ID   LERI_AGRRK              Reviewed;         261 AA.
AC   B9JN20;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Arad_7454 {ECO:0000312|EMBL:ACM28951.1};
OS   Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=311403;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K84 / ATCC BAA-868;
RX   PubMed=19251847; DOI=10.1128/jb.01779-08;
RA   Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA   Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA   Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA   Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA   Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA   Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT   "Genome sequences of three Agrobacterium biovars help elucidate the
RT   evolution of multichromosome genomes in bacteria.";
RL   J. Bacteriol. 191:2501-2511(2009).
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; CP000629; ACM28951.1; -; Genomic_DNA.
DR   RefSeq; WP_007689316.1; NC_011983.1.
DR   AlphaFoldDB; B9JN20; -.
DR   SMR; B9JN20; -.
DR   STRING; 311403.Arad_7454; -.
DR   EnsemblBacteria; ACM28951; ACM28951; Arad_7454.
DR   KEGG; ara:Arad_7454; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_5; -.
DR   OMA; VWAIGEH; -.
DR   OrthoDB; 1266295at2; -.
DR   BioCyc; MetaCyc:MON-20967; -.
DR   Proteomes; UP000001600; Chromosome 2.
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; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..261
FT                   /note="L-erythrulose-1-phosphate isomerase"
FT                   /id="PRO_0000446037"
FT   ACT_SITE        99
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
FT   ACT_SITE        172
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10127"
SQ   SEQUENCE   261 AA;  28482 MW;  757F861260153393 CRC64;
     MTASPRYWIG TSWKMNKTLA EARGFAEALR DADALRDPAI QRFIIPPFTA VREVKSILSD
     TSVKVGAQNM HWADQGAWTG EVSPLMLRDC NLDIVELGHS ERREHFGETN ETVGLKTEAA
     VRHGLIPLIC IGETLSDRES GRAAEILSEQ VVGALSKLSG SQKQAQILLA YEPVWAIGEK
     GIPAEPSYAD ARQAEIIAVA EKVLGRRIPC LYGGSVNPDN CEELISCPHI DGLFIGRSAW
     NVEGYLDILA KCAAKLRGDT K