaDKKGVTAFRDIKDTDTM--LA 140
Cdd:PRK13512 67 FYDRKQITVKTYHEVIAINDERQTVtvlnrKTNEQFEESYDKLILSPGASANSLGF---ESDITFTLRNLEDTDAIdqFI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 141 ASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLmERQLDATAGRLLQNELEKQGMTFLLEkqtEEIvgdDRVE 220
Cdd:PRK13512 144 KANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLN---EEI---DAIN 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 221 G--LRFKDGTSIEADLVVMAVGIRPNTTLGAESGIPVNRG--IIVNDYMQTEIPHIYAVGECAE--HRGIAYGLVAPL-- 292
Cdd:PRK13512 217 GneVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITshYRHVDLPASVPLaw 296
|
250 260 270
....*....|....*....|....*....|.
gi 1835700157 293 --YEQAKVLAKHMCGIETKPYEGSVLSTQLK 321
Cdd:PRK13512 297 gaHRAASIVAEQIAGNDTIEFKGFLGNNIVK 327
|
|
| NirB_Fer2_BFD-like_1 |
cd19943 |
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
412-464 |
6.75e-27 |
|
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: 103.47 E-value: 6.75e-27
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1835700157 412 SDDEIICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVEEIL 464
Cdd:cd19943 1 PDDAEVCGCNGVSKGAIVQAIQEKGLTTLDEVKACTKASTSCGGCTPLVEQLL 53
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
70-373 |
1.14e-25 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 111.04 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 70 EENNIQLYTNETVIKvdtENKTVITDADRIQpYDELILATGS-VPfilPIPGADKKGVTafrDIKDTDTMLAASKQYKKA 148
Cdd:PRK06292 103 KKPKIDKIKGTARFV---DPNTVEVNGERIE-AKNIVIATGSrVP---PIPGVWLILGD---RLLTSDDAFELDKLPKSL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 149 AVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMeRQLDATAGRLLQNELEKQgMTFLLEKQTEEI-VGDDRVEGLRFKDG 227
Cdd:PRK06292 173 AVIGGGVIGLELGQALSRLGVKVTVFERGDRIL-PLEDPEVSKQAQKILSKE-FKIKLGAKVTSVeKSGDEKVEELEKGG 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 228 --TSIEADLVVMAVGIRPNT-TLGAES-GIPV-NRGII-VNDYMQTEIPHIYAVGEC---------AEHRGIAYGLVAPL 292
Cdd:PRK06292 251 ktETIEADYVLVATGRRPNTdGLGLENtGIELdERGRPvVDEHTQTSVPGIYAAGDVngkppllheAADEGRIAAENAAG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 293 YEQAKVLAKHMCG-IETKPYEGSVLST--QLKVSGVEvFSAGDFNESEEKKAiKVFDEQDGIYKKIVLRGN-QIVGAVLF 368
Cdd:PRK06292 331 DVAGGVRYHPIPSvVFTDPQIASVGLTeeELKAAGID-YVVGEVPFEAQGRA-RVMGKNDGFVKVYADKKTgRLLGAHII 408
|
....*
gi 1835700157 369 GDSSE 373
Cdd:PRK06292 409 GPDAE 413
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
90-278 |
2.44e-24 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 107.21 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 90 KTVITDADRIQpYDELILATGSVPFILPIPGADKKGVTafrdikDTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGM 169
Cdd:PRK06370 123 NTVRVGGETLR-AKRIFINTGARAAIPPIPGLDEVGYL------TNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 170 DVSVIHLAPFLMERQlDATAGRLLQNELEKQGMTFLLEKQTEEI--VGDDRVEGLRFKDGT-SIEADLVVMAVGIRPNTT 246
Cdd:PRK06370 196 EVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVerDGDGIAVGLDCNGGApEITGSHILVAVGRVPNTD 274
|
170 180 190
....*....|....*....|....*....|....*.
gi 1835700157 247 -LGAE-SGIPVNR--GIIVNDYMQTEIPHIYAVGEC 278
Cdd:PRK06370 275 dLGLEaAGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
69-310 |
1.12e-23 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 105.24 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 69 YEENNIQLYT------NETVIKVDTEN--KTVITdADRIqpydelILATGSVPFILP-IPgadkkgvtaFRD--IKDTDT 137
Cdd:PRK05249 104 YERNRVDLIQgrarfvDPHTVEVECPDgeVETLT-ADKI------VIATGSRPYRPPdVD---------FDHprIYDSDS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 138 MLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVI----HLAPFLmerqlDATAGRLLQNELEKQGMTFLLEKQTEEI 213
Cdd:PRK05249 168 ILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLIntrdRLLSFL-----DDEISDALSYHLRDSGVTIRHNEEVEKV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 214 VGDDRVEGLRFKDGTSIEADLVVMAVGIRPNT-TLGAES-GIPVN-RGII-VNDYMQTEIPHIYAVGECaehrgIAY-GL 288
Cdd:PRK05249 243 EGGDDGVIVHLKSGKKIKADCLLYANGRTGNTdGLNLENaGLEADsRGQLkVNENYQTAVPHIYAVGDV-----IGFpSL 317
|
250 260
....*....|....*....|..
