|
Name |
Accession |
Description |
Interval |
E-value |
| glcF |
PRK11274 |
glycolate oxidase subunit GlcF; |
1-417 |
0e+00 |
|
glycolate oxidase subunit GlcF;
Pssm-ID: 236890 [Multi-domain] Cd Length: 407 Bit Score: 837.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 1 MQTNLADFLRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKQVLEGHAITESTRLHLDRCLTCRN 80
Cdd:PRK11274 1 MQTNLADFIRDTPEGEEAEAILRKCVHCGFCTATCPTYQLLGDELDGPRGRIYLIKQVLEGAEVTEKTQLHLDRCLTCRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 81 CESTCPSGVRYGRLVDIGRKLVDDKleaegVQRPARERIARWVLREGLTRPALFGTALRLGQMVRPLLPGTLRNKVPAls 160
Cdd:PRK11274 81 CETTCPSGVQYGRLLDIGRKVVEEK-----VPRPLGERLLRWGLREVLPRPALFGPLMRLGQAVRPLLPEALRAKVPA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 161 sTAAPGTWPRNAHARKMLLLDGCVQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMRRNIDAW 240
Cdd:PRK11274 154 -RQPAAPWPPPRHARRVLMLEGCVQPAMSPNINAATARVLDRLGISLVVAPEAGCCGAVRYHLNAQEGGLARMRRNIDAW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 241 WPHIEDGAEAIVMTASGCGAMVKDYGHLLRNDPKYAERARRVSALTRDLSEVLPDFADELHTLAGAVPrdnRRVAYHPPC 320
Cdd:PRK11274 233 WPAIEAGAEAIVMTASGCGATVKEYGHLLRDDPAYAEKAARVSALTRDLSELLPAEPLELLALLGRPD---RRVAFHPPC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 321 TLQHGQQIRGKVEALLTGLGVEVKLCADSHLCCGSAGTYSVLQPELAYRLRDDKLAKLQATQPEAIVSANIGCIAHLQGG 400
Cdd:PRK11274 310 TLQHGQKLRGKVERLLTRLGFELTLVADSHLCCGSAGTYSLLQPELSYQLRDNKLAALEAGKPEVIVTANIGCQTHLQSG 389
|
410
....*....|....*..
gi 499935255 401 TGTPVMHWIELVDKMLG 417
Cdd:PRK11274 390 TRTPVRHWIELVDEALA 406
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
4-417 |
4.93e-112 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 335.12 E-value: 4.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 4 NLADFLRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKQVLEGHA---ITESTRLHLDRCLTCRN 80
Cdd:COG0247 59 DLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELpldLSEEVYEVLDLCLTCKA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 81 CESTCPSGVRYGRLVDIGRklvdDKLEAEGvQRPARERIARwvlregltrpalfgtalrlgqmvrpllpgTLRNKVPAls 160
Cdd:COG0247 139 CETACPSGVDIADLIAEAR----AQLVERG-GRPLRDRLLR-----------------------------TFPDRVPA-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 161 staapgtwpRNAHARKMLLLDGCVQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMRRNIDAW 240
Cdd:COG0247 183 ---------ADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 241 WPHiedGAEAIVMTASGCGAMVKD-YGHLLRNdpkyaerarRVSALTRDLSEVLpdfADELHTLAGAVPRDNRRVAYHPP 319
Cdd:COG0247 254 ERL---GVKAIVTTCPSCGLTLKDeYPELLGD---------RVAFEVLDISEFL---AELILEGKLKLKPLGEKVTYHDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 320 CTLQHGQQIRGKVEALLTGL-GVEVKLCADSHLCCGSAGTYSVLQPELAYRLRDDKLAKLQATQPEAIVSANIGCIAHLQ 398
Cdd:COG0247 319 CHLGRGGGVYDAPRELLKAIpGVEVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRATGADVVVTACPSCRTQLE 398
|
410 420
....*....|....*....|..
gi 499935255 399 GGT---GTPVMHWIELVDKMLG 417
Cdd:COG0247 399 DGTkeyGIEVKHPVELLAEALG 420
|
|
| CCG |
pfam02754 |
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ... |
314-397 |
6.97e-13 |
|
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.
