ID Q2BYJ7_9GAMM Unreviewed; 327 AA.
AC Q2BYJ7;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Putaive pyruvate dehydrogenase E1 component, beta subunit {ECO:0000313|EMBL:EAR53835.1};
GN ORFNames=SKA34_04310 {ECO:0000313|EMBL:EAR53835.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR53835.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR53835.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR53835.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:EAR53835.1}.
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DR EMBL; AAOU01000042; EAR53835.1; -; Genomic_DNA.
DR RefSeq; WP_006643832.1; NZ_CH724141.1.
DR AlphaFoldDB; Q2BYJ7; -.
DR HOGENOM; CLU_012907_1_0_6; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000005284; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Pyruvate {ECO:0000313|EMBL:EAR53835.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 35895 MW; E47F238CC2A4C474 CRC64;
MADITLIEAV NLALHYEMQH DPNVVILGED IAENGGVFRA TLGLKQAFGC KRVIDTPLAE
SLIAGVTVGM ASQGLRPIAE FQFQGFIFPA MEHLVCHAAR LRNRTRGRLT CPAVFRAPFG
GGIHAPEHHS ESIEAMFAHI PGLKVVIPSS PQRAYGLLLA AIRSNDPILF FEPKRIYRTV
KSHVENNGLA LPLDQCFTLR KGTDITLVTW GACVVESLQA AETLSQHGIE LDVIDLASIK
PIDMATISAS LEKTGRLLVV HEAAKTCGVG AEIITRVAES AMFLLKAPPK RLTGFDTIMP
YYRNEDYFMI QHDDIVNAAR ELMEGWQ
//
