ID A0A2A4Z6N1_9PROT Unreviewed; 309 AA.
AC A0A2A4Z6N1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Ferredoxin {ECO:0000313|EMBL:PCJ02622.1};
GN ORFNames=COB13_05185 {ECO:0000313|EMBL:PCJ02622.1};
OS OCS116 cluster bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; OCS116 cluster.
OX NCBI_TaxID=2030921 {ECO:0000313|EMBL:PCJ02622.1, ECO:0000313|Proteomes:UP000218076};
RN [1] {ECO:0000313|Proteomes:UP000218076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-2017) 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:PCJ02622.1}.
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DR EMBL; NVUS01000004; PCJ02622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A4Z6N1; -.
DR Proteomes; UP000218076; 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:SF1; CARNITINE MONOOXYGENASE REDUCTASE SUBUNIT; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 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}.
FT DOMAIN 1..100
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 226..309
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 309 AA; 34448 MW; 3DF3F6E487D38817 CRC64;
MHAEIIRKRM LTPSVCEFTF TVDDGNLPTF EPGSHITVET PSGAMRRYSL VNDGRNSPEN
YVIAIKSETT SRGGSLSMHE QTEEGTILRI SPPENTFPLK EAADYLLIAG GIGITPIYSM
ARHLTDLGKS FRIIYCTKNV DDSPYLDELK NKFNAKLLVN HTLGVAENRF DFWDYFAKIK
NMHVYCCGPE PLTEEIKAIS GHWPEGRVNF EDFKPVEVTR ADDVAFEVTL QKSNQTITIP
ADRSILEAIR DSGIDTISSC ESGTCGSCKS RLIKGDVDHR DMVLMDDEKA DQIMICVSRP
ATGDLTIDL
//
