ID X6KWM2_9RHOB Unreviewed; 360 AA.
AC X6KWM2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Contig26, whole genome shotgun sequence {ECO:0000313|EMBL:ETA49649.1};
GN ORFNames=P279_23645 {ECO:0000313|EMBL:ETA49649.1};
OS Rhodobacteraceae bacterium PD-2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA49649.1, ECO:0000313|Proteomes:UP000023196};
RN [1] {ECO:0000313|EMBL:ETA49649.1, ECO:0000313|Proteomes:UP000023196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD-2 {ECO:0000313|EMBL:ETA49649.1,
RC ECO:0000313|Proteomes:UP000023196};
RX PubMed=25700405;
RA Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT Prorocentrum donghaiense.";
RL Genome Announc. Announc.3:e01549-14(2015).
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:ETA49649.1}.
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DR EMBL; AWRV02000026; ETA49649.1; -; Genomic_DNA.
DR AlphaFoldDB; X6KWM2; -.
DR PATRIC; fig|1169855.3.peg.4292; -.
DR HOGENOM; CLU_003827_14_3_5; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000023196; 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:UP000023196}.
FT DOMAIN 13..116
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 276..360
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 360 AA; 39117 MW; 86184E33DF0A9B71 CRC64;
MAKTKASAAG SWTDDEALEC VSILPESPNV VTVCFQAPSG RPFNFQAGQF LTLELPVPGG
PLYRTFTISS APSRPQSLTI TMKAQASSIG VRWIIDNLRP GMTLKATGPA GRFTSVEYPA
KKYLFISAGS GITPMMSMTT EIYDLGRHCD IVFVNCAPRP SEIIFKRRLE HMATRIEGLD
LKWVVQESDP YSPWTGYKGT FNQLMLGLMA PDYLEREVFC CGPEGFMLAV REALAGLGFD
MDHYHQESFH APGTPGPELV EVELPDDDLP EDNVMAEIVF DISGISQSCP ETETVLAVAR
NAGIAIPSGC TFGVCGTCKT KKLSGDVHMV HNGGITDEEI EEGYILACCS NPRGKVTLDL
//
