ID   ERYH_RHIEC              Reviewed;         267 AA.
AC   Q2JZQ2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=L-erythrulose-1-phosphate isomerase {ECO:0000250|UniProtKB:Q2YIQ6};
DE            EC=5.3.1.33 {ECO:0000250|UniProtKB:Q2YIQ6};
DE   AltName: Full=D-3-tetrulose-4-phosphate isomerase {ECO:0000250|UniProtKB:Q2YIQ6};
GN   Name=eryH {ECO:0000250|UniProtKB:Q2YIQ6}; Synonyms=tpiAf;
GN   OrderedLocusNames=RHE_PF00040;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42f.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to L-
CC       erythrulose-1P. {ECO:0000250|UniProtKB:Q2YIQ6}.
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:0000250|UniProtKB:Q2YIQ6};
CC   -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC       {ECO:0000250|UniProtKB:Q2YIQ6}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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; CP000138; ABC93934.1; -; Genomic_DNA.
DR   RefSeq; WP_011428351.1; NC_007766.1.
DR   AlphaFoldDB; Q2JZQ2; -.
DR   SMR; Q2JZQ2; -.
DR   EnsemblBacteria; ABC93934; ABC93934; RHE_PF00040.
DR   KEGG; ret:RHE_PF00040; -.
DR   HOGENOM; CLU_024251_2_3_5; -.
DR   OMA; CIGEKTH; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000001936; Plasmid p42f.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; 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   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   PANTHER; PTHR21139; PTHR21139; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; SSF51351; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Pentose shunt; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..267
FT                   /note="L-erythrulose-1-phosphate isomerase"
FT                   /id="PRO_0000236166"
FT   ACT_SITE        95
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   ACT_SITE        168
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         211
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
SQ   SEQUENCE   267 AA;  29175 MW;  3A6085823E800D93 CRC64;
     MVVWVGTSFK MNKTLEEALA FARRLADADL ERDPRVQRFV IPSFTAVREV KRVLTESSVK
     VGAQNMHWED AGAWTGEISP LMLKDCRLDL VELGHSERRE HFGETDETVG LKAAAAIRHG
     LTPLICIGET LQERNEGRAD AVLRRQVEAA LRGVDTEAGE APILLAYEPV WAIGVNGIPA
     TADYASERHR GIAEVAKSIL GRPVPVLYGG SVNPGNCEEL IGQPDIDGLF IGRSAWSVEG
     YLDILARVSA AIDRSSPRQT ASERKLP