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Database: UniProt
Entry: P96801
LinkDB: P96801
Original site: P96801 
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   10-APR-2019, entry version 120.
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
OS   100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   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.,
RA   Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O.,
RA   Malykh A.G., Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19
RT   and 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
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; Y09871; CAA70999.1; -; Genomic_DNA.
DR   EMBL; AE009439; AAM01482.1; -; Genomic_DNA.
DR   ProteinModelPortal; P96801; -.
DR   SMR; P96801; -.
DR   PRIDE; P96801; -.
DR   EnsemblBacteria; AAM01482; AAM01482; MK0265.
DR   KEGG; mka:MK0265; -.
DR   PATRIC; fig|190192.8.peg.268; -.
DR   eggNOG; arCOG02235; Archaea.
DR   eggNOG; COG1148; LUCA.
DR   HOGENOM; HOG000230698; -.
DR   KO; K03388; -.
DR   OMA; TAKHAML; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000001826; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 3.
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; 3.
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.
FT   CHAIN         1    656       CoB--CoM heterodisulfide reductase iron-
FT                                sulfur subunit A 2.
FT                                /FTId=PRO_0000150059.
FT   DOMAIN      238    269       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      286    315       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      577    606       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      610    639       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     152    175       FAD. {ECO:0000255}.
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       254    254       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       258    258       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       301    301       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       305    305       Iron-sulfur 1 (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       592    592       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       596    596       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       625    625       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       629    629       Iron-sulfur 3 (4Fe-4S).
FT                                {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
//
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