|
Name |
Accession |
Description |
Interval |
E-value |
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
6-783 |
0e+00 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 910.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 6 LVMIGNGMAGIRTIEEILERANDLYDITVIGKEPYPNYNRIMLSNILQNKMTVEETIMNPYEWYEEHDIKLITNDPVVDV 85
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMFEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 86 DRTNQNVTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECARGLL 165
Cdd:TIGR02374 81 DTDQKQVITDAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 166 DQGMEVTVLHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPADLVVMAVGIRPYT 245
Cdd:TIGR02374 161 NLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPND 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 246 EVAKESGLDVNRGIVVNDVMQTSDSNVFAVGECAEHNGKVYGLVAPLYEQGKVLADHLTNKETNGYKGSTTFTSLKVSGC 325
Cdd:TIGR02374 241 ELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECEEYEGSDLSAKLKLLGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 326 DLYSAGQIVENAEIKGIEIFNSVDNNYKKIFLKDGNVVGAVLYGDIDDGSRFYNMM-KKGESTEDYTLVSLLTKGGEEAS 404
Cdd:TIGR02374 321 DVWSAGDAQETERTTSIKIYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVlKQADISEDPAIIKPQISGPEAGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 405 LSIADMADDETICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGNSCGKCKPQIAQILQHTLGDDFVAAKPAgICGCTD 484
Cdd:TIGR02374 401 PGVEAMPDSEQICSCNTVTKGAIIDAIHTGSCTTVEELKACTKAGTSCGGCKPLVEQLLRAELNSQYTASTPA-LCECTD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 485 LTRDQIVTQIRAKGLKTSKEVRHVLNFKNKGGCPKCRPAINYYLNMVYPHDHEDERESRFANERYHANIQNDGTFSVIPQ 564
Cdd:TIGR02374 480 FSRDELFEEIQARGFTTFAEVMNQLGWKTKNGCSTCKPAVQYYLAMLYPGFILDEEATSLSNDHFLANIQKDGTYSVIPR 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 565 MRGGVTDADQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIWQDLGMRSAS-AYGKKTRSVKSCVGKEFCRFGT 643
Cdd:TIGR02374 560 MYGGRTNPEQLRTIANIAEAYSIPYVKITGGQRLDLFGAKKDDLPNIWKDLKMPGYEhAYGKALRTVKTCVGSQWCRYGN 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 644 QYTTRLGIRLEKTFEYIDTPHKFKMGVSGCPRSCVESGVKDFGVISVENGFQIYIGGNGGTEVEKAEFLTTVETEDEVIK 723
Cdd:TIGR02374 640 QDSVQLAIQLERRYEGLRTPHKIKIGVSGCERECAEAAGKDVGVIATEKGWNLYVGGNGGTHPRHGDLLAVDEDEETLIG 719
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 724 LCGALMQYYRETGIYAERTAPWLRRLGFENVKEVLLDPERQNELFERiMDAKKAVEAEPW 783
Cdd:TIGR02374 720 YIDRFLQYYRETADYLERTAPWLERLGIDHVREVLFEDDLRAELEES-MQRDLSLIKCPW 778
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
3-392 |
4.53e-173 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 503.91 E-value: 4.53e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 3 KQKLVMIGNGMAGIRTIEEILERANDlYDITVIGKEPYPNYNRIMLSNILQNKMTVEETIMNPYEWYEEHDIKLITNDPV 82
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPD-GEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 83 VDVDRTNQNVTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECAR 162
Cdd:COG1251 80 TAIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 163 GLLDQGMEVTVLHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPADLVVMAVGIR 242
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 243 PYTEVAKESGLDVNRGIVVNDVMQTSDSNVFAVGECAEHNGKVYG-----LVAPLYEQGKVLADHLTNKETnGYKGSTTF 317
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGrrvleLVAPAYEQARVAAANLAGGPA-AYEGSVPS 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613310046 318 TSLKVSGCDLYSAGQIVENAEIkgIEIFNSVDNNYKKIFLKDGNVVGAVLYGDIDDGSRFYNMMKKGESTEDYTL 392
Cdd:COG1251 319 TKLKVFGVDVASAGDAEGDEEV--VVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRAL 391
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
1-796 |
5.19e-172 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 517.36 E-value: 5.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 1 MAKQKLVMIGNGMAGIRTIEEILERA-NDLYDITVIGKEPYPNYNRIMLSNILQNKmTVEETIMNPYEWYEEHDIKLITN 79
Cdd:PRK14989 1 MSKVRLAIIGNGMVGHRFIEDLLDKAdAANFDITVFCEEPRIAYDRVHLSSYFSHH-TAEELSLVREGFYEKHGIKVLVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 80 DPVVDVDRTNQNVTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMMNIAKTKKKAIVIGGGLLGLE 159
Cdd:PRK14989 80 ERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 160 CARGLLDQGMEVTVLHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEIL--GEDDVEGVKLADGREIPADLVVM 237
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVqeGVEARKTMRFADGSELEVDFIVF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 238 AVGIRPYTEVAKESGLDVNR--GIVVNDVMQTSDSNVFAVGECAEHNGKVYGLVAPLYEQGKVLADHLTNKEtNGYKGST 315
Cdd:PRK14989 240 STGIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSE-NAFEGAD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 316 TFTSLKVSGCDLYSAGQivENAEIKGIEIFNSVDNN---YKKIFLKDGN--VVGAVLYGDIDD-GSRFYNMMKKGESTED 389
Cdd:PRK14989 319 LSAKLKLLGVDVGGIGD--AHGRTPGARSYVYLDESkeiYKRLIVSEDNktLLGAVLVGDTSDyGNLLQLVLNAIELPEN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 390 -YTLVSLLTKGGEEASLSIADMADDETICGCNGVDKGTIVNAITEnGFTTVEEVTAKTKAGNSCGKCKPQIAQILQHTLG 468
Cdd:PRK14989 397 pDSLILPAHAGSGKPSIGVDKLPDSAQICSCFDVTKGDLIAAINK-GCHTVAALKAETKAGTGCGGCIPLVTQVLNAELA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 469 DDFVAAKpAGICGCTDLTRDQIVTQIRAKGLKTSKEVrhvLNFKNKG-GCPKCRPAINYYL-----NMVYPHDHEDERES 542
Cdd:PRK14989 476 KQGIEVN-NNLCEHFAYSRQELFHLIRVEGIKTFEEL---LAKHGKGyGCEVCKPTVGSLLascwnEYILKPQHTPLQDT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 543 rfaNERYHANIQNDGTFSVIPQMRGGVTDADQLIRLGEVAKKYHVpLVKVTGSQRVGLYGVKKEELPNIWQDL---GMRS 619
Cdd:PRK14989 552 ---NDNFLANIQKDGTYSVIPRSAGGEITPEGLMAVGRIAREFNL-YTKITGSQRIGLFGAQKDDLPEIWRQLieaGFET 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 620 ASAYGKKTRSVKSCVGKEFCRFGTQYTTRLGIRLEKTFEYIDTPHKFKMGVSGCPRSCVESGVKDFGVISVENGFQIYIG 699
Cdd:PRK14989 628 GHAYAKALRMAKTCVGSTWCRYGVGDSVGLGVELENRYKGIRTPHKMKFGVSGCTRECAEAQGKDVGIIATEKGWNLYVC 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 700 GNGGTEVEKAEFLTTVETEDEVIKLCGALMQYYRETGIYAERTAPWLRRL--GFENVKEVLLDPERQ-NELFERIMDAKK 776
Cdd:PRK14989 708 GNGGMKPRHADLLAADLDRETLIKYLDRFMMFYIRTADKLQRTAVWLENLegGIDYLKAVIIDDKLGlNAQLEEEMARLR 787
|
810 820
....*....|....*....|
gi 613310046 777 AVEAEPWEAITSNAQARKIF 796
Cdd:PRK14989 788 EAVVCEWTETVNTPSAQTRF 807
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
25-319 |
2.35e-74 |
|
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: 244.72 E-value: 2.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 25 RANDLYDITVIGKEPYPNYNRIMLSN-ILQNKMTVEETIMNPYEWYEEHDIKLITNDPVVDVDRTNQNVTTANGIEVAYD 103
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYyVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 104 KLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMMNIAKTK--KKAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLM 181
Cdd:COG0446 81 KLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 182 eMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVeGVKLADGREIPADLVVMAVGIRPYTEVAKESGL--DVNRGI 259
Cdd:COG0446 161 -GVLDPEMAALLEEELREHGVELRLGETVVAIDGDDKV-AVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLalGERGWI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613310046 260 VVNDVMQTSDSNVFAVGECAEHNGKVYG------LVAPLYEQGKVLADHLTNKETnGYKGSTTFTS 319
Cdd:COG0446 239 KVDETLQTSDPDVYAAGDCAEVPHPVTGktvyipLASAANKQGRVAAENILGGPA-PFPGLGTFIS 303
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-278 |
1.01e-59 |
|
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: 204.86 E-value: 1.01e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 5 KLVMIGNGMAGIRTIEEiLERANdlYDITVIGKEPYPNYNRIMLSNILQNKMTVEETIMNP---YEWYEEH------DIK 75
Cdd:pfam07992 2 DVVVIGGGPAGLAAALT-LAQLG--GKVTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWadlYKRKEEVvkklnnGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 76 LITNDPVVDVDRTNQNVT-----TANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMmNIAKTKKKAIV 150
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVleelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEAL-RLKLLPKRVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 151 IGGGLLGLECARGLLDQGMEVTVLHLAEWLMEMqLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREI 230
Cdd:pfam07992 158 VGGGYIGVELAAALAKLGKEVTLIEALDRLLRA-FDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 613310046 231 PADLVVMAVGIRPYTEVAKESGL--DVNRGIVVNDVMQTSDSNVFAVGEC 278
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLelDERGGIVVDEYLRTSVPGIYAAGDC 286
