ID W4HJJ2_9RHOB Unreviewed; 354 AA.
AC W4HJJ2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:ETW12869.1};
GN ORFNames=ATO8_10008 {ECO:0000313|EMBL:ETW12869.1};
OS Roseivivax marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1379903 {ECO:0000313|EMBL:ETW12869.1, ECO:0000313|Proteomes:UP000019063};
RN [1] {ECO:0000313|EMBL:ETW12869.1, ECO:0000313|Proteomes:UP000019063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s10s {ECO:0000313|EMBL:ETW12869.1,
RC ECO:0000313|Proteomes:UP000019063};
RX PubMed=24567080; DOI=10.1007/s10482-014-0140-5;
RA Li G., Lai Q., Liu X., Sun F., Shao Z.;
RT "Roseivivax atlanticus sp. nov., isolated from surface seawater of the
RT Atlantic Ocean.";
RL Antonie Van Leeuwenhoek 105:863-869(2014).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:ETW12869.1}.
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DR EMBL; AQQW01000005; ETW12869.1; -; Genomic_DNA.
DR AlphaFoldDB; W4HJJ2; -.
DR STRING; 1379903.ATO8_10008; -.
DR PATRIC; fig|1317118.6.peg.2063; -.
DR eggNOG; COG1018; Bacteria.
DR Proteomes; UP000019063; 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; cd06215; FNR_iron_sulfur_binding_1; 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; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
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:SF6; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00970; FAD_binding_6; 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; PS00197; 2FE2S_FER_1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019063}.
FT DOMAIN 10..113
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 270..354
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 354 AA; 38742 MW; C5A7C9BC9850F29D CRC64;
MPRQDSPVWA DSEELECVAT VPEAPNVMSF AFRPPSGARF HFRAGQFITL DLPVPGGNVQ
RTYTISSSPS TQAFITVTVK AQADSIGTRW MLDNLRPGMR IRAYGPAGHF HVPPQPDGRY
LFISAGSGVT PMMSMSSFLW ERGEEPDIAF VHCAQSPQNI IFRQKLEYMA SRTSGLKLHF
VVDDDDPYTV WTGYRGRLSA LMLGLMVPDY LEREVYCCGP EGFMEGVREM LISLGYDMEN
YHQESFSAPA ESRAELTEFD DLVPDESAAA EVVFAKSGVT APCHETDTIL NVAKGAGLNL
PSGCTFGLCG TCKVRKTSGE VHMVHNGGIS DEDIAEGYIL ACCSNPIGKV EVEV
//