gi 1835700157 289 VAPLYEQAKVLAKHMCGIETKP 310
Cdd:PRK05249 318 ASASMDQGRIAAQHAVGEATAH 339
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
70-278 |
1.97e-22 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 101.00 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 70 EENNIQLY------TNETVIKVDTENKTvitdADRIqpydeLIlATGSVPFILPIPGADKkGVTafrdikdTDTMLAASK 143
Cdd:PRK06116 104 ENNGVDLIegfarfVDAHTVEVNGERYT----ADHI-----LI-ATGGRPSIPDIPGAEY-GIT-------SDGFFALEE 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 144 QYKKAAVIGGGLLGLEAArGLLN-LGMDVSVIHLAP-FLmeRQLDATAGRLLQNELEKQGMTFLLEKQTEEIV--GDDRV 219
Cdd:PRK06116 166 LPKRVAVVGAGYIAVEFA-GVLNgLGSETHLFVRGDaPL--RGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEknADGSL 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835700157 220 EgLRFKDGTSIEADLVVMAVGIRPNTT-LGAES-GIPVN-RG-IIVNDYMQTEIPHIYAVGEC 278
Cdd:PRK06116 243 T-LTLEDGETLTVDCLIWAIGREPNTDgLGLENaGVKLNeKGyIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
81-285 |
3.62e-22 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 100.77 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 81 TVIKVDTENKTVITdADRIqpydelILATGSVPfiLPIPGADKKGvtafRDIKDTDTMLAASKQYKKAAVIGGGLLGLEA 160
Cdd:PRK06327 132 YEIKVTGEDETVIT-AKHV------IIATGSEP--RHLPGVPFDN----KIILDNTGALNFTEVPKKLAVIGAGVIGLEL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 161 ARGLLNLGMDVSVIHLAP-FLMerQLDATAGRLLQNELEKQGMTFLLEKQTEEI-VGDDRVEgLRFKDGT----SIEADL 234
Cdd:PRK06327 199 GSVWRRLGAEVTILEALPaFLA--AADEQVAKEAAKAFTKQGLDIHLGVKIGEIkTGGKGVS-VAYTDADgeaqTLEVDK 275
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835700157 235 VVMAVGIRPNTT-LGAES-GIPVN-RGII-VNDYMQTEIPHIYAVGEC---------AEHRGIA 285
Cdd:PRK06327 276 LIVSIGRVPNTDgLGLEAvGLKLDeRGFIpVDDHCRTNVPNVYAIGDVvrgpmlahkAEEEGVA 339
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
89-277 |
8.30e-21 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 95.97 E-value: 8.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 89 NKTVITDA--DRIQ-PYDELILATGSVPFILPIPG-ADKKGVTafrdikDTDTMLAASKQYKKAAVIGGGLLGLEAARGL 164
Cdd:PRK07251 103 NKVIEVQAgdEKIElTAETIVINTGAVSNVLPIPGlADSKHVY------DSTGIQSLETLPERLGIIGGGNIGLEFAGLY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 165 LNLGMDVSVIHLAPFLMERQLDATAgRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTSIeADLVVMAVGIRPN 244
Cdd:PRK07251 177 NKLGSKVTVLDAASTILPREEPSVA-ALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDETYR-FDALLYATGRKPN 254
|
170 180 190
....*....|....*....|....*....|....*..
gi 1835700157 245 TT-LGAE-SGIPVN-RG-IIVNDYMQTEIPHIYAVGE 277
Cdd:PRK07251 255 TEpLGLEnTDIELTeRGaIKVDDYCQTSVPGVFAVGD 291
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
70-281 |
1.08e-20 |
|
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: 95.95 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 70 EENNIQLYTNETVIKVDtenKTVITDADR-IQPYDELILATGSVPFILPIPGADKKgvtafrDIKDTDTMLAASKQYKKA 148
Cdd:TIGR02053 99 SSYGVDYLRGRARFKDP---KTVKVDLGReVRGAKRFLIATGARPAIPPIPGLKEA------GYLTSEEALALDRIPESL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 149 AVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMERQlDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFK--- 225
Cdd:TIGR02053 170 AVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPRE-EPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEkpg 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 226 DGTSIEADLVVMAVGIRPNT-TLGAE-SGIPVNR--GIIVNDYMQTEIPHIYAVGECAEH 281
Cdd:TIGR02053 249 GQGEVEADELLVATGRRPNTdGLGLEkAGVKLDErgGILVDETLRTSNPGIYAAGDVTGG 308
|
|
| Rubredoxin_C |
pfam18267 |
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin ... |
317-385 |
3.01e-19 |
|
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: 82.22 E-value: 3.01e-19
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835700157 317 STQLKVSGVEVFSAGDFNESEEKKAIKVFDEQDGIYKKIVLRGNQIVGAVLFGDSSEGNRLFSMIQKEA 385
Cdd:pfam18267 2 STILKVFGIDLFSMGDIEENDNAEEIVKVDASNGIYKKLFIRDGKLVGAILIGDTSESPKLKKAIEKKI 70
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-227 |
3.27e-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: 82.64 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 147 KAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMeRQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKD 226
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 1835700157 227 G 227
Cdd:pfam00070 80 G 80
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
59-283 |
4.03e-19 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 90.96 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 59 KDITLNDWDWYEENNIQLYTNeTVIKVDtenktvITDADRIQPYDELILATGS-VPFILPIPGADKKGV-------TAFR 130
Cdd:COG0493 171 KDVLDREIELIEALGVEFRTN-VEVGKD------ITLDELLEEFDAVFLATGAgKPRDLGIPGEDLKGVhsamdflTAVN 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 131 DIKDTDTMLAASKqykKAAVIGGGLLGLEAARGLLNLG-MDVSVIHL-----APFLMERQLDAtagrllqnelEKQGMTF 204
Cdd:COG0493 244 LGEAPDTILAVGK---RVVVIGGGNTAMDCARTALRLGaESVTIVYRrtreeMPASKEEVEEA----------LEEGVEF 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 205 LLEKQTEEIVGDD--RVEGLRF------------------KDGTS--IEADLVVMAVGIRPNTT-LGAESGIPVN-RGII 260
Cdd:COG0493 311 LFLVAPVEIIGDEngRVTGLECvrmelgepdesgrrrpvpIEGSEftLPADLVILAIGQTPDPSgLEEELGLELDkRGTI 390
|
250 260
....*....|....*....|....*
gi 1835700157 261 VND--YMQTEIPHIYAVGECaeHRG 283
Cdd:COG0493 391 VVDeeTYQTSLPGVFAGGDA--VRG 413
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
552-753 |
7.25e-18 |
|
