ID A0A1J5A312_9CHLR Unreviewed; 473 AA.
AC A0A1J5A312;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=2Fe-2S ferredoxin-type domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Fragment;
GN ORFNames=AUK03_08420 {ECO:0000313|EMBL:OIO93252.1};
OS Anaerolineae bacterium CG2_30_64_16.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1805005 {ECO:0000313|EMBL:OIO93252.1, ECO:0000313|Proteomes:UP000182267};
RN [1] {ECO:0000313|EMBL:OIO93252.1, ECO:0000313|Proteomes:UP000182267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_64_16 {ECO:0000313|EMBL:OIO93252.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
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:OIO93252.1}.
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DR EMBL; MNXL01000201; OIO93252.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5A312; -.
DR Proteomes; UP000182267; Unassembled WGS sequence.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR PANTHER; PTHR42659:SF2; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR Pfam; PF00111; Fer2; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
FT DOMAIN 1..175
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 368..444
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 449..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 473
FT /evidence="ECO:0000313|EMBL:OIO93252.1"
SQ SEQUENCE 473 AA; 51010 MW; E85A9CA68BADBB8D CRC64;
MWHTYYAPQT VADALDLLAR YGADCRVIAG GTDLILEIER GVRTQEVLVD ISRIAGLDRI
TREDGLLRLG ALTTHNQVVA SADAVTHAFP LARACWQVGA PQIRNRGTVA GNLTTASPAN
DTITPLWAMD ATVTLASRDR GERTLSFDQF FLGVRKTALA PDEMLVGINV PALGPHERGT
FLKLGLRQAQ AISVVNAAVV VESGIGYWVI PNTQYPISRA RIALGAVAPT IIRCPEAEDY
LVGKTLREDI IERAAELAAA AARPISDIRA SADYRRAMVR VLVARALRQL RDGTERQEWP
ERPVLLWGTA NRRTCPELGR RISESTNQRI GEPVLRSPLR SSKGLVEGSA NAPSSIPNAQ
YPIPNTQYPI TLHLNGKPTV LNNAHGKTLL RALREDAGLT GTKEGCAEGE CGACTVWLDG
IAVMSCLVPV ERADGCQVVT IEGLTNLTPQ PPSLRGKGEF SPLPVGEGLG ERL
//
