ID   H2FTQ7_OCESG            Unreviewed;       462 AA.
AC   H2FTQ7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Rubredoxin-NAD(+) reductase {ECO:0000313|EMBL:AEY01355.1};
GN   OrderedLocusNames=GU3_07995 {ECO:0000313|EMBL:AEY01355.1};
OS   Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Oceanimonas.
OX   NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY01355.1, ECO:0000313|Proteomes:UP000007742};
RN   [1] {ECO:0000313|EMBL:AEY01355.1, ECO:0000313|Proteomes:UP000007742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GK1 {ECO:0000313|EMBL:AEY01355.1,
RC   ECO:0000313|Proteomes:UP000007742};
RX   PubMed=22461556; DOI=10.1128/JB.00023-12;
RA   Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA   Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT   "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT   from Gavkhouni Wetland in Iran.";
RL   J. Bacteriol. 194:2123-2124(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00006442}.
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DR   EMBL; CP003171; AEY01355.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2FTQ7; -.
DR   STRING; 511062.GU3_07995; -.
DR   KEGG; oce:GU3_07995; -.
DR   eggNOG; COG1251; Bacteria.
DR   eggNOG; COG1773; Bacteria.
DR   HOGENOM; CLU_003291_4_4_6; -.
DR   OrthoDB; 9808980at2; -.
DR   Proteomes; UP000007742; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd00730; rubredoxin; 1.
DR   Gene3D; 2.20.28.10; -; 1.
DR   Gene3D; 3.30.390.120; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR041364; Rbx-bd.
DR   InterPro; IPR024934; Rubredoxin-like_dom.
DR   InterPro; IPR024935; Rubredoxin_dom.
DR   PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18113; Rbx_binding; 1.
DR   Pfam; PF00301; Rubredoxin; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00163; RUBREDOXIN.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF57802; Rubredoxin-like; 1.
DR   PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007742};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..52
FT                   /note="Rubredoxin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50903"
SQ   SEQUENCE   462 AA;  49000 MW;  D5DC234D29ECC626 CRC64;
     MKKWLCIICG LIYDEAKGWP ADDIAPGTRW EDVPDDWLCP DCLVGKADFE MIEITNDEPA
     PVAAVAEVAT PAAEPALEPV VIIGTGHGGY QLAVALRARS PELPITLFTA DDGALYSKPA
     LSNALALGKD GDGLVSETAL SWEQRLGVRV YPHTRVERID RENKRLHTSI GEYPYGRLVL
     ATGASPIQIP VAGIPVAGEQ SAMVSVNDLL DYRRFRERLA GKQHVTILGD GLIGCEFAND
     LAAQGIGVTV VGLGQWPMER LIPQPLGEAL QRALSGLGVE WALQDSISRI DAADEGYCLQ
     LQSGRELATD LVLSAVGLRP NTGLAQAAGL ATGRGISVDL AHATSDPAIF ALGDCAEVAG
     QWAPYIAPIN QAIPALVETL LGRPTEATLK ASPVLVKTPV LPLSVQPAMG PGEWRVDAHG
     EELAAGFYGA DGSLSGFALL GRELQSQRSQ WLEQLNPARN VA
//