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
7-308 |
1.98e-48 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 175.88 E-value: 1.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 7 VMIGNGMAGIRTIEEIlERANDLYDITVIGKEPYPNYNRIMLSNILQNKMTVEE-TIMNPYEWYEEHDIKLITNDPVVDV 85
Cdd:PRK04965 6 VIIGSGFAARQLVKNI-RKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDlTRQSAGEFAEQFNLRLFPHTWVTDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 86 DRTNQNVTtANGIEVAYDKLIFATGSKAFVIPVPGS----TLPSVIGWRTIddtEQMMNIAKtkkKAIVIGGGLLGLECA 161
Cdd:PRK04965 85 DAEAQVVK-SQGNQWQYDKLVLATGASAFVPPIPGRelmlTLNSQQEYRAA---ETQLRDAQ---RVLVVGGGLIGTELA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 162 RGLLDQGMEVTVLHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPADLVVMAVGI 241
Cdd:PRK04965 158 MDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613310046 242 RPYTEVAKESGLDVNRGIVVNDVMQTSDSNVFAVGECAEHNGKVYGLVAPLYEQGKVLADHLTNKET 308
Cdd:PRK04965 238 RPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNT 304
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
66-361 |
5.25e-40 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 153.66 E-value: 5.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 66 YEWYEEHDIKLITNDPVVDVDRTNQNVTTANG-----IEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMMN 140
Cdd:PRK09564 63 PEEFIKSGIDVKTEHEVVKVDAKNKTITVKNLktgsiFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 141 IAKTK--KKAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDD 218
Cdd:PRK09564 143 LLKDEeiKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDK 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 219 VEGVKlADGREIPADLVVMAVGIRPYTEVAKESGLDV--NRGIVVNDVMQTSDSNVFAVGECAehngKVYGLV------A 290
Cdd:PRK09564 223 VEGVV-TDKGEYEADVVIVATGVKPNTEFLEDTGLKTlkNGAIIVDEYGETSIENIYAAGDCA----TIYNIVsnknvyV 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613310046 291 PLY----EQGKVLADHLTNKETNgYKGSTTFTSLKVSGCDLYSAGQIVENAEIKGIeifnsvdnNYKKIFLKDGN 361
Cdd:PRK09564 298 PLAttanKLGRMVGENLAGRHVS-FKGTLGSACIKVLDLEAARTGLTEEEAKKLGI--------DYKTVFIKDKN 363
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
3-303 |
4.56e-35 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 137.57 E-value: 4.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 3 KQKLVMIGNGMAGIRTIEEILERANDLYDITVIGKEPY----PnynriMLSNILQNKMTVEETIMnPY-EWYEEHDIKLI 77
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYhlfqP-----LLPEVAAGTLSPDDIAI-PLrELLRRAGVRFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 78 TnDPVVDVDRTNQNVTTANGIEVAYDKLIFATGSKAFVIPVPGSTlPSVIGWRTIDDTE-------QMMNIAKTKKKA-- 148
Cdd:COG1252 75 Q-GEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIPGLA-EHALPLKTLEDALalrerllAAFERAERRRLLti 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 149 IVIGGGLLGLECA-------------RGLLDQGMEVTVLHLAEWLMEMqLDRKAGNMLKADLEKQGMKFEMQANTTEIlg 215
Cdd:COG1252 153 VVVGGGPTGVELAgelaellrkllryPGIDPDKVRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEV-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 216 edDVEGVKLADGREIPADLVVMAVGIRPyTEVAKESGLDVNRG--IVVNDVMQT-SDSNVFAVGECA---EHNGKVYGLV 289
Cdd:COG1252 230 --DADGVTLEDGEEIPADTVIWAAGVKA-PPLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAavpDPDGKPVPKT 306
|
330
....*....|....*
gi 613310046 290 APL-YEQGKVLADHL 303
Cdd:COG1252 307 AQAaVQQAKVLAKNI 321
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
1-279 |
7.84e-31 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 125.42 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 1 MAKQKLVMIGNGMAGIRTIEEILERANDlYDITVIGKEPYPNYNRIMLSNILQNKMTVEETIMNPYEWYEEHDIKLITND 80
Cdd:PRK09754 1 MKEKTIIIVGGGQAAAMAAASLRQQGFT-GELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 81 PVVDVDRTNQNVTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIDDTEQMMNIAKTKKKAIVIGGGLLGLEC 160
Cdd:PRK09754 80 TIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 161 ARGLLDQGMEVTVLHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEgVKLADGREIPADLVVMAVG 240
Cdd:PRK09754 160 AASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIG 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 613310046 241 IRPYTEVAKESGLDVNRGIVVNDVMQTSDSNVFAVGECA 279
Cdd:PRK09754 239 ISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| NIR_SIR |
pfam01077 |
Nitrite and sulphite reductase 4Fe-4S domain; Sulphite and nitrite reductases are vital in the ... |
624-761 |
2.92e-27 |
|
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: 108.13 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 624 GKKTRSVKSCVGKEFCRFGTQYTTRLGIRLEKTFEYI----DTPHKFKMGVSGCPRSCVESGVKDFGVISVEN-----GF 694
Cdd:pfam01077 1 GDNVRNVTLCPGAGLCPEELLDTRPLAKAIEDEFEPDygfpYLPRKFKIAVSGCPNNCVAAHANDIGFVGVWKdggeiGF 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613310046 695 QIYIGGNGGTEVEKAEFLTTVE--TEDEVIKLCGALMQYYR----ETGIYAERTAPWLRRLGFENVKEVLLDP 761
Cdd:pfam01077 81 NILVGGGLGRTPGAAATLKVVPfvPEEDVLEVIEAILEVYRdhgdRENRKKERLKYLIERLGLEKFREEVEER 153
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
92-307 |
2.81e-26 |
|
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: 112.87 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 92 VTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIGWRTIddteqmMNIAKTKKKAIVIGGGLLGLECA---RGLldqG 168
Cdd:COG1249 121 VEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSDEA------LELEELPKSLVVIGGGYIGLEFAqifARL---G 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 169 MEVTVLHLAEWLMEMqLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDD-VEgVKLADGRE---IPADLVVMAVGIRPY 244
Cdd:COG1249 192 SEVTLVERGDRLLPG-EDPEISEALEKALEKEGIDILTGAKVTSVEKTGDgVT-VTLEDGGGeeaVEADKVLVATGRRPN 269
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613310046 245 TEV--AKESGLDVNR--GIVVNDVMQTSDSNVFAVGECaehNGKvYGL--VAplYEQGKVLADHLTNKE 307
Cdd:COG1249 270 TDGlgLEAAGVELDErgGIKVDEYLRTSVPGIYAIGDV---TGG-PQLahVA--SAEGRVAAENILGKK 332
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
77-290 |
3.50e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 97.88 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 77 ITNDPVVDVDRTNQN--VTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIG--WRTIDDTEQMmniakTKKKAIVIG 152
Cdd:COG0492 74 ILLEEVTSVDKDDGPfrVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGvsYCATCDGFFF-----RGKDVVVVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 153 GGLLGLECARGLLDQGMEVTVLHLAEWLmemqldRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADG----- 227
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLIHRRDEL------RASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVktgee 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613310046 228 REIPADLVVMAVGIRPYTEVAKESGLDVNRG--IVVNDVMQTSDSNVFAVGECAehnGKVYGLVA 290
Cdd:COG0492 223 KELEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR---DYKYRQAA 284
|
|
| NirB_Fer2_BFD-like_2 |
cd19944 |
second bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
478-528 |
7.76e-22 |
|
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: 89.17 E-value: 7.76e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 613310046 478 GICGCTDLTRDQIVTQIRAKGLKTSKEVRHVLNFKNKGGCPKCRPAINYYL 528
Cdd:cd19944 2 TLCSCTDLSHDEVREAIQEHGLTSFEEVMAALGWKTPDGCEKCRPALNYYL 52
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
4-327 |
8.81e-22 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 99.09 E-value: 8.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 4 QKLVMIGnGMAGIRTIEEILERANDLYDITVIGKEPYPNYNRIMLSNILQNKMTVEETIM--NPYEWYEEHDIKLITNDP 81
Cdd:PRK13512 2 PKIIVVG-AVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALayTPEKFYDRKQITVKTYHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 82 VVDVDRTNQNVTTAN-----GIEVAYDKLIFATGSKAFVipvPGSTLPSVIGWRTIDDTEQMMNIAKTK--KKAIVIGGG 154
Cdd:PRK13512 81 VIAINDERQTVTVLNrktneQFEESYDKLILSPGASANS---LGFESDITFTLRNLEDTDAIDQFIKANqvDKALVVGAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 155 LLGLECARGLLDQGMEVTVLHLAEWLMEmQLDRKAGNMLKADLEKQGMKFEMQantTEIlgeDDVEG--VKLADGREIPA 232
Cdd:PRK13512 158 YISLEVLENLYERGLHPTLIHRSDKINK-LMDADMNQPILDELDKREIPYRLN---EEI---DAINGneVTFKSGKVEHY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 233 DLVVMAVGIRPYTEVAKESGLDVNRG--IVVNDVMQTSDSNVFAVGECAEHNGKVYGLVA--PL----YEQGKVLADHLT 304
Cdd:PRK13512 231 DMIIEGVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIITSHYRHVDLPAsvPLawgaHRAASIVAEQIA 310
|
330 340 350
....*....|....*....|....*....|...