Pssm-ID: 397052 [Multi-domain] Cd Length: 84 Bit Score: 63.87 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 314 VAYHPPCTLQHG--QQIRGKVEALLTGLGVEVKLcADSHLCCGSAGTYSVlQPELAYRLRDDKLAKLQATQPEAIVSANI 391
Cdd:pfam02754 1 VAYFDGCHLGRAlyPEPRKALKKVLGALGVEVVI-LEKQSCCGAGGGFSG-KEDVAEALAKRNIDTAEETGADAIVTACP 78
|
....*.
gi 499935255 392 GCIAHL 397
Cdd:pfam02754 79 GCLLQL 84
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
9-99 |
3.50e-07 |
|
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
Pssm-ID: 273049 [Multi-domain] Cd Length: 220 Bit Score: 50.89 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 9 LRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELdGPRGRIYLMKQVLEGHAITESTRLH-------LDRCLTCRNC 81
Cdd:TIGR00384 124 FLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL-GPAALTAAYRFLIDSRDHATKDRLEglndkngVWRCTTCMNC 202
|
90
....*....|....*...
gi 499935255 82 ESTCPSGVRYGRLVDIGR 99
Cdd:TIGR00384 203 SEVCPKGVNPARAIEKLK 220
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
9-90 |
5.67e-05 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 45.48 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 9 LRNTPEGEEAKSIVGNCVHCGFCTATCPtyqllgDELDGPRGriylMKQVLEGHaITESTRLHlDRCLTCRNCESTCPSG 88
Cdd:cd01916 351 EKKLPTDEEFQELAAKCTDCGWCTRACP------NSLRIKEA----MEAAKEGD-FSGLADLF-DQCVGCGRCEQECPKE 418
|
..
gi 499935255 89 VR 90
Cdd:cd01916 419 IP 420
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glcF |
PRK11274 |
glycolate oxidase subunit GlcF; |
1-417 |
0e+00 |
|
glycolate oxidase subunit GlcF;
Pssm-ID: 236890 [Multi-domain] Cd Length: 407 Bit Score: 837.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 1 MQTNLADFLRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKQVLEGHAITESTRLHLDRCLTCRN 80
Cdd:PRK11274 1 MQTNLADFIRDTPEGEEAEAILRKCVHCGFCTATCPTYQLLGDELDGPRGRIYLIKQVLEGAEVTEKTQLHLDRCLTCRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 81 CESTCPSGVRYGRLVDIGRKLVDDKleaegVQRPARERIARWVLREGLTRPALFGTALRLGQMVRPLLPGTLRNKVPAls 160
Cdd:PRK11274 81 CETTCPSGVQYGRLLDIGRKVVEEK-----VPRPLGERLLRWGLREVLPRPALFGPLMRLGQAVRPLLPEALRAKVPA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 161 sTAAPGTWPRNAHARKMLLLDGCVQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMRRNIDAW 240
Cdd:PRK11274 154 -RQPAAPWPPPRHARRVLMLEGCVQPAMSPNINAATARVLDRLGISLVVAPEAGCCGAVRYHLNAQEGGLARMRRNIDAW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 241 WPHIEDGAEAIVMTASGCGAMVKDYGHLLRNDPKYAERARRVSALTRDLSEVLPDFADELHTLAGAVPrdnRRVAYHPPC 320
Cdd:PRK11274 233 WPAIEAGAEAIVMTASGCGATVKEYGHLLRDDPAYAEKAARVSALTRDLSELLPAEPLELLALLGRPD---RRVAFHPPC 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 321 TLQHGQQIRGKVEALLTGLGVEVKLCADSHLCCGSAGTYSVLQPELAYRLRDDKLAKLQATQPEAIVSANIGCIAHLQGG 400
Cdd:PRK11274 310 TLQHGQKLRGKVERLLTRLGFELTLVADSHLCCGSAGTYSLLQPELSYQLRDNKLAALEAGKPEVIVTANIGCQTHLQSG 389
|
410
....*....|....*..
