ID B4RBV7_PHEZH Unreviewed; 481 AA.
AC B4RBV7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=pdhB {ECO:0000313|EMBL:ACG78154.1};
GN OrderedLocusNames=PHZ_c1743 {ECO:0000313|EMBL:ACG78154.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG78154.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG78154.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG78154.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU364074};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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DR EMBL; CP000747; ACG78154.1; -; Genomic_DNA.
DR RefSeq; WP_012522296.1; NC_011144.1.
DR AlphaFoldDB; B4RBV7; -.
DR STRING; 450851.PHZ_c1743; -.
DR KEGG; pzu:PHZ_c1743; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_012907_0_0_5; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000001868; Chromosome.
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; cd06849; lipoyl_domain; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 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; DEHYDROGENASE RELATED; 1.
DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 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; Single hybrid motif; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 4: Predicted;
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364074};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 1..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 70..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 51829 MW; 4FFF746E3B18E8EC CRC64;
MTDILMPALS PTMEEGTLAK WHVKPGDKVR SGDVIAEIET DKATMEVEAV DDGVVAEILV
PEGSQEVKVN TPIARLQGED GTAQPSKAPS KTEAAQTEAV QTDTIAEKPF RKEPSGDEEK
KGPSEAKGER PEGEGPAAVT PDRPLADPEI PEGVQLVKQT VRDALRDAMA EEMRRDPDVF
LMGEEVAQYQ GAYKVSRGLL DEFGDRRVID TPITEHGFAG LGVGAGMAGL KPIVEFMTFN
FAMQAIDQII NSAAKTLYMS GGQLKTSVVF RGPNGAAARV AAQHSQDYAA WYAHVPGLKV
IAPYDAADAK GLLKAAIRDP NPVVFLEHEM LYGQEFDVPE GIDWVVPIGK AKVRRPGKDV
TIVGYSRMVG LALKAAEELA AEGIEAEVID LRTLRPLDHE TVVESVKKTN RLVTVEEGWG
PMGVGAEVAA RVVEHAFDWL DAPPARVCQE DVPLPYAANL EALSLPSVER IVKAAKAVSY
R
//
