GenomeNet

Database: UniProt
Entry: Q98MY8_RHILO
LinkDB: Q98MY8_RHILO
Original site: Q98MY8_RHILO 
ID   Q98MY8_RHILO            Unreviewed;       461 AA.
AC   Q98MY8;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   24-JAN-2024, entry version 133.
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=mlr0384 {ECO:0000313|EMBL:BAB47975.1};
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB47975.1, ECO:0000313|Proteomes:UP000000552};
RN   [1] {ECO:0000313|EMBL:BAB47975.1, ECO:0000313|Proteomes:UP000000552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC   {ECO:0000313|Proteomes:UP000000552};
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000012; BAB47975.1; -; Genomic_DNA.
DR   RefSeq; WP_010909332.1; NC_002678.2.
DR   AlphaFoldDB; Q98MY8; -.
DR   KEGG; mlo:mlr0384; -.
DR   PATRIC; fig|266835.9.peg.304; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_012907_0_1_5; -.
DR   OMA; SRMRHHC; -.
DR   Proteomes; UP000000552; 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   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN          2..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          85..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  48866 MW;  85A8FBA80E40DB36 CRC64;
     MPIEILMPAL SPTMEEGNLS KWLKNEGDKV VAGDVIAEIE TDKATMEVEA VDEGTLAKIV
     VPAGTEGVKV NAVIAVLAVE GEDTDKAGEG IGEEPAKAET ASPAPVAAKS EAAAPVAAAP
     KTEIAADPDI PAGTEMVSTT VREALRDAMA EEMRRDGDVF VMGEEVAEYQ GAYKITQGLL
     QEFGPRRVVD TPITEHGFAG VGVGAAMAGL KPIVEFMTFN FAMQAIDQII NSAAKTLYMS
     GGQMGAPIVF RGPNGAAARV AAQHSQCYAA WYSHIPGLKV VMPYTAADAK GLLKAAIRDP
     NPVIFLENEI LYGQSFDVPK LDDFVLPIGK ARIHKQGKDV TIVSFGIGMT YAVKAEAELR
     GLGIDAEIID LRTIRPLDLD TIIASVKKTN RLVVVEEGFP QSSVGDHIAN QVSQRAFDFL
     DAPVITIAGK DVPMPYAANL EKLALPNVGE VIEAVKAVTY R
//
DBGET integrated database retrieval system