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Database: UniProt
Entry: B9NPX7_9RHOB
LinkDB: B9NPX7_9RHOB
Original site: B9NPX7_9RHOB 
ID   B9NPX7_9RHOB            Unreviewed;       457 AA.
AC   B9NPX7;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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:EEE38146.1};
GN   ORFNames=RKLH11_1987 {ECO:0000313|EMBL:EEE38146.1};
OS   Rhodobacteraceae bacterium KLH11.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE38146.1, ECO:0000313|Proteomes:UP000005135};
RN   [1] {ECO:0000313|Proteomes:UP000005135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX   PubMed=21742885; DOI=10.1128/jb.05556-11;
RA   Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT   "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT   Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL   J. Bacteriol. 193:5011-5012(2011).
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; DS999531; EEE38146.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9NPX7; -.
DR   STRING; 467661.RKLH11_1987; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_0_3_5; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000005135; Unassembled WGS sequence.
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|RuleBase:RU364074,
KW   ECO:0000313|EMBL:EEE38146.1};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005135};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          2..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   457 AA;  48768 MW;  1969F9471D962526 CRC64;
     MATEILMPAL SPTMEEGTLA KWLVKEGDTV SSGDIMAEIE TDKATMEFEA VDEGIIGKIL
     IEEGAEGVKV NTPIAILVEE GEDASALPAA APAAAAGTEA APAAVEEAAP VATAPAAPVV
     DLSPDWPADA EMAQQTVREA LRDAMAEEMR GDEDVYLMGE EVAEYQGAYK ISQGLLDEFG
     AKRVIDTPIT EHGFAGIAVG SAFGGLKPIV EFMTFNFAMQ AIDQIINSAA KTLYMSGGQM
     GCPIVFRGPN GAAARVAAQH SQDYTAWYMQ IPGLKVVMPY SAADAKGLLK SAIRDPNPVV
     FLENEILYGR SFDMPQVDDL TIPLGKARIW REGSDVTIVS FGIGMQYALE AADKLAEDGI
     SAEVIDLRTI RPMDTGAILN SVMKTNRLVT VEEGWPQGSV GNYISSVVMQ EAFDYLDAPV
     INCTGKDVPM PYAANLEKLA LITTDEVIEA VKQVTYR
//
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