gi 613310046 305 NKET---NGYKGST-------TFTSLKVSGCDL 327
Cdd:PRK13512 311 GNDTiefKGFLGNNivkffdyTFASVGVKPNEL 343
|
|
| NirB_Fer2_BFD-like_1 |
cd19943 |
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
411-463 |
3.80e-21 |
|
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: 87.29 E-value: 3.80e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 613310046 411 ADDETICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGNSCGKCKPQIAQIL 463
Cdd:cd19943 1 PDDAEVCGCNGVSKGAIVQAIQEKGLTTLDEVKACTKASTSCGGCTPLVEQLL 53
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
105-370 |
4.68e-21 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 97.14 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 105 LIFATGSKAFVIPvpgsTLPsvIGWRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLMEMQ 184
Cdd:PRK06416 138 IILATGSRPRELP----GIE--IDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 185 lDRKAGNMLKADLEKQGMKFEMQANTTEIL-GEDDVEgVKLADG---REIPADLVVMAVGIRPYTE-VAKES-GLDVNRG 258
Cdd:PRK06416 212 -DKEISKLAERALKKRGIKIKTGAKAKKVEqTDDGVT-VTLEDGgkeETLEADYVLVAVGRRPNTEnLGLEElGVKTDRG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 259 -IVVNDVMQTSDSNVFAVGEcaehngkvygLVAPL------YEQGKVLADHLT-NKETNGYKG--STTFTSLKVSgcdly 328
Cdd:PRK06416 290 fIEVDEQLRTNVPNIYAIGD----------IVGGPmlahkaSAEGIIAAEAIAgNPHPIDYRGipAVTYTHPEVA----- 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 613310046 329 SAGQIVENAEIKGIEIFNSVDN---NYKKIFL-------------KDGNVVGAVLYGD 370
Cdd:PRK06416 355 SVGLTEAKAKEEGFDVKVVKFPfagNGKALALgetdgfvklifdkKDGEVLGAHMVGA 412
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
550-758 |
2.54e-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: 89.02 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 550 HANIQnDG----TFSVIPqmrGGVTDaDQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIWQDL-GMRSASAYG 624
Cdd:COG0155 298 HEQKQ-DGlyyvGLSVEN---GRITD-EQLRALADLAERYGSGEIRLTPNQNLILADVPEEDLPALEAALrALGLATPPS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 625 KKTRSVKSCVGKEFCRFGTQYTTRLGIRLEKTFE----YIDTPHKFKMGVSGCPRSCVESGVKDFG-----VISVENGFQ 695
Cdd:COG0155 373 GLRRDSIACPGLPTCKLAIAESKRLAPALADRLEedldGLHDDEPIRIRISGCPNSCGRHYIADIGlvgkaKKGVVEAYQ 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613310046 696 IYIGGNGGtevEKAEFLTTVE---TEDEVIKLCGALMQYYRETGIYAERTAPWLRRLGFENVKEVL 758
Cdd:COG0155 453 LYLGGGLG---GDARLGRKYGpkvPADEIPDALERLLEAYLAEREEGESFGDFVRRVGIEPLKELL 515
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
96-344 |
6.37e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 87.54 E-value: 6.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 96 NGIEVAYDKLIFATGSKafVIPVPGstlpsviGWRTIDD----TEQMMNIAKTKKKAIVIGGGLLGLECARGLLDQGMEV 171
Cdd:PRK06292 125 NGERIEAKNIVIATGSR--VPPIPG-------VWLILGDrlltSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKV 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 172 TVLHLAEWLMEMQlDRKAGNMLKADLEKQgMKFEMQANTTEILGEDDVEGVKLADG---REIPADLVVMAVGIRPYTEVA 248
Cdd:PRK06292 196 TVFERGDRILPLE-DPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGgktETIEADYVLVATGRRPNTDGL 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 249 KESGLDV---NRG-IVVNDVMQTSDSNVFAVGECaehNGKvyglvAPL----YEQGKVLADHLTNKETNGYK----GSTT 316
Cdd:PRK06292 274 GLENTGIeldERGrPVVDEHTQTSVPGIYAAGDV---NGK-----PPLlheaADEGRIAAENAAGDVAGGVRyhpiPSVV 345
|
250 260
....*....|....*....|....*...
