GenomeNet

Database: UniProt
Entry: Q2GHV6_EHRCR
LinkDB: Q2GHV6_EHRCR
Original site: Q2GHV6_EHRCR 
ID   Q2GHV6_EHRCR            Unreviewed;       332 AA.
AC   Q2GHV6;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   28-FEB-2018, entry version 76.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
GN   OrderedLocusNames=ECH_0149 {ECO:0000313|EMBL:ABD44682.1};
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD44682.1, ECO:0000313|Proteomes:UP000008320};
RN   [1] {ECO:0000313|EMBL:ABD44682.1, ECO:0000313|Proteomes:UP000008320}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU364074};
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; CP000236; ABD44682.1; -; Genomic_DNA.
DR   RefSeq; WP_011452429.1; NC_007799.1.
DR   ProteinModelPortal; Q2GHV6; -.
DR   STRING; 205920.ECH_0149; -.
DR   EnsemblBacteria; ABD44682; ABD44682; ECH_0149.
DR   KEGG; ech:ECH_0149; -.
DR   eggNOG; ENOG4105CPP; Bacteria.
DR   eggNOG; COG0022; LUCA.
DR   HOGENOM; HOG000281450; -.
DR   KO; K00162; -.
DR   OMA; SRMRHHC; -.
DR   OrthoDB; POG091H04FE; -.
DR   BioCyc; ECHA205920:G1G5L-123-MONOMER; -.
DR   Proteomes; UP000008320; Chromosome.
DR   GO; GO:0045250; C:cytosolic pyruvate dehydrogenase complex; ISS:TIGR.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:TIGR.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:TIGR.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR027110; PDHB.
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:SF94; PTHR11624:SF94; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000008320};
KW   Glycolysis {ECO:0000256|RuleBase:RU364074};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364074};
KW   Pyruvate {ECO:0000256|RuleBase:RU364074, ECO:0000313|EMBL:ABD44682.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008320};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU364074}.
FT   DOMAIN        4    179       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   332 AA;  36412 MW;  9A24912D70D51138 CRC64;
     MRTLTVREAL CEAIREEMER DHTVLIMGEE VGEYQGAYKV TQGLLEQFGP DRVIDTPITE
     HGFAGIGVGA AFAGLKPIVE FMTFNFAMQA IDQIINSAAK TSYMSGGQLN CPIVFRGPNG
     AAARVGAQHS QCYASWYAHI PGLKVVSPYF AADCKGLLKA AIRDLNPVVF LENEIAYGHK
     HEIPNEVSTS DYITEIGKAA IVKEGTDITI TAFSLQVKFA LEAAELLAKE GINAEVIDLR
     TLRPLDTETI LRSIKKTNKI ISIEEGWPYS GIGSEIAALI MEYAFDDLDA PMIRITGKDV
     PLPYATNLEK LALPQIEDIL EAARALCIRN YR
//
DBGET integrated database retrieval system