gi 499935255 401 TGTPVMHWIELVDKMLG 417
Cdd:PRK11274 390 TRTPVRHWIELVDEALA 406
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
4-417 |
4.93e-112 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 335.12 E-value: 4.93e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 4 NLADFLRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKQVLEGHA---ITESTRLHLDRCLTCRN 80
Cdd:COG0247 59 DLHDKNLKTLPWKELLDALDACVGCGFCRAMCPSYKATGDEKDSPRGRINLLREVLEGELpldLSEEVYEVLDLCLTCKA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 81 CESTCPSGVRYGRLVDIGRklvdDKLEAEGvQRPARERIARwvlregltrpalfgtalrlgqmvrpllpgTLRNKVPAls 160
Cdd:COG0247 139 CETACPSGVDIADLIAEAR----AQLVERG-GRPLRDRLLR-----------------------------TFPDRVPA-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 161 staapgtwpRNAHARKMLLLDGCVQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMRRNIDAW 240
Cdd:COG0247 183 ---------ADKEGAEVLLFPGCFTNYFDPEIGKAAVRLLEAAGVEVVLPPEELCCGAPALSKGDLDLARKLARRNIEAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 241 WPHiedGAEAIVMTASGCGAMVKD-YGHLLRNdpkyaerarRVSALTRDLSEVLpdfADELHTLAGAVPRDNRRVAYHPP 319
Cdd:COG0247 254 ERL---GVKAIVTTCPSCGLTLKDeYPELLGD---------RVAFEVLDISEFL---AELILEGKLKLKPLGEKVTYHDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 320 CTLQHGQQIRGKVEALLTGL-GVEVKLCADSHLCCGSAGTYSVLQPELAYRLRDDKLAKLQATQPEAIVSANIGCIAHLQ 398
Cdd:COG0247 319 CHLGRGGGVYDAPRELLKAIpGVEVVEMPEDSGCCGGAGGYGFEEPELSMRIGERKLEQIRATGADVVVTACPSCRTQLE 398
|
410 420
....*....|....*....|..
gi 499935255 399 GGT---GTPVMHWIELVDKMLG 417
Cdd:COG0247 399 DGTkeyGIEVKHPVELLAEALG 420
|
|
| glpC |
PRK11168 |
anaerobic glycerol-3-phosphate dehydrogenase subunit C; |
24-359 |
1.20e-24 |
|
anaerobic glycerol-3-phosphate dehydrogenase subunit C;
Pssm-ID: 236869 [Multi-domain] Cd Length: 396 Bit Score: 104.57 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 24 NCVHCGFCTATCP----TYQLLGDELDGPRGRIYLMKqvlEGHAITEStrlhLDRCLTCRNCESTCPSGVRYGRLVDIGR 99
Cdd:PRK11168 8 SCIKCTVCTTACPvarvNPLYPGPKQAGPDGERLRLK---DGALYDES----LKYCSNCKRCEVACPSGVKIGDIIQRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 100 -KLVDDKLEaegvqrPARERIarwvlregLTRPALFGtalRLGQMVRPLLPGTLRNKV-----------------PALSS 161
Cdd:PRK11168 81 aKYVTERGP------PLRDRI--------LSHTDLMG---SLATPFAPLVNAATGLKPvrwllektlgidhrrplPKYAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 162 TAAPGTWPRNAHAR-----KMLLLDGCVQPAMSPNINAATARVFDRVGVQLLVAREaGCCGAIRFHTGDHDGGLDNMRRN 236
Cdd:PRK11168 144 GTFRRWYRKQAAQQaqykkQVAYFHGCYVNYNHPQLGKDLVKVLNAMGYEVLLPKE-KCCGLPLIANGFLDKARKQAEFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 237 IDAWWPHIEDGAeAIVMTASGCGAMVKD-YGHLLR-NDPKYAERarrvsalTRDLSEVLPDFADELHTLAGAvpRDNRRV 314
Cdd:PRK11168 223 VESLREAIEKGI-PVIATSSSCTLTLRDeYPELLGvDNAGVRDH-------IEDATEFLRRLLDQGKLLPLK--PLPLKV 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499935255 315 AYHPPCTLQhGQQIRGKVEALLTGL-GVEVKLCADShlCCGSAGTY 359
Cdd:PRK11168 293 AYHTPCHLE-KQGWGLYTLELLRLIpGLEVVVLDSQ--CCGIAGTY 335
|
|
| PRK06259 |
PRK06259 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional |
7-414 |
3.67e-24 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
Pssm-ID: 235756 [Multi-domain] Cd Length: 486 Bit Score: 104.32 E-value: 3.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 7 DFLRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLlgDELDGPrgriYLMKQVL--------EGHAITESTRLHLDRCLTC 78
