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Database: UniProt
Entry: P60200
LinkDB: P60200
Original site: P60200 
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   16-JAN-2019, entry version 90.
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 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   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.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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
RT   of Methanococcus jannaschii probably directing selenocysteine
RT   insertion.";
RL   J. Mol. Biol. 266:637-641(1997).
CC   -!- FUNCTION: Part of a complex that catalyzes the reversible
CC       reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme
CC       M) and H-S-CoB (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
CC       heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme
CC       M-coenzyme B heterodisulfide: step 1/1.
CC       {ECO:0000250|UniProtKB:Q6LWL2}.
CC   -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is
CC       composed of three subunits; HdrA, HdrB and HdrC.
CC       {ECO:0000250|UniProtKB:Q6LWL2}.
CC   -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
DR   EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PRIDE; P60200; -.
DR   InParanoid; P60200; -.
DR   OMA; CTPKIHE; -.
DR   PhylomeDB; P60200; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IDA:MENGO.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039650; HdrA-like.
DR   PANTHER; PTHR43498; PTHR43498; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 4.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Methanogenesis; Oxidoreductase; Reference proteome;
KW   Repeat; Selenocysteine.
FT   CHAIN         1    657       CoB--CoM heterodisulfide reductase iron-
FT                                sulfur subunit A.
FT                                /FTId=PRO_0000150057.
FT   DOMAIN      235    266       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      283    312       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      574    603       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      607    636       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     149    172       FAD. {ECO:0000255}.
FT   METAL       245    245       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       248    248       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       251    251       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       255    255       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       292    292       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       295    295       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       298    298       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       302    302       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       583    583       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       586    586       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       589    589       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       593    593       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       616    616       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       619    619       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       622    622       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       626    626       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NON_STD     196    196       Selenocysteine. {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
//
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