ID B4WYV6_9GAMM Unreviewed; 331 AA.
AC B4WYV6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Oxidoreductase NAD-binding domain protein {ECO:0000313|EMBL:EDX88503.1};
GN ORFNames=ADG881_605 {ECO:0000313|EMBL:EDX88503.1};
OS Alcanivorax sp. DG881.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=236097 {ECO:0000313|EMBL:EDX88503.1, ECO:0000313|Proteomes:UP000003954};
RN [1] {ECO:0000313|EMBL:EDX88503.1, ECO:0000313|Proteomes:UP000003954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG881 {ECO:0000313|EMBL:EDX88503.1,
RC ECO:0000313|Proteomes:UP000003954};
RA Bolch C., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS989915; EDX88503.1; -; Genomic_DNA.
DR RefSeq; WP_007148911.1; NZ_DS989915.1.
DR AlphaFoldDB; B4WYV6; -.
DR STRING; 236097.ADG881_605; -.
DR eggNOG; COG0543; Bacteria.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_7_0_6; -.
DR Proteomes; UP000003954; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 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 CDD; cd00207; fer2; 1.
DR CDD; cd06189; flavin_oxioreductase; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714}.
FT DOMAIN 3..91
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 98..196
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 331 AA; 36120 MW; 87BD3808F216A250 CRC64;
MPQTFTITVS GKGHFPCRTD QSIVDAGQQA GFGFPIACRN GVCERCIGQL SHGQVQQKNR
TIHAGDASSS QVLYCIALPL SDCEIDVPEV TAPGELPVHQ IHCQIQQIDA LNHDVSRVWL
RLPAGKKIQW HAGQYLMLNL HGESYPFSIA NHCDGRDIEL HVRHGDDNSA AQDIMASLQA
DSTVSTTLPA GLRFIDSAPD QPVWFICGST GFAPVKAMIE RLIALNFTQP VRLFWGARTD
ADLYLPHLPA QWQGALADFD FVTSLSDIRH PDHAEGLVHE AALEALSEPD LPLFFLGGSP
PMGWAVFDAL VAEGVPASNI HCDVFDYAPR D
//