Cdd:PRK06259 117 NEKITYPEDIEDIKKLRGCIECLSCVSTCPARKV--SDYPGP----TFMRQLArfafdprdEGDREKEAFDEGLYNCTTC 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 79 RNCESTCPsgvrygRLVDIGRKLVDdKLEA----EGVQRPARERIARWVLREGLTRPalfgtalrlgQMVRPLLPgtlrn 154
Cdd:PRK06259 191 GKCVEVCP------KEIDIPGKAIE-KLRAlafkKGLGLPAHLEVRENVLKTGRSVP----------KEKPSFLE----- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 155 kvpalsstAAPGTWPRNAHARKMLLLDGCVQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMR 234
Cdd:PRK06259 249 --------EVSDIYPYGNEKLRVAFFTGCLVDYRLQEVGKDAIRVLNAHGISVIIPKNQVCCGSPLIRTGQTDVAEELKK 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 235 RNIDAWwphIEDGAEAIVMTASGCGAMVKdyghllrNDpkYAERARRVsaltRDLSEVLPDFADELHTlagavpRDNRRV 314
Cdd:PRK06259 321 KNLEIF---NKLDVDTVVTICAGCGSTLK-------ND--YKEKEFNV----MDITEVLVEVGLEKYK------PLDITV 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 315 AYHPPCTLQHGQQIRGKVEALLTGLG----VEVKLCADshlCCGSAGTYSVLQPELAYRLRDDKLAKLQATQPEAIVSAN 390
Cdd:PRK06259 379 TYHDPCHLRRGQGIYEEPRKILRSIPglefVEMEIPDQ---CCGAGGGVRSGKPEIAEALGKRKAEMIRETGADYVITVC 455
|
410 420
....*....|....*....|....*....
gi 499935255 391 IGCIAHLQ-----GGTGTPVMHWIELVDK 414
Cdd:PRK06259 456 PFCEYHIRdslkkYSEDIPVMNIVSLLDK 484
|
|
| CCG |
pfam02754 |
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ... |
314-397 |
6.97e-13 |
|
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.
Pssm-ID: 397052 [Multi-domain] Cd Length: 84 Bit Score: 63.87 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 314 VAYHPPCTLQHG--QQIRGKVEALLTGLGVEVKLcADSHLCCGSAGTYSVlQPELAYRLRDDKLAKLQATQPEAIVSANI 391
Cdd:pfam02754 1 VAYFDGCHLGRAlyPEPRKALKKVLGALGVEVVI-LEKQSCCGAGGGFSG-KEDVAEALAKRNIDTAEETGADAIVTACP 78
|
....*.
gi 499935255 392 GCIAHL 397
Cdd:pfam02754 79 GCLLQL 84
|
|
| HdrB |
COG2048 |
Heterodisulfide reductase, subunit B [Energy production and conversion]; |
182-412 |
7.39e-13 |
|
Heterodisulfide reductase, subunit B [Energy production and conversion];
Pssm-ID: 441651 [Multi-domain] Cd Length: 285 Bit Score: 68.69 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 182 GCVQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMRRNIDAwwphiedgAEA----IVMTASG 257
Cdd:COG2048 8 GCSLPGTAPEYEKSTRAVAKALGIELVELPDWNCCGASSAHSVDELLWLALAARNLAL--------AEKmgldIVTPCNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 258 CGAMVKDYGHLLRNDPKYAERARRVSALT----------RDLSEVLPDFADeLHTLAGAV--PRDNRRVAYHPPCTLQHG 325
Cdd:COG2048 80 CYGSLKEANHELKEDPELREKVNEILAEAgleykgtvkvRHLLEVLYEDVG-LEKIKEKVkkPLKGLKVAPYYGCHLLRP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 326 QQIRG--------KVEALLTGLGVEV-----KLcadshLCCGSAGTYSvlQPELAYRLRDDKLAKLQATQPEAIVSANIG 392
Cdd:COG2048 159 SEIAGfddpenptSLDELVEALGAEPvdypyKT-----ECCGASLRLS--NPEVSLKLTGKILESAKEAGADAIVTACPL 231
|
250 260 270
....*....|....*....|....*....|...
gi 499935255 393 CiaHLQ-----------GGT--GTPVMHWIELV 412
Cdd:COG2048 232 C--HLNldmyqpeinkkFGTefNIPVLYFTQLL 262
|
|
| CCG |
pfam02754 |
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif ... |
181-262 |
1.12e-11 |
|
Cysteine-rich domain; The key element of this family is the CX31-38CCX33-34CXXC sequence motif normally found at the C-terminus in archaeal and bacterial Hdr-like proteins. There may be one or two copies, and the motif is probably an iron-sulfur binding cluster. In some instances one of the cysteines is replaced by an aspartate, and aspartate can in principle also function as a ligand of an iron-sulfur cluster. The family includes a subunit from heterodisulphide reductase and a subunit from glycolate oxidase and glycerol-3-phosphate dehydrogenase.
