ID HDRA_METJA Reviewed; 657 AA. AC P60200; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 02-SEP-2026, entry version 106. DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000305}; DE EC=1.8.98.- {ECO:0000305}; GN Name=hdrA; OrderedLocusNames=MJ1190; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM OS 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanococci; Methanococcales; Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L., RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-196. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element of RT Methanococcus jannaschii probably directing selenocysteine insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- FUNCTION: Part of a complex that catalyzes the reversible reduction of CC CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB CC (coenzyme B). {ECO:0000250|UniProtKB:Q6LWL2}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711}; CC Note=Binds 4 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00711}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:Q8TM02}; CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide CC reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B CC heterodisulfide: step 1/1. {ECO:0000250|UniProtKB:Q6LWL2}. CC -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed CC of three subunits; HdrA, HdrB and HdrC. {ECO:0000250|UniProtKB:Q6LWL2}. CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; WP_162484757.1; NC_000909.1. DR FunCoup; P60200; 2. DR GeneID; 1452597; -. DR InParanoid; P60200; -. DR OrthoDB; 32867at2157; -. DR PhylomeDB; P60200; -. DR BRENDA; 1.8.7.3; 3260. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IDA:MENGO. DR FunFam; 3.30.70.20:FF:000076; CoB--CoM heterodisulfide reductase iron-sulfur subunit A; 1. DR Gene3D; 3.30.70.20; -; 3. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR039650; HdrA-like. DR PANTHER; PTHR43498:SF1; COB--COM HETERODISULFIDE REDUCTASE IRON-SULFUR SUBUNIT A; 1. DR PANTHER; PTHR43498; FERREDOXIN:COB-COM HETERODISULFIDE REDUCTASE SUBUNIT A; 1. DR Pfam; PF12831; FAD_oxidored; 1. DR Pfam; PF14697; Fer4_21; 1. DR Pfam; PF13187; Fer4_9; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 4. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat; Selenocysteine. FT CHAIN 1..657 FT /note="CoB--CoM heterodisulfide reductase iron-sulfur FT subunit A" FT /id="PRO_0000150057" FT DOMAIN 235..266 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 283..312 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 574..603 FT /note="4Fe-4S ferredoxin-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 607..636 FT /note="4Fe-4S ferredoxin-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 149..172 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" FT BINDING 245 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 248 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 251 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 255 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 292 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 295 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 298 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 302 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 583 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 586 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 589 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 593 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 616 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 619 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 622 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 626 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT NON_STD 196 FT /note="Selenocysteine" FT /evidence="ECO:0000305" SQ SEQUENCE 657 AA; 71922 MW; D3607042434DBC32 CRC64; MSPRVGVFVC YCGANINGVV DCEAVRDFAE KLDGVVVAKT YPFMCADPGQ NLIKEAIKEY NLDRVVVAAC TPKIHEPTFR NCIKEAGLSP YYLEFVNIRE HCSFVHMNDR EKATKKAMEL VAGAVERAKR LEDVPQKIVE VDKSCLIIGG GIAGIQAALD LGDQGYKVYL VEKEPSIGGR MAQLAKTFPT DDCALUILAP KMVSVANHPN VELITYAEVK NVEGFIGNFE VTIEKKPRYV DENICTGCGA CAAVCPIEVP NEFDLGLGTR KAIYVPFAQA VPLVYTIDMD HCIRCGLCEK ACGPGAIRYD QKPEEIKLKV GTIICAVGYD EFDATLKEEY GYGVYDNVIT TLELERMINP AGPTGGHEIR PSDGKHPHRV VFIQCVGSRD AKVGKHYCSR ICCMFALKNA QLIKQHDPST EVYICYMDIR SFGKGYEEYY RRAQEQFGVK FIRGRPACIM EDPETKNLIV RVEDTLLGEI VEIEADLVVL SAGLSPRPDN PKLAKMLGLE LSPDGFFKEL HPKLAPVNTK VDGIAIAGVA QGPKDIPDTV AQAKGAASAV SIPMAQGQFR IEMIRAVVDE DVCGGCQVCA KMCPYNAITY VEKDGHLVAQ VNDVACKGCG SCAGACPSGA MQLRYYRDEQ IISFIDGVLE AHQKLES //