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: 87.48 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 552 HANIQkDGTYSVVPRMYGGVTNSTDLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWEDLDmPSGYA--YGKTL 629
Cdd:COG0155 298 HEQKQ-DGLYYVGLSVENGRITDEQLRALADLAERYGSGEIRLTPNQNLILADVPEEDLPALEAALR-ALGLAtpPSGLR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 630 RTVKTCVGEQFCRFGTQDSMALGIALEKKFE----GLNTPHKVKMAVSACPRNCAESGIKDLGVVGIDG-----GWELYV 700
Cdd:COG0155 376 RDSIACPGLPTCKLAIAESKRLAPALADRLEedldGLHDDEPIRIRISGCPNSCGRHYIADIGLVGKAKkgvveAYQLYL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1835700157 701 GGNGGTHLRAGDLLMKVKTNEEVLEYAGAYLQYYRETANYLERTSAWLERVGL 753
Cdd:COG0155 456 GGGLGGDARLGRKYGPKVPADEIPDALERLLEAYLAEREEGESFGDFVRRVGI 508
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
73-276 |
7.30e-16 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 80.77 E-value: 7.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 73 NIQLYTNETVI----KVDTENKTVITdADRIqpydelILATGSVPFILPIPGADkkGVtafrDIKDTDTMLAASKQYKKA 148
Cdd:PRK07846 103 NIDVYRGHARFigpkTLRTGDGEEIT-ADQV------VIAAGSRPVIPPVIADS--GV----RYHTSDTIMRLPELPESL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 149 AVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMeRQLDATAGRLLqNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGT 228
Cdd:PRK07846 170 VIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLL-RHLDDDISERF-TELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGS 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 229 SIEADLVVMAVGIRPNT-TLGAES-GIPVNRG--IIVNDYMQTEIPHIYAVG 276
Cdd:PRK07846 248 TVEADVLLVATGRVPNGdLLDAAAaGVDVDEDgrVVVDEYQRTSAEGVFALG 299
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
40-278 |
1.19e-15 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 80.97 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 40 HPNYNRILLS----KVLQGDTDIKDI-TLndwdwyeenniqlytneTVIKVDtenktvitDADRIQPYDELILATGSVPF 114
Cdd:PRK13748 191 HAKYEGILDGnpaiTVLHGEARFKDDqTL-----------------IVRLND--------GGERVVAFDRCLIATGASPA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 115 ILPIPGadkkgvtafrdIKDT-----DTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVihLAP---FLMErqlD 186
Cdd:PRK13748 246 VPPIPG-----------LKETpywtsTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTI--LARstlFFRE---D 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 187 ATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTsIEADLVVMAVGIRPNT-TLGAES-GIPVN-RG-IIVN 262
Cdd:PRK13748 310 PAIGEAVTAAFRAEGIEVLEHTQASQVAHVDGEFVLTTGHGE-LRADKLLVATGRAPNTrSLALDAaGVTVNaQGaIVID 388
|
250
....*....|....*.
gi 1835700157 263 DYMQTEIPHIYAVGEC 278
Cdd:PRK13748 389 QGMRTSVPHIYAAGDC 404
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
556-617 |
6.00e-15 |
|
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: 69.86 E-value: 6.00e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 556 QKDGTYSVVPRMYGGVTNSTDLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWEDL 617
Cdd:pfam03460 3 QKDGDYMVRVRVPGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELLEEL 64
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
97-276 |
7.11e-14 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 73.87 E-value: 7.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 97 DRIQPYDELILATGS-VPFILPIPGADKKGVTA-----FRdIKdtdtmlAASKQY-----------KKAAVIGGGLLGLE 159
Cdd:PRK12770 114 ELVKKYDAVLIATGTwKSRKLGIPGEDLPGVYSaleylFR-IR------AAKLGYlpwekvppvegKKVVVVGAGLTAVD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 160 AARGLLNLGMDVSVIhlapfLMERQL-DATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRF-------KDGTS-- 229
Cdd:PRK12770 187 AALEAVLLGAEKVYL-----AYRRTInEAPAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVELakmrlgePDESGrp 261
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835700157 230 -----------IEADLVVMAVGIRPNTTLGAES-GIPVNRG--IIVNDYMQTEIPHIYAVG 276
Cdd:PRK12770 262 rpvpipgsefvLEADTVVFAIGEIPTPPFAKEClGIELNRKgeIVVDEKHMTSREGVFAAG 322
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
59-285 |
1.33e-13 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 73.67 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 59 KDITLNDWDWYEENNIQLYTNETVIKVdtenktvITDADRIQPYDELILATG--SVPFiLPIPGADKKGVTAFRD-IKDT 135
Cdd:PRK11749 190 KDIVDREVERLLKLGVEIRTNTEVGRD-------ITLDELRAGYDAVFIGTGagLPRF-LGIPGENLGGVYSAVDfLTRV 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 136 DTMLAASKQY--KKAAVIGGGLLGLEAARGLLNLG-MDVSVIHlapflmERQLDATAGRllQNELE---KQGMTFLLEKQ 209
Cdd:PRK11749 262 NQAVADYDLPvgKRVVVIGGGNTAMDAARTAKRLGaESVTIVY------RRGREEMPAS--EEEVEhakEEGVEFEWLAA 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 210 TEEIVGDD-RVEGLRF---------KDGTS----------IEADLVVMAVGIRPNT-TLGAESGIPVNR--GIIVND-YM 265
Cdd:PRK11749 334 PVEILGDEgRVTGVEFvrmelgepdASGRRrvpiegseftLPADLVIKAIGQTPNPlILSTTPGLELNRwgTIIADDeTG 413
|
250 260
....*....|....*....|
gi 1835700157 266 QTEIPHIYAVGECAehRGIA 285
Cdd:PRK11749 414 RTSLPGVFAGGDIV--TGAA 431
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
569-736 |
1.87e-13 |
|
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: 73.61 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 569 GGVTNSTDLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWEDL---DMPSGYAYGKTLRTVKTCVGEQFCRFGT 645
Cdd:COG0155 63 GGVLTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELaevGLTTIGACGDVVRNVTASPLAGVDPDEL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 646 QDSMALGIALEKKF----EGLNTPHKVKMAVSACPRNCAESGIKDLGVVGI---DG--GWELYVGGN-GGTHlRAGDLLM 715
Cdd:COG0155 143 FDVRPYAEAISQHLlghpEYTYLPRKFKIAFSGPPEDDADVEINDLGFIAVvkeDGlvGFNVLVGGGlGRTP-RLADVLG 221
|
170 180
....*....|....*....|.