gi 613310046 317 FTSLKVSgcdlySAGQIVENAEIKGIEI 344
Cdd:PRK06292 346 FTDPQIA-----SVGLTEEELKAAGIDY 368
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
92-283 |
1.40e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 86.52 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 92 VTTANGIEVAYDKLIFATGSKAfvIPVPGSTLPSvigwRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECA---RGLldqG 168
Cdd:PRK06327 136 VTGEDETVITAKHVIIATGSEP--RHLPGVPFDN----KIILDNTGALNFTEVPKKLAVIGAGVIGLELGsvwRRL---G 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 169 MEVTVLHLAEWLMEMQLDRKAGNMLKAdLEKQGMKFEMQANTTEIlgEDDVEGVKL----ADGRE--IPADLVVMAVGIR 242
Cdd:PRK06327 207 AEVTILEALPAFLAAADEQVAKEAAKA-FTKQGLDIHLGVKIGEI--KTGGKGVSVaytdADGEAqtLEVDKLIVSIGRV 283
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 613310046 243 PYTE--VAKESGLDVN-RG-IVVNDVMQTSDSNVFAVGEC---------AEHNG 283
Cdd:PRK06327 284 PNTDglGLEAVGLKLDeRGfIPVDDHCRTNVPNVYAIGDVvrgpmlahkAEEEG 337
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
415-465 |
2.40e-16 |
|
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: 73.33 E-value: 2.40e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 613310046 415 TICGCNGVDKGTIVNAItENGFTTVEEVTAKTKAGNSCGKCKPQIAQILQH 465
Cdd:pfam04324 1 IVCRCFGVTDGEIRDAI-REGLTTVEEVKRRTKAGTGCGSCRPAIEEILAE 50
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
87-279 |
1.00e-15 |
|
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: 80.18 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 87 RTNQNV---TTANGIEVAYDKLIFATGS-KAFVIPVPGSTLPSVIG----WRTIDDTEQMMNIAKTKKKAIVIGGGLLGL 158
Cdd:COG0493 189 RTNVEVgkdITLDELLEEFDAVFLATGAgKPRDLGIPGEDLKGVHSamdfLTAVNLGEAPDTILAVGKRVVVIGGGNTAM 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 159 ECARGLLDQG-MEVTVLHLaewlmemqldRKAGNMlKADLEKQ------GMKFEMQANTTEILGEDD--VEGVKL----- 224
Cdd:COG0493 269 DCARTALRLGaESVTIVYR----------RTREEM-PASKEEVeealeeGVEFLFLVAPVEIIGDENgrVTGLECvrmel 337
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613310046 225 ----ADGR-----------EIPADLVVMAVGIRP-YTEVAKESGLDVNRG--IVVNDV-MQTSDSNVFAVGECA 279
Cdd:COG0493 338 gepdESGRrrpvpiegsefTLPADLVILAIGQTPdPSGLEEELGLELDKRgtIVVDEEtYQTSLPGVFAGGDAV 411
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
96-278 |
3.28e-15 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 79.09 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 96 NGIEVAYDKLIFATGSKAFVIPVPGstlpsvigwrtIDDT-----EQMMNIAKTKKKAIVIGGGLLGLECA---RGLldq 167
Cdd:PRK06370 128 GGETLRAKRIFINTGARAAIPPIPG-----------LDEVgyltnETIFSLDELPEHLVIIGGGYIGLEFAqmfRRF--- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 168 GMEVTVLHLAEWLMEMQlDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKL---ADGREIPADLVVMAVGIRPY 244
Cdd:PRK06370 194 GSEVTVIERGPRLLPRE-DEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLdcnGGAPEITGSHILVAVGRVPN 272
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 613310046 245 TEvakESGL-------DVNRGIVVNDVMQTSDSNVFAVGEC 278
Cdd:PRK06370 273 TD---DLGLeaagvetDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| CysI |
COG0155 |
Sulfite reductase, beta subunit (hemoprotein) [Inorganic ion transport and metabolism]; ... |
562-758 |
7.81e-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: 78.24 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 562 IPqmrGGVTDADQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIWQDL---GMRSASAYGKKTRSVKSCVGKEF 638
Cdd:COG0155 61 IP---GGVLTPEQLRALADIAREYGRGYLHLTTRQNIQLHWILLEDLPEILRELaevGLTTIGACGDVVRNVTASPLAGV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 639 CRFGTQYTTRLGIRLEKTF----EYIDTPHKFKMGVSGCPRSCVESGVKDFGVISVEN-----GFQIYIGGnG------- 702
Cdd:COG0155 138 DPDELFDVRPYAEAISQHLlghpEYTYLPRKFKIAFSGPPEDDADVEINDLGFIAVVKedglvGFNVLVGG-Glgrtprl 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613310046 703 GTEVEkaEFLttveTEDEVIKLCGALMQYYRETGIYAER-------TapwLRRLGFENVKEVL 758
Cdd:COG0155 217 ADVLG--EFV----PPEDLLDVAEAVVRVFRDYGDRDNRkkarlkyL---VDDLGVEKFREEV 270
|
|
| Rubredoxin_C |
pfam18267 |
Rubredoxin NAD+ reductase C-terminal domain; This is the C-terminal domain of NADH rubredoxin ... |
318-385 |
1.65e-14 |
|
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: 68.74 E-value: 1.65e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613310046 318 TSLKVSGCDLYSAGQIVENAEIKGIEIFNSVDNNYKKIFLKDGNVVGAVLYGDIDDGSRFYNMMKKGE 385
Cdd:pfam18267 3 TILKVFGIDLFSMGDIEENDNAEEIVKVDASNGIYKKLFIRDGKLVGAILIGDTSESPKLKKAIEKKI 70
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-227 |
1.96e-14 |
|
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: 68.77 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 147 KAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLMeMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLAD 226
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
.
gi 613310046 227 G 227
Cdd:pfam00070 80 G 80
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
87-278 |
5.37e-13 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 72.12 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 87 RTNQNV---TTANGIEVAYDKLIFATGS-KAFVIPVPGSTLPSV------IGW--RTIDDTEQMMNIAKTKKKAIVIGGG 154
Cdd:PRK12810 211 RTNVEVgkdITAEELLAEYDAVFLGTGAyKPRDLGIPGRDLDGVhfamdfLIQntRRVLGDETEPFISAKGKHVVVIGGG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 155 LLGLECARGLLDQG-MEVTVLHLaewlMEMQLDRKAGNM---LKADLEKQ------GMKFEMQANTTEILGEDD-VEGVK 223
Cdd:PRK12810 291 DTGMDCVGTAIRQGaKSVTQRDI----MPMPPSRRNKNNpwpYWPMKLEVsnaheeGVEREFNVQTKEFEGENGkVTGVK 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613310046 224 LAD--------------GREIPADLVVMAVGIR-PYTEVAKESGLDVN-RGIVVND--VMQTSDSNVFAVGEC 278
Cdd:PRK12810 367 VVRtelgegdfepvegsEFVLPADLVLLAMGFTgPEAGLLAQFGVELDeRGRVAAPdnAYQTSNPKVFAAGDM 439
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
102-276 |
5.61e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 71.17 E-value: 5.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 102 YDKLIFATGS-KAFVIPVPGSTLPSV--------------IG---WRTIDDTEqmmniaktKKKAIVIGGGLLGLECARG 163
Cdd:PRK12770 119 YDAVLIATGTwKSRKLGIPGEDLPGVysaleylfriraakLGylpWEKVPPVE--------GKKVVVVGAGLTAVDAALE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 164 LLDQGME-VTVLHlaewlmemqldRK------AGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGR-------- 228
Cdd:PRK12770 191 AVLLGAEkVYLAY-----------RRtineapAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGVELAKMRlgepdesg 259
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613310046 229 ------------EIPADLVVMAVGIRPYTEVAKES-GLDVNRG--IVVNDVMQTSDSNVFAVG 276
Cdd:PRK12770 260 rprpvpipgsefVLEADTVVFAIGEIPTPPFAKEClGIELNRKgeIVVDEKHMTSREGVFAAG 322
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
92-304 |
6.10e-13 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 71.73 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 92 VTTANGIEVAY--DKLIFATGSKAFVIP-VPgstlpsvIGWRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECA---RGLl 165
Cdd:PRK05249 126 VECPDGEVETLtaDKIVIATGSRPYRPPdVD-------FDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYAsifAAL- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 166 dqGMEVTVLHLAEWLMEMqLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPADLVVMAVGIRPYT 245
Cdd:PRK05249 198 --GVKVTLINTRDRLLSF-LDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNT 274
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613310046 246 EV--AKESGLDVN-RG-IVVNDVMQTSDSNVFAVGEcaehngkVYG---LVAPLYEQGKVLADHLT 304
Cdd:PRK05249 275 DGlnLENAGLEADsRGqLKVNENYQTAVPHIYAVGD-------VIGfpsLASASMDQGRIAAQHAV 333
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
98-277 |
1.47e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 70.55 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 98 IEVAYDKLIFATGSKAFVIPVPGSTLPsvigwRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECARGLLDQGMEVTVLHLA 177
Cdd:PRK07251 115 IELTAETIVINTGAVSNVLPIPGLADS-----KHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 178 EWLMEMQLDRKAgNMLKADLEKQGMKFEMQANTTEILGEDDvEGVKLADGREIPADLVVMAVGIRPYTEVAKESGLDV-- 255
Cdd:PRK07251 190 STILPREEPSVA-ALAKQYMEEDGITFLLNAHTTEVKNDGD-QVLVVTEDETYRFDALLYATGRKPNTEPLGLENTDIel 267
|
170 180
....*....|....*....|....
