ID A3VLL3_9RHOB Unreviewed; 296 AA.
AC A3VLL3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Ferredoxin:Oxidoreductase FAD/NAD(P)-binding:Oxidoreductase FAD-binding region protein {ECO:0000313|EMBL:EAQ10901.1};
GN ORFNames=RB2654_22073 {ECO:0000313|EMBL:EAQ10901.1};
OS Maritimibacter alkaliphilus HTCC2654.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ10901.1, ECO:0000313|Proteomes:UP000002931};
RN [1] {ECO:0000313|EMBL:EAQ10901.1, ECO:0000313|Proteomes:UP000002931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ10901.1,
RC ECO:0000313|Proteomes:UP000002931};
RX PubMed=20729358; DOI=10.1128/JB.00873-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of Pelagibaca bermudensis HTCC2601T and Maritimibacter
RT alkaliphilus HTCC2654T, the type strains of two marine Roseobacter
RT genera.";
RL J. Bacteriol. 192:5552-5553(2010).
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:EAQ10901.1}.
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DR EMBL; AAMT01000023; EAQ10901.1; -; Genomic_DNA.
DR AlphaFoldDB; A3VLL3; -.
DR STRING; 314271.RB2654_22073; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_17_0_5; -.
DR Proteomes; UP000002931; 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; cd06185; PDR_like; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00409; PHDIOXRDTASE.
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:UP000002931}.
FT DOMAIN 1..91
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 212..296
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 296 AA; 31502 MW; FF2D5F22CAA6810B CRC64;
MRWECTGVLR IELEPLAGEL TPPEPGAHID VSILDAPLRQ YSLTAGSDTG HYVLGIRREV
QSRGGSEAVH DRLRPGDVID ISEPRNTFPL AADGEVHLIA GGIGVTPILF MAEALAKVGR
SYRFTYCARS RTDAGFLSDA LTLGGTLHFD DEDGMPDLAA LTSMAPDNAH LFCCGPAPML
DAFVAACADR PADHVHIERF EPSKLEAGAG EFVVELAKTG AEVIVPSDKT ILDALIDAGL
SPEHSCGVGV CGTCETRVLA GEADHQDLVL TDEERAEGAM LICCSRAKTD RLVLDL
//