gi 1835700157 716 KVKTNEEVLEYAGAYLQYYRE 736
Cdd:COG0155 222 EFVPPEDLLDVAEAVVRVFRD 242
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
95-349 |
2.06e-13 |
|
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: 73.35 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 95 DADRIQPYDEL-----------ILATGSVPFILPIPGADKKGVTafrdikdTDTMLAASKQYKKAAVIGGGLLGLEAARG 163
Cdd:TIGR01438 126 DKHRIKATNKKgkekiysaerfLIATGERPRYPGIPGAKELCIT-------SDDLFSLPYCPGKTLVVGASYVALECAGF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 164 LLNLGMDVSVIHLAPFLmeRQLDATAGRLLQNELEKQGMTF---LLEKQTEEIVGDDRVEGLRFKDGTSIEADLVVMAVG 240
Cdd:TIGR01438 199 LAGIGLDVTVMVRSILL--RGFDQDCANKVGEHMEEHGVKFkrqFVPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLLAIG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 241 IRPNT-TLGAES-GIPVNRG---IIVNDYMQTEIPHIYAVGECAEHRgiayGLVAPLYEQA-KVLAKHMcgietkpYEGS 314
Cdd:TIGR01438 277 RDACTrKLNLENvGVKINKKtgkIPADEEEQTNVPYIYAVGDILEDK----PELTPVAIQAgRLLAQRL-------FKGS 345
|
250 260 270
....*....|....*....|....*....|....*...
gi 1835700157 315 VLSTQLKVSGVEVFSA---GDFNESEEkKAIKVFDEQD 349
Cdd:TIGR01438 346 TVICDYENVPTTVFTPleyGACGLSEE-KAVEKFGEEN 382
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
416-466 |
3.30e-13 |
|
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: 64.47 E-value: 3.30e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1835700157 416 IICGCNGVSKGAIIQAIQEkGCSSTDEIKACTGASRSCGGCKPLVEEILQH 466
Cdd:pfam04324 1 IVCRCFGVTDGEIRDAIRE-GLTTVEEVKRRTKAGTGCGSCRPAIEEILAE 50
|
|
| Bfd |
COG2906 |
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism]; |
416-469 |
2.64e-12 |
|
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
Pssm-ID: 442150 [Multi-domain] Cd Length: 54 Bit Score: 62.14 E-value: 2.64e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1835700157 416 IICGCNGVSKGAIIQAIQEkGCSSTDEIKACTGASRSCGGCKPLVEEILQHTLG 469
Cdd:COG2906 2 YVCLCNGVTDRQIRAAIAE-GATSLEELRAALGAGTQCGSCVPEARELLAEALA 54
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
77-312 |
7.71e-12 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 68.25 E-value: 7.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 77 YTNETVIKVDTENKTVI----------TDADRIQPYDELILATGSVPFILPIPGADK-----KGVTAFRDIKD------- 134
Cdd:PTZ00318 79 YLRAVVYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGARPNTFNIPGVEErafflKEVNHARGIRKrivqcie 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 135 ----TDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDvSVIHLAPFLMER--------------QLDATAGRLLQNE 196
Cdd:PTZ00318 159 raslPTTSVEERKRLLHFVVVGGGPTGVEFAAELADFFRD-DVRNLNPELVEEckvtvleagsevlgSFDQALRKYGQRR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 197 LEKQGMTFLLEKQTEEIVGDDRVeglrFKDGTSIEADLVVMAVGIRPNTTLGAESGIPVNRG-IIVNDYMQT-EIPHIYA 274
Cdd:PTZ00318 238 LRRLGVDIRTKTAVKEVLDKEVV----LKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGrISVDDHLRVkPIPNVFA 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1835700157 275 VGECAEHRGIAYGLVAPLYE-QAKVLAKHMCGI-----ETKPYE 312
Cdd:PTZ00318 314 LGDCAANEERPLPTLAQVASqQGVYLAKEFNNElkgkpMSKPFV 357
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
105-277 |
1.54e-11 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 67.59 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 105 LILATGSVPFILPIPGADKkgvtafrdIKDTDTMLAASKQYKKAAVIGGGLLGLEAArGLLN-LGMDVSV-IHLAPFLme 182
Cdd:PLN02546 220 ILIAVGGRPFIPDIPGIEH--------AIDSDAALDLPSKPEKIAIVGGGYIALEFA-GIFNgLKSDVHVfIRQKKVL-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 183 RQLDATAGRLLQNELEKQGMTFLLEKQTEEIV-GDDRVEGLRFKDGTSIEADLVVMAVGIRPNT-TLGAES-GIPVNR-- 257
Cdd:PLN02546 289 RGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIkSADGSLSLKTNKGTVEGFSHVMFATGRKPNTkNLGLEEvGVKMDKng 368
|
170 180
....*....|....*....|
gi 1835700157 258 GIIVNDYMQTEIPHIYAVGE 277
Cdd:PLN02546 369 AIEVDEYSRTSVPSIWAVGD 388
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
146-278 |
1.77e-11 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 67.49 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 146 KKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLmerqldaTAGRLLQNELEKQG-MTFLLEKQTEEIVGD-DRVEGLR 223
