ID   R6VQ67_9BACT            Unreviewed;       632 AA.
AC   R6VQ67;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=2-oxoglutarate ferredoxin oxidoreductase subunit beta {ECO:0000313|EMBL:CDC99180.1};
GN   ORFNames=BN673_00397 {ECO:0000313|EMBL:CDC99180.1};
OS   Prevotella sp. CAG:474.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262926 {ECO:0000313|EMBL:CDC99180.1, ECO:0000313|Proteomes:UP000018116};
RN   [1] {ECO:0000313|EMBL:CDC99180.1, ECO:0000313|Proteomes:UP000018116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:474 {ECO:0000313|Proteomes:UP000018116};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDC99180.1}.
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DR   EMBL; CBGF010000069; CDC99180.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6VQ67; -.
DR   STRING; 1262926.BN673_00397; -.
DR   Proteomes; UP000018116; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   InterPro; IPR022367; 2-oxoacid/accept_OxRdtase_asu.
DR   InterPro; IPR033412; PFOR_II.
DR   InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR   InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   NCBIfam; TIGR03710; OAFO_sf; 1.
DR   PANTHER; PTHR32154:SF20; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORA; 1.
DR   PANTHER; PTHR32154; PYRUVATE-FLAVODOXIN OXIDOREDUCTASE-RELATED; 1.
DR   Pfam; PF17147; PFOR_II; 1.
DR   Pfam; PF01558; POR; 1.
DR   Pfam; PF01855; POR_N; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018116}.
FT   DOMAIN          22..212
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          264..445
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          514..582
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
SQ   SEQUENCE   632 AA;  68960 MW;  32826A0AA56F6D62 CRC64;
     MEEDIVIKEL DQVVVRFSGD SGDGMQLAGN IFSTISATVG NDISTFPDYP ADIRAPQGSL
     TGVSGFQVHI GDGTVYTPGD RCDVLVAMNA AALKTQYKYT RPQATIIIDT DSFGPNDLRK
     ADFLTDDYLG ELGIDPDCVV ACPITTMVKH CLEDSGMDNK SILKCRNMFA LGMVCWLFDR
     NLELAEEFLH HKFGKKPQVA EANIRVVHAG YDYAHNTHAG VPATYRIETH SKVPGRYMDI
     TGNKATAYGL IAAAEKAGLK LYLGSYPITP ATDILHELSK HKSCGVITVQ CEDEISACAS
     AIGASFAGAL AATSTSGPGI CLKSEAINLA VIDELPLVII DVQRGGPSTG LPTKSEQTDL
     LQVLYGRNGE SPMPVIAATS PTDCFSAAYM AAKIALEHLT PVVLLTDAFI ANGSAAWRLP
     KMDELPEIHP HYATSDQRYR YTPYQRDPET CVRYWAIPGQ EGYAHILGGL EKDGKTGSIS
     TEPENHDLMD HLRSRKVARI EVPDLEVQGD KDDAELLIVG FGSTYGHLLS TLKELRGKGY
     KVALAQFKYV NPLPHNTVEV LNRYPKVVVA EQNLGQLAAL LRIRINNFSP YQYNKVKGQP
     FVVSELTEEF EKILLAPNRT KTGLTYEDNI IA
//