ID HDRA2_METKA Reviewed; 656 AA. AC P96801; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 02-SEP-2026, entry version 141. DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2 {ECO:0000305}; DE EC=1.8.98.- {ECO:0000305}; GN Name=hdrA2; Synonyms=hdrA_2; OrderedLocusNames=MK0265; OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanopyri; Methanopyrales; Methanopyraceae; Methanopyrus. OX NCBI_TaxID=190192; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9063468; DOI=10.1111/j.1432-1033.1997.00226.x; RA Kuenkel A., Vaupel M., Heim S., Thauer R.K., Hedderich R.; RT "Heterodisulfide reductase from methanol-grown cells of Methanosarcina RT barkeri is not a flavoenzyme."; RL Eur. J. Biochem. 244:226-234(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; RX PubMed=11930014; DOI=10.1073/pnas.032671499; RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., RA Koonin E.V., Kozyavkin S.A.; RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and RT monophyly of archaeal methanogens."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002). 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; Y09871; CAA70999.1; -; Genomic_DNA. DR EMBL; AE009439; AAM01482.1; -; Genomic_DNA. DR RefSeq; WP_011018637.1; NC_003551.1. DR AlphaFoldDB; P96801; -. DR SMR; P96801; -. DR STRING; 190192.MK0265; -. DR PaxDb; 190192-MK0265; -. DR EnsemblBacteria; AAM01482; AAM01482; MK0265. DR GeneID; 1477568; -. DR KEGG; mka:MK0265; -. DR PATRIC; fig|190192.8.peg.268; -. DR HOGENOM; CLU_020302_0_0_2; -. DR InParanoid; P96801; -. DR OrthoDB; 32867at2157; -. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000001826; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-ARBA. DR FunFam; 3.50.50.60:FF:000644; H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A; 1. DR Gene3D; 3.30.70.20; -; 3. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2. 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; PF12838; Fer4_7; 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; 3. 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. FT CHAIN 1..656 FT /note="CoB--CoM heterodisulfide reductase iron-sulfur FT subunit A 2" FT /id="PRO_0000150059" FT DOMAIN 238..269 FT /note="4Fe-4S ferredoxin-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 286..315 FT /note="4Fe-4S ferredoxin-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 577..606 FT /note="4Fe-4S ferredoxin-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT DOMAIN 610..639 FT /note="4Fe-4S ferredoxin-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 152..175 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255" 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 254 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 258 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 301 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 305 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" 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 592 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 596 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 625 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" FT BINDING 629 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711" SQ SEQUENCE 656 AA; 71925 MW; C7CF218545ACEA7C CRC64; MAEEEPRIGV YVCHCGVNIA GVVDVKEVAE FAKTLKNVVV ARDYKYVCSD PGQEIIQRDI EKYDLNRVVV AACSPRLHEP TFRRCVEEAG LNPYCFEMAN IREHCSWVHM DDPARATEKA KDLVRMAVAK ARLLESLETI KVDVTDRALV IGGGVSGIQA ALDLADMGFE VILVEKEPSI GGRMAQLDKT FPTNDCSICI LAPKMVDVSK HPNIKMYTYA EVVEVDGYVG NFTVKIEKKP RYVDEDACTG CGACAEVCPI EVPNEFDEGL GMRKAIYKPF PQAVPSVFTI DEEHCIRCGL CEEVCDADAI DFDQEPEIVE EEVGAIICAI GYDTCDPTER EEYGYGVYDN VITSIELERL INASGPTGGK VVRPSDGKKP KRIAFIQCVG SRDPHRTNPY CSNVCCMYAM KLAQLIREKY PETQIDIYYM DVRAFGKGYE EYYERSQKQY GIRFIRGRPA EIVEDPETKN LIVRAEDTLL GDVVEREYDL VVLSVGMVPR DSADVIQEVL SISRSPDGFF MEAHPKLRPV DTAIDGIFLA GACQGPKDIP SSVAQGSAAA ARAATALAAG EVAVEPIVSE VDEEICGGCG TCVELCPYGA IELVEKDGKL VAEVTAALCK GCGTCAAACP SGAMEQNHFK TEQLYKQIEG AFRDPA //