Cdd:PRK15317 352 KRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPEL-------KADQVLQDKLRSLPnVTIITNAQTTEVTGDgDKVTGLT 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 224 FKDGTS-----IEADLVVMAVGIRPNTTLGAESgIPVN-RG-IIVNDYMQTEIPHIYAVGEC 278
Cdd:PRK15317 425 YKDRTTgeehhLELEGVFVQIGLVPNTEWLKGT-VELNrRGeIIVDARGATSVPGVFAAGDC 485
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
1-277 |
2.13e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 66.97 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 1 MGKKQLVlVGNGMAGVRAIEEIlsvAKDEFQITIFGA--EPH-------PNYnRILLSKVLqgDTDIKDItlndwdwyEE 71
Cdd:PRK12831 139 KGKKVAV-IGSGPAGLTCAGDL---AKMGYDVTIFEAlhEPGgvlvygiPEF-RLPKETVV--KKEIENI--------KK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 72 NNIQLYTNETVikvdteNKTV-ITDADRIQPYDELILATGS-VPFILPIPGADKKGV-------------TAFRDikDTD 136
Cdd:PRK12831 204 LGVKIETNVVV------GKTVtIDELLEEEGFDAVFIGSGAgLPKFMGIPGENLNGVfsanefltrvnlmKAYKP--EYD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 137 TMLAASKqykKAAVIGGGLLGLEAARGLLNLGMDVsviHLAPFLMERQLDATAGRLlqNELEKQGMTFLLEKQTEEIVGD 216
Cdd:PRK12831 276 TPIKVGK---KVAVVGGGNVAMDAARTALRLGAEV---HIVYRRSEEELPARVEEV--HHAKEEGVIFDLLTNPVEILGD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 217 D--RVEGLRF-------KDGTS-------------IEADLVVMAVGIRPNTTL-GAESGIPVN-RGIIVND--YMQTEIP 270
Cdd:PRK12831 348 EngWVKGMKCikmelgePDASGrrrpveiegsefvLEVDTVIMSLGTSPNPLIsSTTKGLKINkRGCIVADeeTGLTSKE 427
|
....*..
gi 1835700157 271 HIYAVGE 277
Cdd:PRK12831 428 GVFAGGD 434
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
4-297 |
3.18e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 66.71 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 4 KQLVLVGNGMAGVRAIeeiLSVAKDEFQITIFGAEPHP----NYNriLLSKVLQGDTDIKDItlndwDWYEENNIQLYTN 79
Cdd:PRK13984 284 KKVAIVGSGPAGLSAA---YFLATMGYEVTVYESLSKPggvmRYG--IPSYRLPDEALDKDI-----AFIEALGVKIHLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 80 ETVIKvDtenktvITDADRIQPYDELILATGsvpFIL----PIPGADKKgvtafrDIKDTDTMLAASKQY---------- 145
Cdd:PRK13984 354 TRVGK-D------IPLEELREKHDAVFLSTG---FTLgrstRIPGTDHP------DVIQALPLLREIRDYlrgegpkpki 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 146 -KKAAVIGGGLLGLEAARGLLNLGM------DVSVIHLapflmERQLDATAGRLLQ-NELEKQGMTFLLEKQTEEI-VGD 216
Cdd:PRK13984 418 pRSLVVIGGGNVAMDIARSMARLQKmeygevNVKVTSL-----ERTFEEMPADMEEiEEGLEEGVVIYPGWGPMEVvIEN 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 217 DRVEGLRFKDGTSI-------------------EADLVVMAVGIRPNTTLGAE---SGIPVNRG-IIVNDYMQTEIPHIY 273
Cdd:PRK13984 493 DKVKGVKFKKCVEVfdeegrfnpkfdesdqiivEADMVVEAIGQAPDYSYLPEelkSKLEFVRGrILTNEYGQTSIPWLF 572
|
330 340
....*....|....*....|....
gi 1835700157 274 AVGECAEHRGIAYGlVAPLYEQAK 297
Cdd:PRK13984 573 AGGDIVHGPDIIHG-VADGYWAAE 595
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
83-278 |
5.84e-11 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 65.65 E-value: 5.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 83 IKVDTENKTVIT-DADRIqpydelILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLaaskqyKKAAVIGGGLLGLEAA 161
Cdd:PRK07845 126 VKVTTADGGEETlDADVV------LIATGASPRILPTAEPDGERILTWRQLYDLDELP------EHLIVVGSGVTGAEFA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 162 RGLLNLGMDVSVIHLApflmERQL---DATAGRLLQNELEKQGMTfLLEKQTEEIV--GDDRVEgLRFKDGTSIEADLVV 236
Cdd:PRK07845 194 SAYTELGVKVTLVSSR----DRVLpgeDADAAEVLEEVFARRGMT-VLKRSRAESVerTGDGVV-VTLTDGRTVEGSHAL 267
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1835700157 237 MAVGIRPNTT-LG-AESGIPVNRG--IIVNDYMQTEIPHIYAVGEC 278
Cdd:PRK07845 268 MAVGSVPNTAgLGlEEAGVELTPSghITVDRVSRTSVPGIYAAGDC 313
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
105-282 |
7.01e-11 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 65.62 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 105 LILATGSVPFILP-IPGADKKGVTafrdikdTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLmeR 183
Cdd:PTZ00052 148 ILIATGGRPSIPEdVPGAKEYSIT-------SDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPL--R 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 184 QLDATAGRLLQNELEKQGMTFL---LEKQTEEIvgDDRVEGLrFKDGTSIEADLVVMAVGIRPNTT-LGAES-GIPVNRG 258
Cdd:PTZ00052 219 GFDRQCSEKVVEYMKEQGTLFLegvVPINIEKM--DDKIKVL-FSDGTTELFDTVLYATGRKPDIKgLNLNAiGVHVNKS 295
|
170 180
....*....|....*....|....*..
