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Database: UniProt
Entry: F7XK56_METZD
LinkDB: F7XK56_METZD
Original site: F7XK56_METZD 
ID   F7XK56_METZD            Unreviewed;       784 AA.
AC   F7XK56;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE            EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
GN   OrderedLocusNames=Mzhil_0654 {ECO:0000313|EMBL:AEH60521.1};
OS   Methanosalsum zhilinae (strain DSM 4017 / NBRC 107636 / OCM 62 / WeN5)
OS   (Methanohalophilus zhilinae).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosalsum.
OX   NCBI_TaxID=679901 {ECO:0000313|EMBL:AEH60521.1, ECO:0000313|Proteomes:UP000006622};
RN   [1] {ECO:0000313|EMBL:AEH60521.1, ECO:0000313|Proteomes:UP000006622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5
RC   {ECO:0000313|Proteomes:UP000006622};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEH60521.1, ECO:0000313|Proteomes:UP000006622}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4017 / NBRC 107636 / OCM 62 / WeN5
RC   {ECO:0000313|Proteomes:UP000006622};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ovchinnikova G., Daligault H., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Spring S., Schueler E., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanosalsum zhilinae DSM 4017.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU366072}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU366072};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU366072};
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:0000256|RuleBase:RU366072}.
CC   -!- SUBUNIT: The ferredoxin:CoB-CoM heterodisulfide reductase is composed
CC       of three subunits; HdrA, HdrB and HdrC.
CC       {ECO:0000256|RuleBase:RU366072}.
CC   -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000256|ARBA:ARBA00006561,
CC       ECO:0000256|RuleBase:RU366072}.
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DR   EMBL; CP002101; AEH60521.1; -; Genomic_DNA.
DR   RefSeq; WP_013897960.1; NC_015676.1.
DR   AlphaFoldDB; F7XK56; -.
DR   STRING; 679901.Mzhil_0654; -.
DR   GeneID; 10822265; -.
DR   KEGG; mzh:Mzhil_0654; -.
DR   HOGENOM; CLU_020302_0_0_2; -.
DR   OMA; CPSGAMQ; -.
DR   OrthoDB; 32867at2157; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000006622; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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   InterPro; IPR003813; MvhD/FlpD.
DR   NCBIfam; NF040770; hetero_SS_HdrA2; 1.
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; PF00037; Fer4; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF02662; FlpD; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 4.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU366072};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366072};
KW   Flavoprotein {ECO:0000256|RuleBase:RU366072};
KW   Iron {ECO:0000256|RuleBase:RU366072};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU366072};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366072};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU366072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006622}.
FT   DOMAIN          233..264
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          282..311
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          571..599
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          600..629
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   784 AA;  86069 MW;  0DBBC37B5CB33673 CRC64;
     MKIGVYICHC GLNIANVINV DILHSKVEKL EDVAVVRDVQ FMCSDAGQEY IIEDIGDNNL
     DRILVAACSP KLHEQTFRRV IEKAGINPYL LEMVNIREQC SWVHGNNPQM ATQKAFDLIK
     MGLARLKHSN PLDIEKFRIN TDVLVIGGGV TGIEASLNLA DSGYNVHLIE QEPTIGGKMA
     LINEVFPTND CSICVLAPKM TEVHNHPNIT LLTLSQITEI TGNVGNFKIK GVKRPRYVLE
     DKCKGCVEDC SGVCPVEIPS KFDYGLGKKK AISIPIPQSV PQVAYINSDY CVGCGLCSLA
     CPAEAIDYKQ KEEEFIFNAG AIIVSTGYSL FDASRKEEYG YGIYPDVITN MELERLLNAS
     GPTRGRVVVP SSGKVPERVA FIQCVGSRDE SVDNPYCSRV CCMASMKNAQ LLKERYPQIE
     IVIHYIDVRA SGEMYEEYYT KTQSMGIDFI RGKASQVLMD KQGRPALRFE DTLESEIRQE
     SYDMIVLATG MEAPENSRTI TRMLNLSCRA DRFYSIAHPK MRPVDSHIDG VFIAGCATGP
     KDIQSSIAQG CAAAAKVMKL LGSGELEADP LCAVVEKASC VGCGLCEDVC IFGKIRVIDS
     KAVVDEISCQ GCGTCSAACP TDAIDMRHFT DEQIFAQIEA AVESRDEFPL IIGFLCNWCS
     YSCADLAGVS RIDYSTNIRI IRTMCAGRVD PEFVIKALEG GADGVLVAGC KLGECHYVHA
     NYSAKKRLEA LQNVLEETGI DPSRLRLLWI SASECEKFAK TVDDFVDNLK NIGPVGHEIL
     EAAD
//
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