ID A6U8E9_SINMW Unreviewed; 465 AA.
AC A6U8E9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Smed_1077 {ECO:0000313|EMBL:ABR59929.1};
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR59929.1, ECO:0000313|Proteomes:UP000001108};
RN [1] {ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR59929.1, ECO:0000313|Proteomes:UP000001108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419 {ECO:0000313|EMBL:ABR59929.1,
RC ECO:0000313|Proteomes:UP000001108};
RX PubMed=21304680; DOI=10.4056/sigs.43526;
RA Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT "Complete genome sequence of the Medicago microsymbiont Ensifer
RT (Sinorhizobium) medicae strain WSM419.";
RL Stand. Genomic Sci. 2:77-86(2010).
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; CP000738; ABR59929.1; -; Genomic_DNA.
DR RefSeq; WP_011975253.1; NC_009636.1.
DR RefSeq; YP_001326764.1; NC_009636.1.
DR AlphaFoldDB; A6U8E9; -.
DR STRING; 366394.Smed_1077; -.
DR GeneID; 61612141; -.
DR KEGG; smd:Smed_1077; -.
DR PATRIC; fig|366394.8.peg.4200; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_0_1_5; -.
DR OrthoDB; 9780894at2; -.
DR Proteomes; UP000001108; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU364074}.
FT DOMAIN 2..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 91..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 49289 MW; 8F89C4EEFE773BAF CRC64;
MPVEILMPAL SPTMEEGTLS KWLKNEGDKV SSGDVIAEIE TDKATMEVEA VDEGTIGKLL
IAAGTEGVKV NTPIAVLLQD GEAASDIDTA KAEAPKAEAP KAEAPKQGDP EAPAASAAPV
AAQPRADVPS DPAIPAGTEM VTMTVREALR DAMAEEMRAN DDVFVMGEEV AEYQGAYKIT
QGLLQEFGAR RVVDTPITEH GFAGVGVGAA MTGLRPIVEF MTFNFAMQAI DQIINSAAKT
LYMSGGQMGA PIVFRGPSGA AARVAAQHSQ CYAAWYSHIP GLKVVMPYTA ADAKGLLKAA
IRDPNPIIFL ENEILYGQSF DVPKLDDFVL PIGKARIHRA GKDATLVSFG IGMTYAIKAA
AELEAQGIDV EIIDLRTIRP MDLPTVIESV KKTGRLVTVE EGYPQSSVGT EIATRVMQQA
FDYLDAPVLT IAGKDVPMPY AANLEKLALP SVAEVVEAVK AVCYK
//