gi 1835700157 259 ---IIVNDymQTEIPHIYAVGECAEHR 282
Cdd:PTZ00052 296 nkiIAPND--CTNIPNIFAVGDVVEGR 320
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
95-277 |
2.32e-10 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 63.49 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 95 DADRIQPYDELILATGSVPFILPIPGadkkgVTAFRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVI 174
Cdd:PRK08010 113 EGNLEIHGEKIFINTGAQTVVPPIPG-----ITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTIL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 175 HLAPFLMERQlDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGtSIEADLVVMAVGIRPNT-TLGAE-SG 252
Cdd:PRK08010 188 EAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHA-QLAVDALLIASGRQPATaSLHPEnAG 265
|
170 180
....*....|....*....|....*..
gi 1835700157 253 IPVNR--GIIVNDYMQTEIPHIYAVGE 277
Cdd:PRK08010 266 IAVNErgAIVVDKYLHTTADNIWAMGD 292
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
73-276 |
2.79e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 62.24 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 73 NIQLYTNETVIKVDTENKTVITDADRIQ-PYdeLILATG--SVPFILPIPGADKKG--VTAFRDIKDTDTMlaaskqykk 147
Cdd:pfam13738 91 PINLFEEVTSVKKEDDGFVVTTSKGTYQaRY--VIIATGefDFPNKLGVPELPKHYsyVKDFHPYAGQKVV--------- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 148 aaVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMERQLDA-------TAGRLlqNELEKQG-MTFLLEKQTEEIVGDDRV 219
Cdd:pfam13738 160 --VIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPsyslspdTLNRL--EELVKNGkIKAHFNAEVKEITEVDVS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835700157 220 EGLRFKDGTSIEA-DLVVMAVGIRPNTTLGAESGIPVNR-GIIV--NDYMQTEIPHIYAVG 276
Cdd:pfam13738 236 YKVHTEDGRKVTSnDDPILATGYHPDLSFLKKGLFELDEdGRPVltEETESTNVPGLFLAG 296
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
143-278 |
3.42e-10 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 63.48 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 143 KQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMeRQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGL 222
Cdd:PTZ00058 235 KEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL-RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLT 313
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835700157 223 RF--KDGTSIEADLVVMAVGIRPNT-TLGAES-GIPVNRG-IIVNDYMQTEIPHIYAVGEC 278
Cdd:PTZ00058 314 IYlsDGRKYEHFDYVIYCVGRSPNTeDLNLKAlNIKTPKGyIKVDDNQRTSVKHIYAVGDC 374
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
2-290 |
4.37e-10 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 62.97 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 2 GKKQLVlVGNGMAGvraieeiLSVA----KDEFQITIFGAEPH---------PNYnRiLLSKVLqgDTDIKDItlndwdw 68
Cdd:PRK12771 137 GKRVAV-IGGGPAG-------LSAAyhlrRMGHAVTIFEAGPKlggmmrygiPAY-R-LPREVL--DAEIQRI------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 69 yEENNIQLYTNETVikvdtenKTVITDADRIQPYDELILATG-SVPFILPIPGADKKGVT---AF-RDI-KDTDTMLAas 142
Cdd:PRK12771 198 -LDLGVEVRLGVRV-------GEDITLEQLEGEFDAVFVAIGaQLGKRLPIPGEDAAGVLdavDFlRAVgEGEPPFLG-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 143 kqyKKAAVIGGGLLGLEAARGLLNLGM-DVSVIHLAPflMErqlDATAgrlLQNELE---KQGMTFLLEKQTEEIVGDDR 218
Cdd:PRK12771 268 ---KRVVVIGGGNTAMDAARTARRLGAeEVTIVYRRT--RE---DMPA---HDEEIEealREGVEINWLRTPVEIEGDEN 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 219 -VEGLRF---------KDGTS---------IEADLVVMAVGIRPNTT-LGAESGIPVNRGIIVND--YMQTEIPHIYAVG 276
Cdd:PRK12771 337 gATGLRVitvekmeldEDGRPspvtgeeetLEADLVVLAIGQDIDSAgLESVPGVEVGRGVVQVDpnFMMTGRPGVFAGG 416
|
330
....*....|....*....
