ID A0A134CKV2_9FIRM Unreviewed; 581 AA.
AC A0A134CKV2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=2-oxoacid:acceptor oxidoreductase, alpha subunit {ECO:0000313|EMBL:KXB92843.1};
GN ORFNames=HMPREF3191_00630 {ECO:0000313|EMBL:KXB92843.1};
OS Veillonellaceae bacterium DNF00626.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae.
OX NCBI_TaxID=1588754 {ECO:0000313|EMBL:KXB92843.1, ECO:0000313|Proteomes:UP000070542};
RN [1] {ECO:0000313|EMBL:KXB92843.1, ECO:0000313|Proteomes:UP000070542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00626 {ECO:0000313|EMBL:KXB92843.1,
RC ECO:0000313|Proteomes:UP000070542};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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:KXB92843.1}.
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DR EMBL; LSDR01000025; KXB92843.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A134CKV2; -.
DR STRING; 1588754.HMPREF3191_00630; -.
DR PATRIC; fig|1588754.3.peg.613; -.
DR Proteomes; UP000070542; 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:UP000070542}.
FT DOMAIN 15..176
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 210..451
FT /note="Pyruvate flavodoxin/ferredoxin oxidoreductase
FT pyrimidine binding"
FT /evidence="ECO:0000259|Pfam:PF01855"
FT DOMAIN 479..540
FT /note="Pyruvate:ferredoxin oxidoreductase core"
FT /evidence="ECO:0000259|Pfam:PF17147"
SQ SEQUENCE 581 AA; 63939 MW; A533D34AE5DCB5DA CRC64;
MEKKDFIWKM GGQQGQGVES CGEILGRVLA QEGYSLFSQR LFASRIKGGH TTIALRIATK
KVATIGEHVD CLVALDQETI DLHGKEVPEG GVVLADAAFH PKWEEHTGRI FLPLLITDLA
KKYGSMQMKN IAALGMSAGL LGFPELPFYR FIAERFAKKG NEIIDKNKGI FKEGYDIAIE
ALHGIELGKL ATPKKTDQFY LLGNEAAALG AISAGARFMA SYPITPATEI MEYVIKVIHK
IKGTVVQTED ELAAVTMAMG AGYAGVRAFT ATSGPGLSLM AESISMATMA EIPVVIIDVM
RAGPSTGMAT KVEQSDIRYA IGSGHGDAEK IVLAAASIED CYYITQEAFN LAEEFQTPVI
LLSDLQFGMC KQSVPAFDLN RIDIRRGKLV RDGLPPLNTQ KKDYFHRFED VEDGISPRTI
PGVENGMFLS TGLEHNVYGK PAEGQGDRVM EMNKRHRKWQ GVSSAIKPFY VTHEEPECDL
LLIGITSTDG ALEETREELE EAGYKVNHLH LRLLSPFPEK ELRPYIEGAK KVLIVEENLT
AQLRELFAIH FICHDKLLSL LQYDGTPFVT STIVNKAKEV L
//
