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LERI_PECAS
ID   LERI_PECAS              Reviewed;         259 AA.
AC   Q6D8V5;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=L-erythrulose-1-phosphate isomerase {ECO:0000303|PubMed:29867142};
DE            EC=5.3.1.33 {ECO:0000269|PubMed:29867142};
GN   Name=lerI {ECO:0000303|PubMed:29867142};
GN   OrderedLocusNames=ECA0867 {ECO:0000312|EMBL:CAG73779.1};
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=29867142; DOI=10.1038/s41589-018-0067-7;
RA   Carter M.S., Zhang X., Huang H., Bouvier J.T., Francisco B.S.,
RA   Vetting M.W., Al-Obaidi N., Bonanno J.B., Ghosh A., Zallot R.G.,
RA   Andersen H.M., Almo S.C., Gerlt J.A.;
RT   "Functional assignment of multiple catabolic pathways for D-apiose.";
RL   Nat. Chem. Biol. 14:696-705(2018).
CC   -!- FUNCTION: Involved in catabolism of D-apiose. Catalyzes the
CC       isomerization of L-erythrulose 1-phosphate to D-erythrulose 4-
CC       phosphate. {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-erythrulose 1-phosphate = D-erythrulose 4-phosphate;
CC         Xref=Rhea:RHEA:49588, ChEBI:CHEBI:58002, ChEBI:CHEBI:90796;
CC         EC=5.3.1.33; Evidence={ECO:0000269|PubMed:29867142};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10127}.
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DR   EMBL; BX950851; CAG73779.1; -; Genomic_DNA.
DR   RefSeq; WP_011092470.1; NC_004547.2.
DR   AlphaFoldDB; Q6D8V5; -.
DR   SMR; Q6D8V5; -.
DR   STRING; 218491.ECA0867; -.
DR   EnsemblBacteria; CAG73779; CAG73779; ECA0867.
DR   KEGG; eca:ECA0867; -.
DR   PATRIC; fig|218491.5.peg.867; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_6; -.
DR   OMA; VWAIGEH; -.
DR   OrthoDB; 1266295at2; -.
DR   BioCyc; MetaCyc:MON-20963; -.
DR   Proteomes; UP000007966; Chromosome.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00311; TIM; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR035990; TIM_sf.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..259
FT                   /note="L-erythrulose-1-phosphate isomerase"
FT                   /id="PRO_0000446038"
FT   ACT_SITE        102
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
SQ   SEQUENCE   259 AA;  28140 MW;  36D6AFBA95CC3D69 CRC64;
     MSSRKLTLGV SLKMYFGYQQ TLDWCQKIHE IAEQHPLASL PSARLFVLPA FPTLAPVVQR
     FAQSPVHVGA QDLHWTDNGA FTGEVSGTML HEMGCRYVEI GHAERRRYFG ETDEHFALKT
     AAAWRNGLTP VLCVGEEQRG STQQAIDTCQ AQLAAALNLA QKQQLTGDLV LAYEPQWAIG
     STEPAPTAYI SEVCQALKQH LPTQAGVREG RIIYGGSAGP GLLSQLGDAV DGLFLGRFAH
     DPAAFNAIMD EAFTLSSQA
 
 
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