ID A0A0B5DV09_9RHOB Unreviewed; 312 AA.
AC A0A0B5DV09;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:AJE45050.1};
GN ORFNames=P73_0335 {ECO:0000313|EMBL:AJE45050.1};
OS Celeribacter indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208324 {ECO:0000313|EMBL:AJE45050.1, ECO:0000313|Proteomes:UP000031521};
RN [1] {ECO:0000313|EMBL:AJE45050.1, ECO:0000313|Proteomes:UP000031521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P73 {ECO:0000313|EMBL:AJE45050.1};
RX PubMed=25256706; DOI=10.1099/ijs.0.069039-0;
RA Lai Q., Cao J., Yuan J., Li F., Shao Z.;
RT "Celeribacter indicus sp. nov., a polycyclic aromatic hydrocarbon-degrading
RT bacterium from deep-sea sediment and reclassification of Huaishuia
RT halophila as Celeribacter halophilus comb. nov.";
RL Int. J. Syst. Evol. Microbiol. 64:4160-4167(2014).
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DR EMBL; CP004393; AJE45050.1; -; Genomic_DNA.
DR RefSeq; WP_052452987.1; NZ_FNNW01000027.1.
DR AlphaFoldDB; A0A0B5DV09; -.
DR STRING; 1208324.P73_0335; -.
DR KEGG; cid:P73_0335; -.
DR HOGENOM; CLU_003827_17_0_5; -.
DR OrthoDB; 9792185at2; -.
DR Proteomes; UP000031521; Chromosome.
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; IPR008333; Cbr1-like_FAD-bd_dom.
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; PF00970; FAD_binding_6; 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:UP000031521}.
FT DOMAIN 1..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 227..312
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 312 AA; 33271 MW; D8B3ABAA39BC3C78 CRC64;
MEIHDFRIAR SAPIAEDTRA IRLEPVDGTS ELAFAPGDHV RLVLPSGEER AYSLVNAPAD
LEGYEIAVQV CPDGTGGSRE LCSLAAGTAV GVHTPRNAFR LHDGPGVSVL VAGGIGITPI
WCMAQSLARE GRPWRLYYAA RRAERAPFLA EVRALAADCG AEVEIAFSDQ GERLDLTRIV
GGIGPKDHLY CCGPDTLLDD FRAATFMVSD RAHTESFAVA EAAEGGFEVE LAQSGLVLTV
PEGYTILETV LEQGILVEYS CMGGTCGSCA TRVLEGTPDH RDSYLSEEEK AAGDKMLICC
SGSLTPRLVL DL
//
