ID Q04RI5_LEPBJ Unreviewed; 324 AA.
AC Q04RI5;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138, ECO:0000256|RuleBase:RU364074};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU364074};
GN Name=acoB {ECO:0000313|EMBL:ABJ76485.1};
GN OrderedLocusNames=LBJ_1967 {ECO:0000313|EMBL:ABJ76485.1};
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=355277 {ECO:0000313|EMBL:ABJ76485.1, ECO:0000313|Proteomes:UP000000656};
RN [1] {ECO:0000313|EMBL:ABJ76485.1, ECO:0000313|Proteomes:UP000000656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB197 {ECO:0000313|EMBL:ABJ76485.1,
RC ECO:0000313|Proteomes:UP000000656};
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO2.
CC {ECO:0000256|RuleBase:RU364074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU364074};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
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DR EMBL; CP000350; ABJ76485.1; -; Genomic_DNA.
DR RefSeq; WP_011670034.1; NC_008510.1.
DR AlphaFoldDB; Q04RI5; -.
DR KEGG; lbj:LBJ_1967; -.
DR PATRIC; fig|355276.3.peg.1678; -.
DR HOGENOM; CLU_012907_1_1_12; -.
DR Proteomes; UP000000656; Chromosome 1.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; 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; IPR027110; PDHB.
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; PTHR11624; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 324 AA; 35678 MW; 399193BA1FDBB4B3 CRC64;
MAILTYREAL NRAMCEEMDK DPNIFLMGEE VGHYDGAYKV SQGMLAKYGE KRVIDTPISE
NGFAGVGIGA AMVGLRPIIE FMTWNFSLVA IDQIINSAAK MNYMSAGQFP IPIVFRGAGG
AGGRLAAQHS QSFESWYAHI PGLKVIAPYT PADACGLLKT AIRDNNPTIF IESEVLYGSR
GEVPDQEYSI PFGKADLKRE GSDITIVSWS RALQYVLPAA ERLSQEGISV EVLDLRSIRP
LDEEAIYASV RKTNRALIVE EGWEVAGFGS QVAYLIQKNS FDDLDAPVER ITQEDVPMPY
AANLEKASLP SEEKIIAKVR EMLE
//