gi 613310046 256 -NRG-IVVNDVMQTSDSNVFAVGE 277
Cdd:PRK07251 268 tERGaIKVDDYCQTSVPGVFAVGD 291
|
|
| NifU_Fer2_BFD-like |
cd19947 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of nitrogen fixation ... |
412-463 |
2.09e-12 |
|
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: 62.30 E-value: 2.09e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 613310046 412 DDETICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGNSCGKCKPQIAQIL 463
Cdd:cd19947 1 EGAIVCKCFGVTEVMIERAIRENNLTTVEDVTNYTKAGGGCGSCHEKIEDIL 52
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
1-277 |
3.15e-12 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 69.66 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 1 MAKQKLVMIGNGMAGiRTIE----------EILERANDLYDITVIGKEPYPNYNRIM-------LSNILQNKMTVEETIM 63
Cdd:PRK08010 1 MNKYQAVIIGFGKAG-KTLAvtlakagwrvALIEQSNAMYGGTCINIGCIPTKTLVHdaqqhtdFVRAIQRKNEVVNFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 64 NPyewyEEHDIKLITNDPVVD-----VDRTNQNVTTANG-IEVAYDKLIFATGSKAFVIPVPG-STLPSVIgwrtidDTE 136
Cdd:PRK08010 80 NK----NFHNLADMPNIDVIDgqaefINNHSLRVHRPEGnLEIHGEKIFINTGAQTVVPPIPGiTTTPGVY------DST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 137 QMMNIAKTKKKAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLMEMQlDRKAGNMLKADLEKQGMKFEMQANTTEILGE 216
Cdd:PRK08010 150 GLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPRE-DRDIADNIATILRDQGVDIILNAHVERISHH 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613310046 217 DDVEGVKLADGREIpADLVVMAVGIRPYTEV--AKESGLDVNR--GIVVNDVMQTSDSNVFAVGE 277
Cdd:PRK08010 229 ENQVQVHSEHAQLA-VDALLIASGRQPATASlhPENAGIAVNErgAIVVDKYLHTTADNIWAMGD 292
|
|
| NIR_SIR_ferr |
pfam03460 |
Nitrite/Sulfite reductase ferredoxin-like half domain; Sulfite and Nitrite reductases are key ... |
554-615 |
3.78e-12 |
|
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: 62.16 E-value: 3.78e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613310046 554 QNDGTFSVIPQMRGGVTDADQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIWQDL 615
Cdd:pfam03460 3 QKDGDYMVRVRVPGGRLTAEQLRALADIAEKYGDGEIRLTTRQNLELHGVPEEDLPELLEEL 64
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
1-309 |
9.62e-12 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 67.87 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 1 MAKQKLVMIGNGMAGIRTIEEIlerANDLYDITVIGKEpypnyNRIMLSNILQNKM--TVE-----ETI-----MNPYEW 68
Cdd:PTZ00318 8 LKKPNVVVLGTGWAGAYFVRNL---DPKKYNITVISPR-----NHMLFTPLLPQTTtgTLEfrsicEPVrpalaKLPNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 69 YEEHdiklitndpVVDVDRTNQNVT----------TANGIEVAYDKLIFATGSKAFVIPVPGST-----LPSVIGWRTI- 132
Cdd:PTZ00318 80 LRAV---------VYDVDFEEKRVKcgvvsksnnaNVNTFSVPYDKLVVAHGARPNTFNIPGVEeraffLKEVNHARGIr 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 133 ----------DDTEQMMNIAKTKKKAIVIGGGLLGLECARGLLD--------------QGMEVTVLHLAEWLMEMqLDRK 188
Cdd:PTZ00318 151 krivqcieraSLPTTSVEERKRLLHFVVVGGGPTGVEFAAELADffrddvrnlnpelvEECKVTVLEAGSEVLGS-FDQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 189 AGNMLKADLEKQGMKFEMQANTTEILGEDdvegVKLADGREIPADLVVMAVGIRPyTEVAKESGLD-VNRG-IVVNDVMQ 266
Cdd:PTZ00318 230 LRKYGQRRLRRLGVDIRTKTAVKEVLDKE----VVLKDGEVIPTGLVVWSTGVGP-GPLTKQLKVDkTSRGrISVDDHLR 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 613310046 267 TSD-SNVFAVGECAEHNGKVYGLVAPLYE-QGKVLADHLTNKETN 309
Cdd:PTZ00318 305 VKPiPNVFALGDCAANEERPLPTLAQVASqQGVYLAKEFNNELKG 349
|
|
| NasA-like_Fer2_BFD-like |
cd19948 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ... |
413-463 |
1.22e-11 |
|
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: 60.23 E-value: 1.22e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 613310046 413 DETICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGNSCGKCKPQIAQIL 463
Cdd:cd19948 1 GRTVCACFSVGENTIRRAIADNGLTSVAQVGTCLKAGTNCGSCVPEIQKLL 51
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
85-353 |
1.51e-11 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 67.57 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 85 VDRTNQNVTTANGIEVAY--DKLIFATGSKAFVIPVPGSTLPSVigwrTIDDteqMMNIAKTKKKAIVIGGGLLGLECAR 162
Cdd:TIGR01438 125 VDKHRIKATNKKGKEKIYsaERFLIATGERPRYPGIPGAKELCI----TSDD---LFSLPYCPGKTLVVGASYVALECAG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 163 GLLDQGMEVTVlhLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPA---DLVVMAV 239
Cdd:TIGR01438 198 FLAGIGLDVTV--MVRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEeeyDTVLLAI 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 240 GIRPYTE-VAKES-GLDVNRG---IVVNDVMQTSDSNVFAVGECAEHNGKvyglVAPLYEQ-GKVLADHL--TNKETNGY 311
Cdd:TIGR01438 276 GRDACTRkLNLENvGVKINKKtgkIPADEEEQTNVPYIYAVGDILEDKPE----LTPVAIQaGRLLAQRLfkGSTVICDY 351
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 613310046 312 KG--STTFTSLKVSGCDlYSAGQIVENAEIKGIEIFNSVDNNYK 353
Cdd:TIGR01438 352 ENvpTTVFTPLEYGACG-LSEEKAVEKFGEENVEVFHSYFWPLE 394
|
|
| Bfd |
COG2906 |
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism]; |
416-468 |
4.05e-11 |
|
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
Pssm-ID: 442150 [Multi-domain] Cd Length: 54 Bit Score: 58.68 E-value: 4.05e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 613310046 416 ICGCNGVDKGTIVNAItENGFTTVEEVTAKTKAGNSCGKCKPQIAQILQHTLG 468
Cdd:COG2906 3 VCLCNGVTDRQIRAAI-AEGATSLEELRAALGAGTQCGSCVPEARELLAEALA 54
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
102-279 |
4.51e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 65.97 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 102 YDKLIFATG-SKAFVIPVPGSTLPSVIgwRTID---DTEQMMNIAKTK--KKAIVIGGGLLGLECARGLLDQGME-VTVL 174
Cdd:PRK11749 226 YDAVFIGTGaGLPRFLGIPGENLGGVY--SAVDfltRVNQAVADYDLPvgKRVVVIGGGNTAMDAARTAKRLGAEsVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 175 H---LAEwlM-----EMQLdrkagnmlkAdlEKQGMKFEMQANTTEILGEDD-VEGVKL---------ADGR-------- 228
Cdd:PRK11749 304 YrrgREE--MpaseeEVEH---------A--KEEGVEFEWLAAPVEILGDEGrVTGVEFvrmelgepdASGRrrvpiegs 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613310046 229 --EIPADLVVMAVGIRPYTEVAKES-GLDVNR--GIVVNDV-MQTSDSNVFAVGECA 279
Cdd:PRK11749 371 efTLPADLVIKAIGQTPNPLILSTTpGLELNRwgTIIADDEtGRTSLPGVFAGGDIV 427
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
94-276 |
4.84e-11 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 65.75 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 94 TANGIEVAYDKLIFATGSKAFVIPVPGStlpSVIGWRTIDDteqMMNIAKTKKKAIVIGGGLLGLECARGLLDQGMEVTV 173
Cdd:PRK07846 121 TGDGEEITADQVVIAAGSRPVIPPVIAD---SGVRYHTSDT---IMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 174 LHLAEWLMEmQLDRkagNMLKADLEKQGMKFEMQANTTEILGEDDVEGVK--LADGREIPADLVVMAVGIRPYTEV--AK 249
Cdd:PRK07846 195 VNRSGRLLR-HLDD---DISERFTELASKRWDVRLGRNVVGVSQDGSGVTlrLDDGSTVEADVLLVATGRVPNGDLldAA 270
|
170 180
....*....|....*....|....*....
