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Database: UniProt
Entry: Q50756
LinkDB: Q50756
Original site: Q50756 
ID   HDRA_METTM              Reviewed;         659 AA.
AC   Q50756; D9PYN8; Q50752;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   10-APR-2019, entry version 115.
DE   RecName: Full=H(2):CoB-CoM heterodisulfide,ferredoxin reductase subunit A {ECO:0000305};
DE            EC=1.8.98.5 {ECO:0000269|PubMed:21262829, ECO:0000305|PubMed:8119281};
DE   AltName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000305};
GN   Name=hdrA; OrderedLocusNames=MTBMA_c17680;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18;
RP   210-226; 425-435; 455-459 AND 641-650.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=7925445; DOI=10.1111/j.1432-1033.1994.00253.x;
RA   Hedderich R., Koch J., Linder D., Thauer R.K.;
RT   "The heterodisulfide reductase from Methanobacterium
RT   thermoautotrophicum contains sequence motifs characteristic of
RT   pyridine-nucleotide-dependent thioredoxin reductases.";
RL   Eur. J. Biochem. 225:253-261(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/JB.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A.,
RA   Seedorf H., Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
RN   [3] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 651-659.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8617278; DOI=10.1111/j.1432-1033.1996.00294.x;
RA   Vaupel M., Dietz H., Linder D., Thauer R.K.;
RT   "Primary structure of cyclohydrolase (Mch) from Methanobacterium
RT   thermoautotrophicum (strain Marburg) and functional expression of the
RT   mch gene in Escherichia coli.";
RL   Eur. J. Biochem. 236:294-300(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-18, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=8119281; DOI=10.1111/j.1432-1033.1994.tb18608.x;
RA   Setzke E., Hedderich R., Heiden S., Thauer R.K.;
RT   "H2: heterodisulfide oxidoreductase complex from Methanobacterium
RT   thermoautotrophicum. Composition and properties.";
RL   Eur. J. Biochem. 220:139-148(1994).
RN   [5] {ECO:0000305}
RP   FUNCTION, COFACTOR, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=2121478; DOI=10.1111/j.1432-1033.1990.tb19331.x;
RA   Hedderich R., Berkessel A., Thauer R.K.;
RT   "Purification and properties of heterodisulfide reductase from
RT   Methanobacterium thermoautotrophicum (strain Marburg).";
RL   Eur. J. Biochem. 193:255-261(1990).
RN   [6]
RP   ASSOCIATION WITH F420-NON-REDUCING HYDROGENASE.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=12856108; DOI=10.1007/s00203-003-0577-9;
RA   Stojanowic A., Mander G.J., Duin E.C., Hedderich R.;
RT   "Physiological role of the F420-non-reducing hydrogenase (Mvh) from
RT   Methanothermobacter marburgensis.";
RL   Arch. Microbiol. 180:194-203(2003).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=21262829; DOI=10.1073/pnas.1016761108;
RA   Kaster A.K., Moll J., Parey K., Thauer R.K.;
RT   "Coupling of ferredoxin and heterodisulfide reduction via electron
RT   bifurcation in hydrogenotrophic methanogenic archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:2981-2986(2011).
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:0000269|PubMed:2121478,
CC       ECO:0000269|PubMed:21262829, ECO:0000269|PubMed:8119281}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coenzyme B + coenzyme M + 2 H(+) + 2 reduced [2Fe-2S]-
CC         [ferredoxin] = coenzyme M-coenzyme B heterodisulfide + 2 H2 + 2
CC         oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:55748, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:18276, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:58319, ChEBI:CHEBI:58411, ChEBI:CHEBI:58596;
CC         EC=1.8.98.5; Evidence={ECO:0000269|PubMed:21262829,
CC         ECO:0000305|PubMed:8119281};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC         ECO:0000305|PubMed:2121478};
CC       Note=Binds 4 [4Fe-4S] clusters per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00711, ECO:0000305|PubMed:2121478};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000305|PubMed:2121478};
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. {ECO:0000305}.
CC   -!- SUBUNIT: The heterodisulfide reductase is composed of three
CC       subunits; HdrA, HdrB and HdrC. It forms a complex with the F420-
CC       non-reducing hydrogenase (Mvh), which provides the reducing
CC       equivalents to the heterodisulfide reductase.