Pssm-ID: 397052 [Multi-domain] Cd Length: 84 Bit Score: 60.40 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 181 DGC-VQPAMSPNINAATARVFDRVGVQLLVAREAGCCGAIRFHTGDHDGGLDNMRRNIDAWWphiEDGAEAIVMTASGCG 259
Cdd:pfam02754 5 DGChLGRALYPEPRKALKKVLGALGVEVVILEKQSCCGAGGGFSGKEDVAEALAKRNIDTAE---ETGADAIVTACPGCL 81
|
...
gi 499935255 260 AMV 262
Cdd:pfam02754 82 LQL 84
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
24-89 |
1.26e-09 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 433017 [Multi-domain] Cd Length: 64 Bit Score: 53.85 E-value: 1.26e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499935255 24 NCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKqvLEGHAITESTRLHLDRCLTCRNCESTCPSGV 89
Cdd:pfam13183 1 RCIRCGACLAACPVYLVTGGRFPGDPRGGAAAL--LGRLEALEGLAEGLWLCTLCGACTEVCPVGI 64
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
25-89 |
3.07e-09 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 52.53 E-value: 3.07e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499935255 25 CVHCGFCTATCPTYQLLGDELDGPRGRiylmkqvleghaitESTRLHLDRCLTCRNCESTCPSGV 89
Cdd:pfam12838 1 CIGCGACVAACPVGAITLDEVGEKKGT--------------KTVVIDPERCVGCGACVAVCPTGA 51
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
24-89 |
2.17e-08 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 50.54 E-value: 2.17e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499935255 24 NCVHCGFCTATCPTYQLLGDELDGPRGRIYLmkQVLEGHAITEStrlhLDRCLTCRNCESTCPSGV 89
Cdd:pfam13534 1 RCIQCGCCVDECPRYLLNGDEPKKLMRAAYL--GDLEELQANKV----ANLCSECGLCEYACPMGL 60
|
|
| dhsB |
TIGR00384 |
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ... |
9-99 |
3.50e-07 |
|
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]
Pssm-ID: 273049 [Multi-domain] Cd Length: 220 Bit Score: 50.89 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 9 LRNTPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELdGPRGRIYLMKQVLEGHAITESTRLH-------LDRCLTCRNC 81
Cdd:TIGR00384 124 FLQTPEQREKLDQLSGCILCGCCYSSCPAFWWNPEFL-GPAALTAAYRFLIDSRDHATKDRLEglndkngVWRCTTCMNC 202
|
90
....*....|....*...
gi 499935255 82 ESTCPSGVRYGRLVDIGR 99
Cdd:TIGR00384 203 SEVCPKGVNPARAIEKLK 220
|
|
| HdrC |
COG1150 |
Heterodisulfide reductase, subunit C [Energy production and conversion]; |
22-101 |
4.87e-07 |
|
Heterodisulfide reductase, subunit C [Energy production and conversion];
Pssm-ID: 440764 [Multi-domain] Cd Length: 79 Bit Score: 47.20 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 22 VGNCVHCGFCTATCPTYQllGDELDgPRGRIYLM-----KQVLEGHAITestrlhldRCLTCRNCESTCPSGVRYGRLVD 96
Cdd:COG1150 2 LKKCYQCGTCTASCPVAR--AMDYN-PRKIIRLAqlglkEEVLKSDSIW--------LCVSCYTCTERCPRGIDIADVMD 70
|
....*
gi 499935255 97 IGRKL 101
Cdd:COG1150 71 ALRNL 75
|
|
| PRK12575 |
PRK12575 |
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; |
12-95 |
2.83e-06 |
|
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
Pssm-ID: 171592 [Multi-domain] Cd Length: 235 Bit Score: 48.03 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 12 TPEGEEAKSIVGNCVHCGFCTATCPTYQLLGDELDGPRGRIYLMKQVLEGHAITESTRL-------HLDRCLTCRNCEST 84
Cdd:PRK12575 133 TPQEREQLDGLYECILCACCSTACPSYWWNPDKFVGPAGLLQAYRFIADSRDDATAARLddledpyRLFRCRTIMNCVDV 212
|
90
....*....|.