gi 613310046 250 ESGLDVNRG--IVVNDVMQTSDSNVFAVG 276
Cdd:PRK07846 271 AAGVDVDEDgrVVVDEYQRTSAEGVFALG 299
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
99-286 |
3.66e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 63.25 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 99 EVAYDKLIFATGSKAFVIPVPGstLPSVIGWRTiddTEQMMNIAkTKKKAIVIGGGLLGLECARGLLDQGMEVTVLhlAE 178
Cdd:PRK13748 230 VVAFDRCLIATGASPAVPPIPG--LKETPYWTS---TEALVSDT-IPERLAVIGSSVVALELAQAFARLGSKVTIL--AR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 179 WLMEMQLDRKAGNMLKADLEKQGMkfemqanttEILGEDDVEGVKLADGR--------EIPADLVVMAVGIRPYT-EVAK 249
Cdd:PRK13748 302 STLFFREDPAIGEAVTAAFRAEGI---------EVLEHTQASQVAHVDGEfvlttghgELRADKLLVATGRAPNTrSLAL 372
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 613310046 250 ES-GLDVN-RG-IVVNDVMQTSDSNVFAVGECAEHNGKVY 286
Cdd:PRK13748 373 DAaGVTVNaQGaIVIDQGMRTSVPHIYAAGDCTDQPQFVY 412
|
|
| Fer2_BFD-like |
cd19942 |
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ... |
415-462 |
7.70e-10 |
|
[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: 54.75 E-value: 7.70e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 613310046 415 TICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGNSCGKCKPQIAQI 462
Cdd:cd19942 2 LVCECFAVTEKELREAIRKGGLKTVEELLTGTGAGGGCGVCHPHVAQL 49
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
146-277 |
1.61e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 60.80 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 146 KKAIVIGGGLLGLECARGLLDQGMEVTVLHlaewlmemqldRKAGNMLKADLE------KQGMKFEMQANTTEILGEDD- 218
Cdd:PRK12831 282 KKVAVVGGGNVAMDAARTALRLGAEVHIVY-----------RRSEEELPARVEevhhakEEGVIFDLLTNPVEILGDENg 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 219 -VEGVKL---------ADGR-----------EIPADLVVMAVGIRPYTEVAKES-GLDVNRG--IVVN-DVMQTSDSNVF 273
Cdd:PRK12831 351 wVKGMKCikmelgepdASGRrrpveiegsefVLEVDTVIMSLGTSPNPLISSTTkGLKINKRgcIVADeETGLTSKEGVF 430
|
....
gi 613310046 274 AVGE 277
Cdd:PRK12831 431 AGGD 434
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
96-278 |
3.39e-09 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 59.78 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 96 NGIEVAYDKLIFATGSKAFVIPVPGSTLpsvigwrTIDDTEqMMNIAKTKKKAIVIGGGLLGLECA---RGLldqGMEVT 172
Cdd:PRK06116 126 NGERYTADHILIATGGRPSIPDIPGAEY-------GITSDG-FFALEELPKRVAVVGAGYIAVEFAgvlNGL---GSETH 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 173 VLHLAEwLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDveG---VKLADGREIPADLVVMAVGIRPYT---- 245
Cdd:PRK06116 195 LFVRGD-APLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNAD--GsltLTLEDGETLTVDCLIWAIGREPNTdglg 271
|
170 180 190
....*....|....*....|....*....|....*.
gi 613310046 246 -EVAkesGLDVN-RG-IVVNDVMQTSDSNVFAVGEC 278
Cdd:PRK06116 272 lENA---GVKLNeKGyIIVDEYQNTNVPGIYAVGDV 304
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
85-277 |
5.41e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 59.44 E-value: 5.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 85 VDRTNQNVTTANGIEVAY--DKLIFATGSKAFVIPVPGSTLPSVigwrtiddTEQMMNIAKTKKKAIVIGGGLLGLECAR 162
Cdd:PLN02507 149 VGPNEVEVTQLDGTKLRYtaKHILIATGSRAQRPNIPGKELAIT--------SDEALSLEELPKRAVVLGGGYIAVEFAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 163 glLDQGMEVTV-LHLAEWLMEMQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPADLVVMAVGI 241
Cdd:PLN02507 221 --IWRGMGATVdLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGR 298
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 613310046 242 RPYT------EVAKEsgLDVNRGIVVNDVMQTSDSNVFAVGE 277
Cdd:PLN02507 299 APNTkrlnleAVGVE--LDKAGAVKVDEYSRTNIPSIWAIGD 338
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
479-530 |
7.84e-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: 7.84e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 613310046 479 ICGCTDLTRDQIVTQIRAkGLKTSKEVRHVLnfKNKGGCPKCRPAINYYLNM 530
Cdd:pfam04324 2 VCRCFGVTDGEIRDAIRE-GLTTVEEVKRRT--KAGTGCGSCRPAIEEILAE 50
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
4-278 |
5.70e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 56.31 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 4 QKLVMIGNGMAGirtieeiLERANDL----YDITVIGKEPYPNynRIMLSNILQNKMtveetimnPYEWYEEhDIKLITN 79
Cdd:PRK13984 284 KKVAIVGSGPAG-------LSAAYFLatmgYEVTVYESLSKPG--GVMRYGIPSYRL--------PDEALDK-DIAFIEA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 80 DPVvdvdRTNQNVTTANGIEV-----AYDKLIFATG-SKAFVIPVPGSTLPSVIgwRTIDDTEQMMNIA-------KTKK 146
Cdd:PRK13984 346 LGV----KIHLNTRVGKDIPLeelreKHDAVFLSTGfTLGRSTRIPGTDHPDVI--QALPLLREIRDYLrgegpkpKIPR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 147 KAIVIGGGLLGLECARGLLD-QGME-----VTVLHLAEWLMEMqldrkagnmlKADLEK------QGMKFEMQANTTEIL 214
Cdd:PRK13984 420 SLVVIGGGNVAMDIARSMARlQKMEygevnVKVTSLERTFEEM----------PADMEEieegleEGVVIYPGWGPMEVV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 215 GEDD-VEGVKL-------------------ADGREIPADLVVMAVGIRPYTEVAKE---SGLDVNRG-IVVNDVMQTSDS 270
Cdd:PRK13984 490 IENDkVKGVKFkkcvevfdeegrfnpkfdeSDQIIVEADMVVEAIGQAPDYSYLPEelkSKLEFVRGrILTNEYGQTSIP 569
|
....*...
gi 613310046 271 NVFAVGEC 278
Cdd:PRK13984 570 WLFAGGDI 577
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
143-277 |
1.24e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 55.52 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 143 KTKKKAIVIGGGLLGLECARGLLDQGME-VTVLHlaewlmemqldRKAGNMLKADLE------KQGMKFEMQANTTEILG 215
Cdd:PRK12778 568 KFGKKVAVVGGGNTAMDSARTAKRLGAErVTIVY-----------RRSEEEMPARLEevkhakEEGIEFLTLHNPIEYLA 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 216 EDD--VEGVKL---------ADGR-----------EIPADLVVMAVGIRPYTEVAKE-SGLDVNR--GIVVNDVMQTSDS 270
Cdd:PRK12778 637 DEKgwVKQVVLqkmelgepdASGRrrpvaipgstfTVDVDLVIVSVGVSPNPLVPSSiPGLELNRkgTIVVDEEMQSSIP 716
|
....*..
