ID   A0A5K8A5H1_9BACT        Unreviewed;      1040 AA.
AC   A0A5K8A5H1;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   02-APR-2025, entry version 23.
DE   RecName: Full=4Fe-4S ferredoxin-type domain-containing protein {ECO:0000259|PROSITE:PS51379};
GN   ORFNames=DSCOOX_09270 {ECO:0000313|EMBL:BBO87747.1};
OS   Desulfosarcina ovata subsp. ovata.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobacteria;
OC   Desulfobacterales; Desulfosarcinaceae; Desulfosarcina.
OX   NCBI_TaxID=2752305 {ECO:0000313|EMBL:BBO87747.1, ECO:0000313|Proteomes:UP000422108};
RN   [1] {ECO:0000313|EMBL:BBO87747.1, ECO:0000313|Proteomes:UP000422108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=oXyS1 {ECO:0000313|Proteomes:UP000422108};
RA   Watanabe M., Kojima H., Fukui M.;
RT   "Comparative genomics of hydrocarbon-degrading Desulfosarcina strains.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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; AP021879; BBO87747.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5K8A5H1; -.
DR   Proteomes; UP000422108; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 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:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; 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; PF00037; Fer4; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF13450; NAD_binding_8; 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; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 3.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000422108}.
FT   DOMAIN          112..142
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          951..980
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          984..1013
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1040 AA;  114549 MW;  9FD8A49240541608 CRC64;
     MKNLPVAETF TTHFAGNDFG DVMVVGGGIS GIQASLDLAT AGYRVYLVEK APTIGGKMAQ
     LDKTFPTNDC SMCIESPKFL ECKRHPNIEI LTMTEVDQVQ GEAGDFRVTL TTRPRYIDED
     KCTGCTSCSE YCPVLVSDPF NQDISDNKAV HMYFAQAIPL TPYVSEQCIF LDGKKCTICM
     GICKNDAIDL NQTARQQQVN VGTIILAPGI EPFDPSVNND YGYGKFANVV TSLDYERLLC
     ATGPYEGEIL RASDKKHPHK IAWVHCVGSR GVNQGYNSYC SGVCCTYTQK QVILTKDHDA
     DAECTIFHND IRSYSKGFER FYQRAEALPG IRFVRSYVSI GREIPETQNV TLRYSTTDEG
     VKEEEFDMVV LSVGLRPPAE YGRLAEKFGI ELNEHGFCKT DPTRPLETSR PGIFISGAFQ
     GPMDIPEAVF SASGAGSQCG EVLSRRRGDL SKERVYPPER DVSGEEPKIG VFVCHCGANI
     GRVVNVPEAV EYALSLPGVV HAQEQLFSCA TNSAKEITDT IKEKGLNRVV VAACTPRTHE
     PVFRDTLREG GINQYFYEMA NIREHCSWVH SKEKEEATEK AKDLIRMSVS RTHLLEPLKE
     FDLPVDKTAV VVGGGISGMT SALSLAKQGF EVHLLEKEKE LGGMARRIQT TIEGMDVQAH
     LKETIRKIYQ HPRVHVAHSA TIMDVAGYVG NFTTTVKSET GMRTIRHGAA ILATGADEYT
     PTEYLYGQDD RVLTQLELEE CISGNDERLA GAENLVMIQC VGCRNEERNY CSRICCTHAI
     KNAIRLKAIN PAMDIHILFR DMRTYGFNED YYRMAADKGV KFIRFDPETA PQVEAAEAED
     GRKVLRVTVA DPVLGHGLEL DADLLTLSAA IVPSAGIEEI SKQFKVALSP EGFFQEAHVK
     LRPVDFAAEG VFLCGTAHYP KHISESISQA YGAAGRAAVL LSQDTVTASG SVCEVDEERC
     ISCGACITAC SYGAIEFEMT PRGRKAKVIP VLCKGDGLCN AKCPTEAIQL KHYTDEEILY
     QLDAAFPELC ENRMPVETTA
//