gi 1835700157 277 EC--AEH---RGIAYGLVA 290
Cdd:PRK12771 417 DMvpGPRtvtTAIGHGKKA 435
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
90-277 |
8.43e-10 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 62.45 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 90 KTVITDADRIQPYDELILATGS-VPFILPIPGADKKGVTAFRD-IKDTDTMLAASKQY-------KKAAVIGGGLLGLEA 160
Cdd:PRK12778 506 KTITIEELEEEGFKGIFIASGAgLPNFMNIPGENSNGVMSSNEyLTRVNLMDAASPDSdtpikfgKKVAVVGGGNTAMDS 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 161 ARGLLNLGMDVSVIhlapfLMERQLDATAGRLLQNELEKQ-GMTFLLEKQTEEIVGDD--RVEGLRFK-------DGT-- 228
Cdd:PRK12778 586 ARTAKRLGAERVTI-----VYRRSEEEMPARLEEVKHAKEeGIEFLTLHNPIEYLADEkgWVKQVVLQkmelgepDASgr 660
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835700157 229 -----------SIEADLVVMAVGIRPNTTL-GAESGIPVNR--GIIVNDYMQTEIPHIYAVGE 277
Cdd:PRK12778 661 rrpvaipgstfTVDVDLVIVSVGVSPNPLVpSSIPGLELNRkgTIVVDEEMQSSIPGIYAGGD 723
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
481-530 |
8.12e-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: 52.15 E-value: 8.12e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1835700157 481 ICGCTTLSRDEVVEEIKAkGLSHTREVMNvlGWKTPEGCSKCRPALNYYL 530
Cdd:pfam04324 2 VCRCFGVTDGEIRDAIRE-GLTTVEEVKR--RTKAGTGCGSCRPAIEEIL 48
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
97-277 |
9.79e-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: 58.45 E-value: 9.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 97 DRIQPyDELILATGSVPFILPIPGADKkgvtafrdIKDTDTMLAASKQYKKAAVIGGGLLGLEAArGLLN----LGMDVS 172
Cdd:TIGR01423 148 ERLQA-EHILLATGSWPQMLGIPGIEH--------CISSNEAFYLDEPPRRVLTVGGGFISVEFA-GIFNaykpRGGKVT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 173 VIHLAPFLMeRQLDATAGRLLQNELEKQGMTFLLEKQTEEI-VGDDRVEGLRFKDGTSIEADLVVMAVGIRPNT------ 245
Cdd:TIGR01423 218 LCYRNNMIL-RGFDSTLRKELTKQLRANGINIMTNENPAKVtLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTqtlqld 296
|
170 180 190
....*....|....*....|....*....|..
gi 1835700157 246 TLGAEsgIPVNRGIIVNDYMQTEIPHIYAVGE 277
Cdd:TIGR01423 297 KVGVE--LTKKGAIQVDEFSRTNVPNIYAIGD 326
|
|
| Fer2_BFD-like |
cd19942 |
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ... |
417-461 |
1.11e-08 |
|
[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: 51.67 E-value: 1.11e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1835700157 417 ICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVE 461
Cdd:cd19942 3 VCECFAVTEKELREAIRKGGLKTVEELLTGTGAGGGCGVCHPHVA 47
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
84-281 |
4.46e-08 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 55.84 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 84 KVDTENKTVITDADRIQ-PYDELILATGSVPFILPIPGADK-KGvtafRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAA 161
Cdd:PRK10262 87 KVDLQNRPFRLTGDSGEyTCDALIIATGASARYLGLPSEEAfKG----RGVSACATCDGFFYRNQKVAVIGGGNTAVEEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 162 RGLLNLGMDVSVIHLAP-FLMERQLDatagRLLQNELEKQGMTFLLEKQTEEIVGDDR-VEGLRFKDGT------SIEAD 233
Cdd:PRK10262 163 LYLSNIASEVHLIHRRDgFRAEKILI----KRLMDKVENGNIILHTNRTLEEVTGDQMgVTGVRLRDTQnsdnieSLDVA 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1835700157 234 LVVMAVGIRPNTT-----LGAESG-IPVNRGIIVNdYMQTEIPHIYAVGECAEH 281
Cdd:PRK10262 239 GLFVAIGHSPNTAifegqLELENGyIKVQSGIHGN-ATQTSIPGVFAAGDVMDH 291
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
105-277 |
4.41e-07 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 53.28 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 105 LILATGSVPFILPIPGADKkGVTafrdikdTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPfLMERQ 184
Cdd:PLN02507 171 ILIATGSRAQRPNIPGKEL-AIT-------SDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKE-LPLRG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 185 LDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTSIEADLVVMAVGIRPNTT-LGAES-GIPVNR--GII 260
Cdd:PLN02507 242 FDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTKrLNLEAvGVELDKagAVK 321
|
170
....*....|....*..
gi 1835700157 261 VNDYMQTEIPHIYAVGE 277
Cdd:PLN02507 322 VDEYSRTNIPSIWAIGD 338
|
|
| Fer2_BFD |
cd19945 |
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ... |
417-468 |
6.44e-07 |
|
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: 46.81 E-value: 6.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 417 ICGCNGVSKGAIIQAIQEkGCSSTDEIKACTGASRSCGGCKPLVEEILQHTL 468
Cdd:cd19945 3 VCLCNGITDKQIRQAVAQ-GATSLRELREQLGVGSQCGKCARMARQVLEEEL 53
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
570-716 |
1.15e-06 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 51.93 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 570 GVTNSTDLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWED-------LDmPSGYAygktlRTVKTCVGEQFCR 642
Cdd:PRK09566 331 GRLYAEDMFELARLAEVYGSGEIRLTVEQNVIIPNIPDENLETFLAEpllqkfsLE-PGPLA-----RGLVSCTGNQYCN 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 643 FG---TQD-SMALGIALEKKfegLNTPHKVKMAVSACPRNCAESGIKDLGVVGI----DG----GWELYVGGNGGTHLRA 710
Cdd:PRK09566 405 FAlieTKNrALALAKELDAE---LDLPQPVRIHWTGCPNSCGQPQVADIGLMGTkarkNGktveGVDIYMGGKVGKDAKL 481
|
....*.