gi 613310046 271 NVFAVGE 277
Cdd:PRK12778 717 GIYAGGD 723
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
20-278 |
1.34e-07 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 55.01 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 20 EEILERANDLYDITVigKEPYPNYNRIMLSNILQNKMTVEETIMNPYEWYEEHDIKLITNDPVVDVDRTNQNVTTANgie 99
Cdd:PTZ00058 131 DKYIRRLNDIYRQNL--KKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQVIEGKN--- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 100 vaydkLIFATGSKafviPVpgstLPSVIGWRTIDDTEQMMNIAKTKKkAIVIGGGLLGLECARGLLDQGMEVTVLHLAEW 179
Cdd:PTZ00058 206 -----ILIAVGNK----PI----FPDVKGKEFTISSDDFFKIKEAKR-IGIAGSGYIAVELINVVNRLGAESYIFARGNR 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 180 LMEmQLDRKAGNMLKADLEKQGMKFEMQANTTEIlGEDDVEGVK--LADGR-EIPADLVVMAVGIRPYTEVAKESGLDVN 256
Cdd:PTZ00058 272 LLR-KFDETIINELENDMKKNNINIITHANVEEI-EKVKEKNLTiyLSDGRkYEHFDYVIYCVGRSPNTEDLNLKALNIK 349
|
250 260
....*....|....*....|....*
gi 613310046 257 RG---IVVNDVMQTSDSNVFAVGEC 278
Cdd:PTZ00058 350 TPkgyIKVDDNQRTSVKHIYAVGDC 374
|
|
| Fer2_BFD |
cd19945 |
bacterioferritin-associated ferredoxin (BFD) [2Fe-2S]-binding domain; This family includes ... |
416-467 |
1.76e-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: 48.35 E-value: 1.76e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 613310046 416 ICGCNGVDKGTIVNAItENGFTTVEEVTAKTKAGNSCGKCKPQIAQILQHTL 467
Cdd:cd19945 3 VCLCNGITDKQIRQAV-AQGATSLRELREQLGVGSQCGKCARMARQVLEEEL 53
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
105-351 |
9.16e-07 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 52.13 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 105 LIFATGSKAFvIP--VPGSTLPSVigwrTIDDteqMMNIAKTKKKAIVIGGGLLGLECARGLLDQGMEVTVlhLAEWLME 182
Cdd:PTZ00052 148 ILIATGGRPS-IPedVPGAKEYSI----TSDD---IFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTV--AVRSIPL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 183 MQLDRKAGNMLKADLEKQGMKFEMQANTTEILGEDDVEGVKLADGREIPADLVVMAVGIRPYTEVAKESGLDV-----NR 257
Cdd:PTZ00052 218 RGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVhvnksNK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 258 GIVVNDVmqTSDSNVFAVGECAEHNGKvyglVAPL-YEQGKVLADHLTN--KETNGYK--GSTTFTSLKVSGCDLYSAGQ 332
Cdd:PTZ00052 298 IIAPNDC--TNIPNIFAVGDVVEGRPE----LTPVaIKAGILLARRLFKqsNEFIDYTfiPTTIFTPIEYGACGYSSEAA 371
|
250
....*....|....*....
gi 613310046 333 IVENAEiKGIEIFNSVDNN 351
Cdd:PTZ00052 372 IAKYGE-DDIEEYLQEFNT 389
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
572-703 |
3.78e-06 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 50.39 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 572 ADQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIWQD-LGMRSASAYGKKTRSVKSCVGKEFCRFGTQYTTRLG 650
Cdd:PRK09566 335 AEDMFELARLAEVYGSGEIRLTVEQNVIIPNIPDENLETFLAEpLLQKFSLEPGPLARGLVSCTGNQYCNFALIETKNRA 414
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613310046 651 IRLEKTFEY-IDTPHKFKMGVSGCPRSCVESGVKDFGVI---------SVEnGFQIYIGGNGG 703
Cdd:PRK09566 415 LALAKELDAeLDLPQPVRIHWTGCPNSCGQPQVADIGLMgtkarkngkTVE-GVDIYMGGKVG 476
|
|
| CopZ-like_Fer2_BFD-like |
cd10141 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of Archaeoglobus ... |
413-455 |
5.49e-06 |
|
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: 44.13 E-value: 5.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 613310046 413 DETICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGN-SC------GKC 455
Cdd:cd10141 1 PKPVCYCFGVTEEDIIEAVAETGATTVEEIRATGKAGRcACevnnpsGRC 50
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
70-276 |
6.44e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 48.76 E-value: 6.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 70 EEHDIKLITNDPVVDVDRTNQN--VTTANGIEVAyDKLIFATGSkaFVIP-VPGStLPSVIGWRTIDDTEQMMNiaktkK 146
Cdd:pfam13738 86 DHFELPINLFEEVTSVKKEDDGfvVTTSKGTYQA-RYVIIATGE--FDFPnKLGV-PELPKHYSYVKDFHPYAG-----Q 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 147 KAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLMEMQLDRKAG------NMLKADLEKQGMKFEMQANTTEILGEDDVE 220
Cdd:pfam13738 157 KVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSlspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVSY 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 221 GVKLADGREIPA-DLVVMAVGIRPYTEVAKESGLDVNRG--IVVND-VMQTSDSNVFAVG 276
Cdd:pfam13738 237 KVHTEDGRKVTSnDDPILATGYHPDLSFLKKGLFELDEDgrPVLTEeTESTNVPGLFLAG 296
|
|
| HyaA_family_Fer2_BFD-like |
cd19951 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of uncharacterized ... |
416-466 |
1.99e-05 |
|
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: 42.48 E-value: 1.99e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 613310046 416 ICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGNSCGKCKPQIAQILQHT 466
Cdd:cd19951 4 VCSCEHVYYQDLIDIIVSCAITSFAELKEFSEAGRVCGRCKKDVDDIIAAS 54
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
92-278 |
2.89e-05 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 47.55 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 92 VTTANGIEVAY--DKLIFATGSKAFVIPvpgSTLPS---VIGWRTIDDTEQMmniaktKKKAIVIGGGLLGLECARGLLD 166
Cdd:PRK07845 128 VTTADGGEETLdaDVVLIATGASPRILP---TAEPDgerILTWRQLYDLDEL------PEHLIVVGSGVTGAEFASAYTE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 167 QGMEVTVLHLAEWLMEMQlDRKAGNMLKADLEKQGMKFEMQ--ANTTEILGeDDVEgVKLADGREIPADLVVMAVGIRPY 244
Cdd:PRK07845 199 LGVKVTLVSSRDRVLPGE-DADAAEVLEEVFARRGMTVLKRsrAESVERTG-DGVV-VTLTDGRTVEGSHALMAVGSVPN 275
|
170 180 190
....*....|....*....|....*....|....*...
gi 613310046 245 TE--VAKESGLDVNRG--IVVNDVMQTSDSNVFAVGEC 278
Cdd:PRK07845 276 TAglGLEEAGVELTPSghITVDRVSRTSVPGIYAAGDC 313
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
146-275 |
2.98e-05 |
|
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: 47.38 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 146 KKAIVIGGGLLGLECARGLLDQGMEVTVLHlaewlmemqlDRKAGNMLKADLEKQGMKFEmqantteiLGEDDVEgvKLA 225
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSD----------DRPAPELAAAELEAPGVEVV--------LGEHPEE--LLD 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 613310046 226 DgreipADLVVMAVGIRPYTEVAKESgldVNRGI-VVNDV---MQTSDSNVFAV 275
Cdd:COG0771 65 G-----ADLVVKSPGIPPDHPLLKAA---RAAGIpVIGEIelaYRLSPAPIIAI 110
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
567-710 |
5.10e-05 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 46.69 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 567 GGVTDADQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIWQD-LGMRSASAYGKKTRSVKSCVGKEFCRFGTQY 645
Cdd:PLN02431 404 VGRLQAADMDELARLADEYGSGELRLTVEQNIIIPNVPNSKVEALLAEpLLQRFSPNPGLLLKGLVACTGNQFCGQAIIE 483
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613310046 646 TTRLGIRLEKTFE-YIDTPHKFKMGVSGCPRSCVESGVKDFGVIS----------VEnGFQIYIGGNGGTEVEKAE 710
Cdd:PLN02431 484 TKARALKVTEELErLVEVPRPVRMHWTGCPNSCGQVQVADIGFMGcmardengkaVE-GADIFVGGRVGSDSHLAE 558
|
|
| NirB_Fer2_BFD-like_1 |
cd19943 |
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
479-524 |
9.33e-05 |
|
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: 40.68 E-value: 9.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 613310046 479 ICGCTDLTRDQIVTQIRAKGLKTSKEVRHVLnfKNKGGCPKCRPAI 524
Cdd:cd19943 6 VCGCNGVSKGAIVQAIQEKGLTTLDEVKACT--KASTSCGGCTPLV 49
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
193-242 |
1.17e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 45.61 E-value: 1.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 613310046 193 LKADLEKQGMKFEMQANTTEILGEDD-VEGVKLADGREIPADLVVMAVGIR 242
Cdd:COG1233 228 LARLAEELGGEIRTGAEVERILVEGGrATGVRLADGEEIRADAVVSNADPA 278
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
103-370 |
3.81e-04 |
|
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: 43.81 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 103 DKLIFATGSKAFVIPVPGSTLpsvigwrTIDDTEQMMnIAKTKKKAIVIGGGLLGLECArGLLD----QGMEVTVLHLAE 178
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGIEH-------CISSNEAFY-LDEPPRRVLTVGGGFISVEFA-GIFNaykpRGGKVTLCYRNN 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 179 WLMEmQLDRKAGNMLKADLEKQGMKFEMQANTTEI-LGEDDVEGVKLADGREIPADLVVMAVGIRPYTEVAK--ESGLDV 255
Cdd:TIGR01423 224 MILR-GFDSTLRKELTKQLRANGINIMTNENPAKVtLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVEL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 256 --NRGIVVNDVMQTSDSNVFAVGECAehnGKVygLVAPL-YEQGKVLADHL-TNK--ETNGYK-GSTTFTSLKVSGCDLy 328
Cdd:TIGR01423 303 tkKGAIQVDEFSRTNVPNIYAIGDVT---DRV--MLTPVaINEGAAFVDTVfGNKprKTDHTRvASAVFSIPPIGTCGL- 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 329 sagqiVENAEIKGIE------------IFNSVDNNYKKIFLK------DGNVVGAVLYGD 370
Cdd:TIGR01423 377 -----VEEDAAKKFEkvavyessftplMHNISGSKYKKFVAKivtnhaDGTVLGVHLLGD 431
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
70-278 |
4.24e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.61 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 70 EEH----DIKLITNDPVVDVDRTNQN--VTTANGIEVAYDKLIFATGSKafvipvpgstlpsvigWRTiddteqmMNIA- 142
Cdd:PRK15317 273 EEHvkeyDVDIMNLQRASKLEPAAGLieVELANGAVLKAKTVILATGAR----------------WRN-------MNVPg 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 143 ----KTK---------------KKAIVIGGGLLGLECARGLLDQGMEVTVLHLAEWLmemqldrKAGNMLKADLEKQG-M 202
Cdd:PRK15317 330 edeyRNKgvaycphcdgplfkgKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPEL-------KADQVLQDKLRSLPnV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 203 KFEMQANTTEILGEDD-VEGVKLAD-----GREIPADLVVMAVGIRPYTEVAKESgLDVN-RG-IVVNDVMQTSDSNVFA 274
Cdd:PRK15317 403 TIITNAQTTEVTGDGDkVTGLTYKDrttgeEHHLELEGVFVQIGLVPNTEWLKGT-VELNrRGeIIVDARGATSVPGVFA 481
|
....
