ODPB_ZYMMO
ID ODPB_ZYMMO Reviewed; 462 AA.
AC O66113; O69012; Q5NM31;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE EC=1.2.4.1;
GN Name=pdhB; Synonyms=pdhAbeta; OrderedLocusNames=ZMO1605;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29191 / DSM 3580 / JCM 10190 / CECT 560 / NBRC 13756 / NCIMB
RC 11199 / NRRL B-4490 / ZM6;
RX PubMed=9515924; DOI=10.1128/jb.180.6.1540-1548.1998;
RA Neveling U., Klasen R., Bringer-Meyer S., Sahm H.;
RT "Purification of the pyruvate dehydrogenase multienzyme complex of
RT Zymomonas mobilis and identification and sequence analysis of the
RT corresponding genes.";
RL J. Bacteriol. 180:1540-1548(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee J., Jin S., Kang H.S.;
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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 -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Note=Binds 1 thiamine pyrophosphate per subunit.;
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
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DR EMBL; Y12884; CAA73385.1; -; Genomic_DNA.
DR EMBL; AF086791; AAC70362.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV90229.1; -; Genomic_DNA.
DR PIR; T33723; T33723.
DR RefSeq; WP_011241359.1; NZ_CP035711.1.
DR AlphaFoldDB; O66113; -.
DR SMR; O66113; -.
DR STRING; 264203.ZMO1605; -.
DR EnsemblBacteria; AAV90229; AAV90229; ZMO1605.
DR GeneID; 58027324; -.
DR KEGG; zmo:ZMO1605; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_012907_0_2_5; -.
DR OMA; SRMRHHC; -.
DR OrthoDB; 900125at2; -.
DR Proteomes; UP000001173; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR011053; Single_hybrid_motif.
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; PTHR11624; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Glycolysis; Lipoyl; Oxidoreductase; Pyruvate; Reference proteome;
KW Thiamine pyrophosphate.
FT CHAIN 1..462
FT /note="Pyruvate dehydrogenase E1 component subunit beta"
FT /id="PRO_0000162237"
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 195
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT CONFLICT 87
FT /note="D -> E (in Ref. 1; CAA73385)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="V -> L (in Ref. 1; CAA73385)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..244
FT /note="SAAKTHYMSGGQV -> LRPKRIICPAAKC (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="R -> P (in Ref. 2; AAC70362)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="A -> E (in Ref. 2; AAC70362)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 49833 MW; 00F53CE4A5731F1C CRC64;
MAIELKMPAL SPTMEEGTLT RWLVKEGDSI KAGEILAEIE TDKAIMEFEA VDEGVITKIL
IPEGSENVKV GTAIAYLGTD ANDVTLDGAS AETKAEESAP VASPAKTEAA AVEEAATPSL
GKVINSAPEI PEGTEFFQQT LREALRDAMA EEMRRDDRVF VMGEEVAEYQ GAYKVTQGLL
QEFGARRVVD TPISEYGFSG IGVGAAMEGL RPVIEFMTMN FSMQAIDHII NSAAKTHYMS
GGQVRCPIVF RGPNGAAPRV GAQHTQNFGP WYAAVPGLVV LAPYDAIDAK GLLKAAIRSD
DPVVFLECEL LYGKTFDVPK MDDFVLPIGK ARIIREGKDV TIVSYSIGVS FALTAAEALA
KEGIDAEVID LRTLRPLDKE TILQSLAKTN RIVTVEDGWP VCSISSEIAA IAMEEGFDNL
DAPVLRVTNA DTPTPYAENL EKKGLVNPEA IIEAVRKVCY RK
