ID   DERI_AGRRK              Reviewed;         151 AA.
AC   B9JN19;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=D-erythrulose-4-phosphate isomerase {ECO:0000303|PubMed:29867142};
DE            EC=5.3.1.34 {ECO:0000269|PubMed:29867142};
GN   Name=derI {ECO:0000303|PubMed:29867142};
GN   OrderedLocusNames=Arad_7453 {ECO:0000312|EMBL:ACM28950.1};
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 D-erythrulose 4-phosphate to D-erythrose 4-phosphate.
CC       {ECO:0000269|PubMed:29867142}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrulose 4-phosphate = D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:48784, ChEBI:CHEBI:16897, ChEBI:CHEBI:90796;
CC         EC=5.3.1.34; Evidence={ECO:0000269|PubMed:29867142};
CC   -!- PATHWAY: Carbohydrate metabolism. {ECO:0000269|PubMed:29867142}.
CC   -!- SIMILARITY: Belongs to the LacAB/RpiB family. {ECO:0000305}.
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DR   EMBL; CP000629; ACM28950.1; -; Genomic_DNA.
DR   RefSeq; WP_012649302.1; NC_011983.1.
DR   AlphaFoldDB; B9JN19; -.
DR   SMR; B9JN19; -.
DR   STRING; 311403.Arad_7453; -.
DR   EnsemblBacteria; ACM28950; ACM28950; Arad_7453.
DR   KEGG; ara:Arad_7453; -.
DR   eggNOG; COG0698; Bacteria.
DR   HOGENOM; CLU_091396_1_0_5; -.
DR   OMA; ETHHANQ; -.
DR   OrthoDB; 1346802at2; -.
DR   BioCyc; MetaCyc:MON-20968; -.
DR   Proteomes; UP000001600; Chromosome 2.
DR   GO; GO:0016861; F:intramolecular oxidoreductase activity, interconverting aldoses and ketoses; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1400.10; -; 1.
DR   InterPro; IPR003500; RpiB_LacA_LacB.
DR   InterPro; IPR036569; RpiB_LacA_LacB_sf.
DR   Pfam; PF02502; LacAB_rpiB; 1.
DR   PIRSF; PIRSF005384; RpiB_LacA_B; 1.
DR   SUPFAM; SSF89623; SSF89623; 1.
DR   TIGRFAMs; TIGR00689; rpiB_lacA_lacB; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Isomerase; Reference proteome.
FT   CHAIN           1..151
FT                   /note="D-erythrulose-4-phosphate isomerase"
FT                   /id="PRO_0000446035"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P37351"
SQ   SEQUENCE   151 AA;  15674 MW;  9FF8F8BC52C25B32 CRC64;
     MKLAIAGDSA GEGLAKVLAD HLKDRYDVSE VSRTDAGPDA FYANLADRVA SGVIDGTYDK
     AILVCGTGIG VSISANKVPG IRAALTHDTY SAERAALSNN AQIITMGARV IGTELAKAIA
     DAFLARTFDT NGRSAGNVQA IDEVDAKYNA R