ID F0T756_METLA Unreviewed; 771 AA.
AC F0T756;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=Metbo_2477 {ECO:0000313|EMBL:ADZ10690.1};
OS Methanobacterium lacus (strain AL-21).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=877455 {ECO:0000313|EMBL:ADZ10690.1, ECO:0000313|Proteomes:UP000007490};
RN [1] {ECO:0000313|Proteomes:UP000007490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL-21 {ECO:0000313|Proteomes:UP000007490};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Cadillo-Quiroz H.,
RA Imachi H., Zinder S., Liu W., Woyke T.;
RT "Complete sequence of Methanobacterium sp. AL-21.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADZ10690.1, ECO:0000313|Proteomes:UP000007490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL-21 {ECO:0000313|EMBL:ADZ10690.1,
RC ECO:0000313|Proteomes:UP000007490};
RX PubMed=24449792; DOI=10.1099/ijs.0.059964-0;
RA Cadillo-Quiroz H., Brauer S.L., Goodson N., Yavitt J.B., Zinder S.H.;
RT "Methanobacterium paludis sp. nov. and a novel strain of Methanobacterium
RT lacus isolated from northern peatlands.";
RL Int. J. Syst. Evol. Microbiol. 64:1473-1480(2014).
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=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
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}.
CC -!- SIMILARITY: Belongs to the MvhD/VhuD family.
CC {ECO:0000256|ARBA:ARBA00009293}.
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DR EMBL; CP002551; ADZ10690.1; -; Genomic_DNA.
DR RefSeq; WP_013646041.1; NC_015216.1.
DR AlphaFoldDB; F0T756; -.
DR STRING; 877455.Metbo_2477; -.
DR GeneID; 10278951; -.
DR KEGG; mel:Metbo_2477; -.
DR eggNOG; arCOG02236; Archaea.
DR HOGENOM; CLU_020302_0_0_2; -.
DR OrthoDB; 32867at2157; -.
DR UniPathway; UPA00647; UER00700.
DR Proteomes; UP000007490; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR039650; HdrA-like.
DR InterPro; IPR003813; MvhD/FlpD.
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; PF13237; Fer4_10; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF02662; FlpD; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|RuleBase:RU366072};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366072};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU366072}; 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:UP000007490};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 234..263
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 281..310
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 573..600
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 601..630
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 771 AA; 83747 MW; B3433C2ED09041FA CRC64;
MKPGVFLCCC GDNISSKIDL DKLKRSVCED VQFIDEATYL CSNEGMEHIV TKIKSEKPGG
IVIAACSPKM HEKRFRSCAE RANMNQYLVD VANIREQCAW VSKDPDPTVK AIDIVNSSIN
AVKNSVGLAK IQIPVIKSAL VVGGGISGIT AALSLAKQGI HVHLVEKSAS IGGNMVKIGK
VFSADTLSEE CAMCSLGPLI SEVGENHNID VISMAEVSGV SGHMGNFSVT LQTDPKMIDG
DRCTSCGRCA EICSINVPDE FNFNLTLRNA AYKPFAGALP SSFSIDPDAC IKCGKCVEAC
PVDAINLESK TKNIVLEVGA IVLATGYTEL NPEQMEEFGY KRIQGVITQM ELARLLAVNG
PTSGKLISPL TGKKPRNIVM IQCVGSRDRK QGSIPQCSTI CCMTALKHAN YIVNHNKGTD
IYICYTDMRT PGTYENYYFE TQKKGEKSLR FIRGKVAQVK KVNNDALVAR VEDTLGGGVT
DIEADMIVLS SALMPSDTIA GVQEATGVGL TNEKFVKEKN SKMDPTQTTV PGIFVSGTAK
GAMDITETIN MSRSAASRVS EMLTQEFIEV EPNFAVLDQD RCNQCLSCLE QCPAKAIYLD
KMVEVDPVAC TGCGYCVSLC ETKALSLPLY SDQVIQARID GALKMGNRSI LTFLDEKIAY
VAADNMGSNR LNYPTDVRII KVPSILRLEV KHLLYGFKKG AKGIFLGDGT ANASDETMDE
MLTKKVQELM QGASEEGIDP SRIYFYPAYL PHYKGLADKL KEFSKILEKI E
//