gi 613310046 275 VGEC 278
Cdd:PRK15317 482 AGDC 485
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
138-174 |
4.38e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 43.33 E-value: 4.38e-04
10 20 30
....*....|....*....|....*....|....*..
gi 613310046 138 MMNIAktkkkaiVIGGGLLGLECARGLLDQGMEVTVL 174
Cdd:COG3380 3 MPDIA-------IIGAGIAGLAAARALQDAGHEVTVF 32
|
|
| nirA |
PRK09567 |
NirA family protein; |
572-758 |
4.72e-04 |
|
NirA family protein;
Pssm-ID: 236573 [Multi-domain] Cd Length: 593 Bit Score: 43.46 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 572 ADQLIRLGEVAKKYHVPLVKVTGSQRVGLYGVKKEELPNIwqdlgMRSASAYGKKTR--SVKS----CVGKEFCRFGTQY 645
Cdd:PRK09567 388 TDQMRGLAKIAARYGDGEIRLTVWQNLLISGVPDADVAAV-----EAAIEALGLTTEasSIRAglvaCTGNAGCKFAAAD 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 646 TTR----LGIRLEKTFEyIDTP---HkfkmgVSGCPRSCVESGVKDFGVI----------SVEnGFQIYIGGNGGTEVEK 708
Cdd:PRK09567 463 TKGhalaIADYCEPRVA-LDQPvniH-----LTGCHHSCAQHYIGDIGLIgakvavsegdTVE-GYHIVVGGGFGEDAAI 535
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 613310046 709 A-EFLTTVETEDeVIKLCGALMQYYRetgiyAERTAP------WLRRLGFENVKEVL 758
Cdd:PRK09567 536 GrEVFRDVKAED-APRLVERLLRAYL-----AHRQGPdetfqaFTRRHDPEALRSLA 586
|
|
| nirA |
PRK09566 |
ferredoxin-nitrite reductase; Reviewed |
557-749 |
6.68e-04 |
|
ferredoxin-nitrite reductase; Reviewed
Pssm-ID: 236572 [Multi-domain] Cd Length: 513 Bit Score: 43.07 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 557 GTFSVIPQMRGGVTDADQLIRLGEVAKKY-HVPLVKVTGSQRVGLYGVKKEELPNIWQDL---GMRSASAYGKKTRSVK- 631
Cdd:PRK09566 64 GKFMLRLRVPNGILTSEQLRVLASIVQRYgDDGSADITTRQNLQLRGILLEDLPEILNRLkavGLTSVQSGMDNVRNITg 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 632 SCV----GKEFcrFGTQ-YTTRLGIRL----EKTFEYIDTPHKFKMGVSGCPRSCVESGVKDFGVISVEN----GFQIYI 698
Cdd:PRK09566 144 SPVagidPDEL--IDTRpLTQKLQDMLtnngEGNPEFSNLPRKFNIAIAGGRDNSVHAEINDIAFVPAYKdgvlGFNVLV 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 613310046 699 GGN-GGTEVEKAEFLTTVETEDEVIKLCGALMQYYRETGIYAERTAPWLRRL 749
Cdd:PRK09566 222 GGFfSSQRCAYAIPLNAWVKPDEVVRLCRAILEVYRDNGLRANRQKGRLMWL 273
|
|
| GlpA-like_Fer2_BFD-like |
cd19946 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of anaerobic ... |
416-465 |
1.08e-03 |
|
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: 37.90 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 613310046 416 ICGCNGVDKGTIVNAITENGFTTVEEVTAKTKAGN-SC--GKCKPQIAQILQH 465
Cdd:cd19946 3 VCRCEEVTEGEIRDAIRRGAARDLDGLKRRTRAGMgRCqgRFCAPRVAELLAR 55
|
|
| PLN02431 |
PLN02431 |
ferredoxin--nitrite reductase |
548-784 |
1.57e-03 |
|
ferredoxin--nitrite reductase
Pssm-ID: 178050 [Multi-domain] Cd Length: 587 Bit Score: 42.07 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 548 RYHANIQNDGTFSVIPQMRGGVTDADQLIRLGEVAKKYHVP-LVKVTGSQRVGLYGVKKEELPNIWQDLGMRSASAYGKK 626
Cdd:PLN02431 126 LFHRRKHQYGRFMMRLKLPNGVTTSAQTRYLASVIEKYGEDgCADVTTRQNWQIRGVVLPDVPAILKGLEEVGLTSLQSG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 627 TRSVKSCVG--------------KEFCRFGTQYTTRLGirlEKTFEYIDTPHKFKMGVSGCPRSCVESGVKDFGVISV-- 690
Cdd:PLN02431 206 MDNVRNPVGnplagidpheivdtRPYTNLLSDYITNNG---RGNPEITNLPRKWNVCVVGSHDLFEHPHINDLAYMPAtk 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 691 --ENGFQIYIGGNGGTE-VEKAEFLTTVETEDEVIKLCGALMQYYRETGIYAERTAP---WLrrlgfenVKEVLLDPERQ 764
Cdd:PLN02431 283 dgRFGFNLLVGGFFSPKrCAEAIPLDAWVPADDVVPLCKAILEAFRDLGTRGNRQKTrmmWL-------IDELGVEGFRS 355
|
250 260
....*....|....*....|....*.
gi 613310046 765 nELFERIMDAKKAVEAE------PWE 784
Cdd:PLN02431 356 -EVEKRMPNGELERAASedlvdkKWE 380
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
92-173 |
5.86e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 39.66 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613310046 92 VTTANGIEVAYDKLIFATGSKAFVIPVPGSTLPSVIG-------WRTIDDTEQMMNIAKTKKKAIVIGGGLLGLECARGL 164
Cdd:COG0569 35 VTTLGGGLLDPVTLVAAIFLIGVVIIPLGYTLITFGDavlfgglLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLAREL 114
|
....*....
gi 613310046 165 LDQGMEVTV 173
Cdd:COG0569 115 EEEGHDVVV 123
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
138-174 |
8.80e-03 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 39.45 E-value: 8.80e-03
10 20 30
....*....|....*....|....*....|....*..
gi 613310046 138 MMniaktKKKAIVIGGGLLGLECARGLLDQGMEVTVL 174
Cdd:COG3349 1 MM-----PPRVVVVGGGLAGLAAAVELAEAGFRVTLL 32
|
|
| |
