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Entry: E3I601_RHOVT
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Original site: E3I601_RHOVT 
ID   E3I601_RHOVT            Unreviewed;       470 AA.
AC   E3I601;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
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   OrderedLocusNames=Rvan_1333 {ECO:0000313|EMBL:ADP70594.1};
OS   Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS   4299).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Rhodomicrobium.
OX   NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP70594.1, ECO:0000313|Proteomes:UP000001399};
RN   [1] {ECO:0000313|Proteomes:UP000001399}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC   {ECO:0000313|Proteomes:UP000001399};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(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; CP002292; ADP70594.1; -; Genomic_DNA.
DR   RefSeq; WP_013418996.1; NC_014664.1.
DR   AlphaFoldDB; E3I601; -.
DR   STRING; 648757.Rvan_1333; -.
DR   KEGG; rva:Rvan_1333; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_012907_0_0_5; -.
DR   OMA; SRMRHHC; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000001399; 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|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          2..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          89..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   470 AA;  49625 MW;  97B91CC073C4F443 CRC64;
     MATQVLMPAL SPTMEEGKLA KWVKAEGDDV RSGDVIAEIE TDKATMEVEA VDEGKIGKIL
     VPAGTEGVKV NTPIAIILAE GEEAGASLNG AGKTNGAHAP ADAATGGGET ARAPVDVRVK
     DQPREAVAPA AYDAASEIPE GAELVQITMR EALRDAMAEE MRRDGDVFVM GEEVAEYQGA
     YKITQGLLDE FGARRVVDTP ITEAGFAGLG VGAAFAGLRP IVEFMTFNFA MQAIDHIINS
     AAKTHYMSGG QIDCPIVFRG PNGAAARVGA QHSQEYSAWY AHVPGLKVIA PSTAADAKGL
     LKAAIRDPNP VVFLENEILY GIAGPVPKGD DWLVPIGKAK IARPGKDVTI VSWSRGMVYA
     LDAAKQLEAD GIDAEVIDLR TLRPLDIDTV LASVRKTNRI VTVEEAWPVC SVGSEIVAQV
     VAKAFDYLDA PPTKVSGEDV PMPYAANLEK LALPNAQKVV EAVKAVCYRS
//
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