gi 499935255 85 CPSGVRYGRLV 95
Cdd:PRK12575 213 CPKGLNPARAI 223
|
|
| ACS_1 |
cd01916 |
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and ... |
9-90 |
5.67e-05 |
|
Acetyl-CoA synthase (ACS), also known as acetyl-CoA decarbonylase, is found in acetogenic and methanogenic organisms and is responsible for the synthesis and breakdown of acetyl-CoA. ACS forms a heterotetramer with carbon monoxide dehydrogenase (CODH) consisting of two ACS and two CODH subunits. CODH reduces carbon dioxide to carbon monoxide and ACS then synthesizes acetyl-CoA from carbon monoxide, CoA, and a methyl group donated by another protein (CoFeSP). ACS has three structural domains, an N-terminal rossman fold domain with a helical region at its N-terminus which interacts with CODH, and two alpha + beta fold domains. A Ni-Fe-S center referred to as the A-cluster is located in the C-terminal domain. A large cavity exists between the three domains which may bind CoA.
Pssm-ID: 238897 [Multi-domain] Cd Length: 731 Bit Score: 45.48 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499935255 9 LRNTPEGEEAKSIVGNCVHCGFCTATCPtyqllgDELDGPRGriylMKQVLEGHaITESTRLHlDRCLTCRNCESTCPSG 88
Cdd:cd01916 351 EKKLPTDEEFQELAAKCTDCGWCTRACP------NSLRIKEA----MEAAKEGD-FSGLADLF-DQCVGCGRCEQECPKE 418
|
..
gi 499935255 89 VR 90
Cdd:cd01916 419 IP 420
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
25-86 |
3.11e-04 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 38.39 E-value: 3.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499935255 25 CVHCGFCTATCPTYQllgdELDGPRGRIYLMKQVLEGhaitestrlhLDRCLTCRNCESTCP 86
Cdd:pfam13237 9 CIGCGRCTAACPAGL----TRVGAIVERLEGEAVRIG----------VWKCIGCGACVEACP 56
|
|
| PLN00129 |
PLN00129 |
succinate dehydrogenase [ubiquinone] iron-sulfur subunit |
25-88 |
4.53e-04 |
|
succinate dehydrogenase [ubiquinone] iron-sulfur subunit
Pssm-ID: 215067 [Multi-domain] Cd Length: 276 Bit Score: 41.70 E-value: 4.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499935255 25 CVHCGFCTATCPTYQLLGDELDGPR-----------GRIYLMKQVLEghAITESTRLHldRCLTCRNCESTCPSG 88
Cdd:PLN00129 189 CILCACCSTSCPSYWWNPEKFLGPAallhayrwisdSRDEYTKERLE--ALDDEFKLY--RCHTIRNCSNACPKG 259
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
25-88 |
1.47e-03 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 38.53 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499935255 25 CVHCGFCTATCPTyqllgdeldgprGRIYLMKQVLEGHAITESTRLHLDRCLTCRNCESTCPSG 88
Cdd:cd10549 42 CVFCGACVEVCPT------------GAIELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVD 93
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
25-89 |
8.53e-03 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 36.22 E-value: 8.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499935255 25 CVHCGFCTATCPTyqllgdeldgprGRIylmkQVLEGHAITESTRLHLDRCLTCRNCESTCPSGV 89
Cdd:cd10549 8 CIGCGICVKACPT------------DAI----ELGPNGAIARGPEIDEDKCVFCGACVEVCPTGA 56
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
24-88 |
9.24e-03 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 34.71 E-value: 9.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499935255 24 NCVHCGFCTATCPTyqllgdeldgprgriylmkqvlegHAITEST---RLHLDRCLTCRNCESTCPSG 88
Cdd:COG2768 12 KCIGCGACVKVCPV------------------------GAISIEDgkaVIDPEKCIGCGACIEVCPVG 55
|
|
| |