CC       {ECO:0000269|PubMed:12856108, ECO:0000269|PubMed:2121478,
CC       ECO:0000269|PubMed:21262829, ECO:0000269|PubMed:8119281}.
CC   -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}.
DR   EMBL; X81134; CAA57039.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL59336.1; -; Genomic_DNA.
DR   EMBL; X92083; CAA63065.1; -; Genomic_DNA.
DR   PIR; S48720; S48720.
DR   RefSeq; WP_013296546.1; NC_014408.1.
DR   ProteinModelPortal; Q50756; -.
DR   SMR; Q50756; -.
DR   DIP; DIP-59606N; -.
DR   IntAct; Q50756; 5.
DR   PRIDE; Q50756; -.
DR   EnsemblBacteria; ADL59336; ADL59336; MTBMA_c17680.
DR   GeneID; 9705479; -.
DR   KEGG; mmg:MTBMA_c17680; -.
DR   PATRIC; fig|79929.8.peg.1705; -.
DR   eggNOG; arCOG02235; Archaea.
DR   eggNOG; COG1148; LUCA.
DR   HOGENOM; HOG000230698; -.
DR   KO; K03388; -.
DR   OMA; TAKHAML; -.
DR   OrthoDB; 1148at2157; -.
DR   BioCyc; MMAR79929:G1GML-1739-MONOMER; -.
DR   BRENDA; 1.8.98.1; 7427.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000000345; 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:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IDA:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
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; PF00037; Fer4; 1.
DR   Pfam; PF13237; Fer4_10; 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   1: Evidence at protein level;
KW   4Fe-4S; Complete proteome; Direct protein sequencing; FAD;
KW   Flavoprotein; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW   Oxidoreductase; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:7925445,
FT                                ECO:0000269|PubMed:8119281}.
FT   CHAIN         2    659       H(2):CoB-CoM heterodisulfide,ferredoxin
FT                                reductase subunit A.
FT                                /FTId=PRO_0000150062.
FT   DOMAIN      244    274       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      292    321       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      581    610       4Fe-4S ferredoxin-type 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN      611    640       4Fe-4S ferredoxin-type 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   NP_BIND     158    181       FAD. {ECO:0000255}.
FT   METAL       254    254       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       257    257       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       260    260       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       264    264       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       304    304       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       307    307       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       311    311       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       591    591       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       594    594       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       597    597       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       601    601       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       620    620       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       623    623       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       626    626       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       630    630       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
SQ   SEQUENCE   659 AA;  72182 MW;  FC01196FEE3A5F9E CRC64;
     MAEEKKETME EPKIGVYVCH CGVNIGGVVD VEAVRDYAAK LPNVVIAKDY KYYCSDPGQL
     EIQKDIKELG INRVVVAACS PRLHEPTFRR CVEEAGLNQF LFEFANIREH DSWVHMDNPE
     GATEKAKDLV RMAVAKARLL EPLEASKVSV DDKALVIGGG VAGIQAALDL ADMGFKTYMV
     EKRPSISGRM GQLDKTFPTL DCSMCILAPK MVDVGKHDNI ELITYAEVKE VDGYIGNFKV
     KIEKKPRYID EELCTGCGSC VEVCPIEMPN YFDEGIGMTK AVYIPFPQAV PLCATIDKDY
     CIECMLCDEV CERGAVKHDQ EPEEIEIEVG TIIVATGYDA YDPTEKLEYG YGRHTNVITG
     LELERMINAS GPTDGKVLKP SDGEKPKRVA FIHCVGSRDE QIGKPYCSRV CCMYIMKNAQ
     LIKDKMPDTE VTLYYMDIRA FGKGFEEFYK RSQEKYGIKF IRGRPAEVIE NPDLTLTVRS
     EDTLLGKVTE YDYDMVVLGV GLVPPEGAET LRQTIGLSKS ADGFLMEAHP KLRPVDTLTD
     GVYLAGVAQG PKDIPDAVAQ ASGAAARAAI PMVKGEVEIE PIIAVTDSDV CGGCEVCIEL
     CPFGAISIEE GHANVNVALC KGCGTCVAAC PSGAMDQQHF KTEQIMAQIE AALNEPASK
//
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