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Database: UniProt
Entry: M1PCY5_DESSD
LinkDB: M1PCY5_DESSD
Original site: M1PCY5_DESSD 
ID   M1PCY5_DESSD            Unreviewed;      1020 AA.
AC   M1PCY5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Tungsten-dependent benzoyl-CoA reductase-related protein bamE {ECO:0000313|EMBL:AGF77615.1};
GN   OrderedLocusNames=UWK_01043 {ECO:0000313|EMBL:AGF77615.1};
OS   Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfocapsaceae; Desulfocapsa.
OX   NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF77615.1, ECO:0000313|Proteomes:UP000011721};
RN   [1] {ECO:0000313|Proteomes:UP000011721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX   PubMed=23961312; DOI=10.4056/sigs.3777412;
RA   Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA   Schreiber L.;
RT   "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT   deltaproteobacterium specialized in disproportionating inorganic sulfur
RT   compounds.";
RL   Stand. Genomic Sci. 8:58-68(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the HdrA family.
CC       {ECO:0000256|ARBA:ARBA00006561}.
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DR   EMBL; CP003985; AGF77615.1; -; Genomic_DNA.
DR   RefSeq; WP_015403311.1; NC_020304.1.
DR   AlphaFoldDB; M1PCY5; -.
DR   STRING; 1167006.UWK_01043; -.
DR   KEGG; dsf:UWK_01043; -.
DR   PATRIC; fig|1167006.5.peg.1166; -.
DR   eggNOG; COG1148; Bacteria.
DR   HOGENOM; CLU_004231_2_0_7; -.
DR   OrthoDB; 9766627at2; -.
DR   Proteomes; UP000011721; Chromosome.
DR   GO; GO:0051536; F:iron-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:InterPro.
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; IPR023753; FAD/NAD-binding_dom.
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; PF12838; Fer4_7; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT   DOMAIN          107..138
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          942..971
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          975..1004
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1020 AA;  110541 MW;  FCAAD264085C1BA3 CRC64;
     MRASIPTPSA LKTVGAVLVV GGGVAGVQAA LDLTELGLKV YLVEKSGAIG GVMARLDKTF
     PTNDCSLCIL APKLVEAGRD PNIEILTKSE LISLDGVPGN FTARIRKEPR YIDEEICTGC
     GQCTLYCLKQ IDDDYNENLG ISNAAHIDYA QAVPTSYYID AKACFMLNYQ TCGLCAVACQ
     AKAIRFDQKE EILDLAIGSV ILAPGFGRTS KEVLGRYGWG KFADVLSAFE HERLMCASGP
     TGGAILRPSD KKHPKKIAFI QCIGSRDQNC GNNYCSSVCC MYAIKQATLA REHDPSAEIT
     LFYMDIRTHG KGFDAARERA TLENNFRVIY ARPPQVEDVF DGRLLLTWAT EDGKHHYEKF
     DMVVLTQGLE SPDDAEQLGQ AAGIDLNSYL FAQTNNYTPL ATSRPGVYVI GAFQGPKDIP
     DSVTQAGGAA ALCSGQLVTA RGMEITKAVF PEERDISREE PRIGVFVCHC GINIAGVVDV
     RAVRDYARDL PGVVYSTDNL YSCSQDTQQH LVNIIREHRL NRIVVSACTP RTHEPLFQTT
     LRDAGLNRAL FEMANIRDQC SWVHMHEPEA ATAKAKDLVR MAVAKAAHLT ALPEQRLPVT
     PSALVIGGGL AGMTAALTIA EQGFLTTLVE QEDTLGGATL LLSADRFGGD PRKTIADLVH
     KVKTHSRIHV YSGATVASVS GYVGNFTTTI TRKAGSEVVN HGIMVIATGG KPYKPEQYLY
     GQSERVLTQL ELEQRLASGR PLSAKTKQVV MIQCVGSRGA DLAYCSRVCC GQALKNAIRL
     KTINPDLTIF VFYRDMRAYG FMEDDYRRAR ELGVIFIRYS PDNPPKVTPG RSKSSPLKVV
     GYDPLLGEEV ELDTDLLVLS VGIVPEDPSI LSRMLKVPVT ADKFYLEAHV KLRPVDMAVD
     GIFVCGLAHA PKSMDETIAQ AQAAAGRACH PLANGSISPE PIVSHVDPYL CIGCGACETF
     CPYKAITINK EVKPRKAQTL TASCKGCGVC AARCPTMAID MGRFTFDGIM AQVSAFGKSV
//
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