gi 1835700157 711 GDLLMK 716
Cdd:PRK09566 482 GECVQK 487
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
576-708 |
2.16e-06 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 51.32 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 576 DLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVwedLDMPSGYAY----GKTLRTVKTCVGEQFCRFGTQDSMAL 651
Cdd:PLN02431 411 DMDELARLADEYGSGELRLTVEQNIIIPNVPNSKVEAL---LAEPLLQRFspnpGLLLKGLVACTGNQFCGQAIIETKAR 487
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835700157 652 GIALEKKFEGL-NTPHKVKMAVSACPRNCAESGIKDLGVVGI-----DG----GWELYVGGNGG--THL 708
Cdd:PLN02431 488 ALKVTEELERLvEVPRPVRMHWTGCPNSCGQVQVADIGFMGCmardeNGkaveGADIFVGGRVGsdSHL 556
|
|
| NasA-like_Fer2_BFD-like |
cd19948 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ... |
414-464 |
2.43e-06 |
|
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: 45.21 E-value: 2.43e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1835700157 414 DEIICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVEEIL 464
Cdd:cd19948 1 GRTVCACFSVGENTIRRAIADNGLTSVAQVGTCLKAGTNCGSCVPEIQKLL 51
|
|
| NifU_Fer2_BFD-like |
cd19947 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation ... |
413-464 |
4.32e-06 |
|
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: 44.58 E-value: 4.32e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 413 DDEIICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVEEIL 464
Cdd:cd19947 1 EGAIVCKCFGVTEVMIERAIRENNLTTVEDVTNYTKAGGGCGSCHEKIEDIL 52
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
105-277 |
4.57e-06 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 50.30 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 105 LILATGSVPFILPIPGADKKGVTAfrdiKDTDTMLAASKQYkkAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMErQ 184
Cdd:PTZ00153 278 IIIATGSTPNIPDNIEVDQKSVFT----SDTAVKLEGLQNY--MGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLP-L 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 185 LDATAGRLLQNELEK-QGMTFLLEKQTEEI-----------------VGDDRVEGLRFKDGTSIEADLVVMAVGIRPNTT 246
Cdd:PTZ00153 351 LDADVAKYFERVFLKsKPVRVHLNTLIEYVragkgnqpviighserqTGESDGPKKNMNDIKETYVDSCLVATGRKPNTN 430
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1835700157 247 -LGAES-GIPVNRGII-VNDYMQTE------IPHIYAVGE 277
Cdd:PTZ00153 431 nLGLDKlKIQMKRGFVsVDEHLRVLredqevYDNIFCIGD 470
|
|
| CopZ-like_Fer2_BFD-like |
cd10141 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus ... |
417-457 |
3.23e-05 |
|
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: 42.21 E-value: 3.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1835700157 417 ICGCNGVSKGAIIQAIQEKGCSSTDEIKAcTGASRSCgGCK 457
Cdd:cd10141 4 VCYCFGVTEEDIIEAVAETGATTVEEIRA-TGKAGRC-ACE 42
|
|
| nirA |
PRK09567 |
NirA family protein; |
574-702 |
1.80e-04 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 45.01 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 574 STD-LRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWEDLDmPSGYAYGKT-LRT-VKTCVGEQFCRFGTQDSMA 650
Cdd:PRK09567 387 TTDqMRGLAKIAARYGDGEIRLTVWQNLLISGVPDADVAAVEAAIE-ALGLTTEASsIRAgLVACTGNAGCKFAAADTKG 465
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835700157 651 LGIALEKKFEG---LNTPhkVKMAVSACPRNCAESGIKDLGVVG----IDG-----GWELYVGG 702
Cdd:PRK09567 466 HALAIADYCEPrvaLDQP--VNIHLTGCHHSCAQHYIGDIGLIGakvaVSEgdtveGYHIVVGG 527
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
146-255 |
2.29e-04 |
|
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: 44.30 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835700157 146 KKAAVIGGGLLGLEAARGLLNLGMDVSVIhlapflmerqlDA-TAGRLLQNELEKQGMTFLLekqteeivGDDRVEGLRf 224
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVS-----------DDrPAPELAAAELEAPGVEVVL--------GEHPEELLD- 64
|
90 100 110
....*....|....*....|....*....|....
gi 1835700157 225 kdgtsiEADLVVMAVGIRPNTTLGA---ESGIPV 255
Cdd:COG0771 65 ------GADLVVKSPGIPPDHPLLKaarAAGIPV 92
|
|
| HyaA_family_Fer2_BFD-like |
cd19951 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of uncharacterized ... |
416-467 |
2.38e-04 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of uncharacterized proteins having a C-terminal Ni,Fe-hydrogenase I small subunit (HyaA) family domain; 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: 381084 [Multi-domain] Cd Length: 54 Bit Score: 39.40 E-value: 2.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1835700157 416 IICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVEEILQHT 467
Cdd:cd19951 3 LVCSCEHVYYQDLIDIIVSCAITSFAELKEFSEAGRVCGRCKKDVDDIIAAS 54
|
|
| GlpA-like_Fer2_BFD-like |
cd19946 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ... |
415-466 |
4.21e-04 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, and similar proteins; This subgroup includes the BFD-like [2Fe-2S]-binding domains of subunits of various component dehydrogenase/oxidases, including anaerobic glycerol 3-phosphate dehydrogenase subunit A of GlpABC, hydrogen cyanide synthase subunit HcnB of HcnABC, octopine oxidase subunit A of OoxAB, and nopaline oxidase subunit A of NoxAB. GlpABC catalyzes the conversion of glycerol 3-phosphate to dihydroxyacetone, and participates in the glycerol degradation by glycerol kinase pathway in step 1 of the sub-pathway that synthesizes glycerone phosphate from sn-glycerol 3-phosphate (anaerobic route). HcnABC oxidizes glycine producing hydrogen cyanide and CO2. In Agrobacterium spp, the first enzymic step in the catabolic utilization of octopine and nopaline is the oxidative cleavage into L-arginine and pyruvate or 2-ketoglutarate, respectively; nopaline oxidase (NoxAB) accepts nopaline and octopine while octopine oxidase (OoaB) has high activity with octopine but barely detectable activity with nopaline, both subunits possibly contributing to the substrate specificity. 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: 381079 [Multi-domain] Cd Length: 55 Bit Score: 39.06 E-value: 4.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835700157 415 EIICGCNGVSKGAIIQAIQEKGCSSTDEIKACT--GASRsCGG--CKPLVEEILQH 466
Cdd:cd19946 1 TIVCRCEEVTEGEIRDAIRRGAARDLDGLKRRTraGMGR-CQGrfCAPRVAELLAR 55
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