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Database: UniProt
Entry: W5QSX6_9BACT
LinkDB: W5QSX6_9BACT
Original site: W5QSX6_9BACT 
ID   W5QSX6_9BACT            Unreviewed;       570 AA.
AC   W5QSX6;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=2-oxoglutarate synthase alpha subunit {ECO:0000313|EMBL:AGH14077.1};
DE   Flags: Fragment;
OS   Prevotella sp. Sc00044.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1231730 {ECO:0000313|EMBL:AGH14077.1};
RN   [1] {ECO:0000313|EMBL:AGH14077.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sc00044 {ECO:0000313|EMBL:AGH14077.1};
RX   PubMed=24448980; DOI=10.1007/s10295-013-1395-y;
RA   Rosewarne C.P., Pope P.B., Cheung J.L., Morrison M.;
RT   "Analysis of the bovine rumen microbiome reveals a diversity of Sus-like
RT   polysaccharide utilization loci from the bacterial phylum Bacteroidetes.";
RL   J. Ind. Microbiol. Biotechnol. 41:601-606(2014).
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DR   EMBL; JX424623; AGH14077.1; -; Genomic_DNA.
DR   AlphaFoldDB; W5QSX6; -.
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}.
FT   DOMAIN          2..166
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          213..398
FT                   /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT                   pyrimidine binding"
FT                   /evidence="ECO:0000259|Pfam:PF01855"
FT   DOMAIN          468..541
FT                   /note="Pyruvate:ferredoxin oxidoreductase core"
FT                   /evidence="ECO:0000259|Pfam:PF17147"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGH14077.1"
SQ   SEQUENCE   570 AA;  61747 MW;  910C13F03F3A6D17 CRC64;
     TFPDYPADIR APQGSLTGVS GFQVHIGAGK VYTPGDKCDV LVAMNAAALK TQYRYAKPGA
     TIIIDTDSFG PKDLEKAQFA TEDYLGEMGI DPDRVIQCPL TTMVKDCLAD SGMDNKAMLK
     CRNMFALGLV CWLFDRDLNL VANFLREKFA KKPAIAEANI KVIQAGWDYG HNTHSSAINV
     YRVETKEKTP GRYMDITGNK ATAYGFIAAA EKAGLRLYLG SYPITPATDV LHELSKHKSC
     GVITVQCEDE ISGCASALGA SFAGALGVTS TSGPGVCLKS EAMNLAVIME LPLVVLDVQR
     GGPATGLPTK SEQTDLLQAL FGRNGESPMP VMAATSPADC FDAAYQAAKM ALEHMTPVVL
     LTDAYIANGS GAFKLPEMAK LDAINPPYVP EELKGKWTPY MRAENGTRYW AVPGREGFAH
     ILGGLEKDSE TGAISTNPEN HDLMTRLRQQ KIDNIQVPDL EVDGDADADL LIVGFGSTYG
     HLHSAMDELK AKGYKVAQAQ FKYLNPLPKN TAAVLTKYKK VVVAEQNMGQ LAAYLRMKVD
     GFVPYQFNQV KGQPFVVEEL VNAFEDILKK
//
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