ID A0A254QUY7_9RHOB Unreviewed; 318 AA.
AC A0A254QUY7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:OWU71784.1};
GN ORFNames=ATO1_23000 {ECO:0000313|EMBL:OWU71784.1};
OS Phaeobacter sp. 22II1-1F12B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1317111 {ECO:0000313|EMBL:OWU71784.1, ECO:0000313|Proteomes:UP000197279};
RN [1] {ECO:0000313|EMBL:OWU71784.1, ECO:0000313|Proteomes:UP000197279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-1F12B {ECO:0000313|EMBL:OWU71784.1,
RC ECO:0000313|Proteomes:UP000197279};
RA Lai Q., Li G., Shao Z.;
RT "Phaeobacter sp. 22II1-1F12B Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:OWU71784.1}.
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DR EMBL; AQQP01000022; OWU71784.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254QUY7; -.
DR OrthoDB; 9792185at2; -.
DR Proteomes; UP000197279; 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; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF2; PHENOXYBENZOATE DIOXYGENASE BETA SUBUNIT; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 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:UP000197279}.
FT DOMAIN 1..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 233..318
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 318 AA; 33868 MW; 69FC88BBD60F09BB CRC64;
MSAITLTVKE VRKAAELIRM VTLVAPDGGS LPPYEAGAHA EVHLPDGATR PYSLIDFDGA
AKEPKAYVFG IRLEDESRGG SRFMHGLAEG DTVTVEPAKN DFPLAGDDAP SVLIAGGIGI
TPMISMATAL KAEGRDYRLH YAIRDESAAA FIEQLTQNHG DCLSVHCDDQ AGGPLDIAKV
LSDANPEAHI YVCGPKPMIE AVKSKAESAG YPAERVHFEL FDAAADQDGD SAFEVEVAST
GAVYTIPPGK TIIDVLEEAG EDLIYDCQRG DCGICQTDVL EGTPDHRDVV LSQAERDSGK
VMQICVSRAK SARLKLDI
//
