GenomeNet

Database: UniProt
Entry: A0A1F2PAD0_9EURY
LinkDB: A0A1F2PAD0_9EURY
Original site: A0A1F2PAD0_9EURY 
ID   A0A1F2PAD0_9EURY        Unreviewed;       644 AA.
AC   A0A1F2PAD0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A {ECO:0000256|RuleBase:RU366072};
DE            EC=1.8.-.- {ECO:0000256|RuleBase:RU366072};
GN   Name=hdrA {ECO:0000313|EMBL:OFV68267.1};
GN   ORFNames=SCAL_000907 {ECO:0000313|EMBL:OFV68267.1};
OS   Candidatus Syntrophoarchaeum caldarius.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinales incertae sedis; ANME-2 cluster;
OC   Syntrophoarchaeum.
OX   NCBI_TaxID=1838285 {ECO:0000313|EMBL:OFV68267.1, ECO:0000313|Proteomes:UP000186940};
RN   [1] {ECO:0000313|EMBL:OFV68267.1, ECO:0000313|Proteomes:UP000186940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BOX2 {ECO:0000313|EMBL:OFV68267.1};
RA   Laso-Perez R., Richter M., Wegener G., Musat F.;
RT   "Microbial consortia oxidize butane by reversing methanogenesis.";
RL   Submitted (MAY-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OFV68267.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LYOS01000002; OFV68267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F2PAD0; -.
DR   STRING; 1838285.SCAL_000907; -.
DR   PATRIC; fig|1838285.3.peg.918; -.
DR   UniPathway; UPA00647; UER00700.
DR   Proteomes; UP000186940; Unassembled WGS sequence.
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; 1.
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; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR039650; HdrA-like.
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   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|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   ECO:0000313|EMBL:OFV68267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186940}.
FT   DOMAIN          231..261
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          279..313
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          570..599
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   644 AA;  70505 MW;  0B8CD7FCD175B795 CRC64;
     MIGVYVCHCG INIASVVDVK AVAEFARTLP GVTVAKDYQY MCSDPGQELI KNDIKEHGLK
     RVVVAACSPR MHEPTFRVAI SDANLNPYLL EVANIREHCS WVHHDREAAT AKAKDLVQSA
     VSKAMLLTPL ESREVGVTPR SLVIGGGIAG LEAALDIADA GFKVYLVERE ATLGGHAAQI
     ERLFPAMEDA SCLVLPKMAS VMEHPNIEVM TDSEILEVDG YVGNFEVTVV KHPRYVDTTK
     CTACGKCEEV CPVDVDDAFN QNLKTRKAIY IPFKSAVPPT YRIDPANCLY FQDGSCKKCV
     DVCSDGAINL EEEEVKTKLE VGTIVIATGY EPFDARNKPE FGYGQYDNVI TGLELERMLA
     KDGPTGGKVF VKDKEPEKIG FIQCVGSRDK QVGNEYCSRV CCMYTAKQAR MLREMYPDAL
     VKVFFMDVRA YGKGYEEFWE ETQRSGVIYV RSNPSEVYRR GDRVVLRGED TLMGEAFEEE
     FDLLVLATGL VPRADTRDFG NLLKVSRSGD GFYLEAHPKL RPVDTASDGV YLAGCCQGPK
     DITDTISQAN GTAIKACIPL FVGKVSIEPT TSMIDSLICS GCRVCEGICT YGALSFDPEM
     GVMTVNEVLC KGCGSCASAC PSSAISMKHF LDQQIFAQIE AIVI
//
DBGET integrated database retrieval system