ID   ERYH_RHILO              Reviewed;         254 AA.
AC   Q986N6;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
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}; OrderedLocusNames=mlr7275;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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}.
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DR   EMBL; BA000012; BAB53417.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q986N6; -.
DR   SMR; Q986N6; -.
DR   STRING; 266835.14026821; -.
DR   EnsemblBacteria; BAB53417; BAB53417; BAB53417.
DR   KEGG; mlo:mlr7275; -.
DR   eggNOG; COG0149; Bacteria.
DR   HOGENOM; CLU_024251_2_3_5; -.
DR   OMA; CIGEKTH; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000000552; Chromosome.
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.
FT   CHAIN           1..254
FT                   /note="L-erythrulose-1-phosphate isomerase"
FT                   /id="PRO_0000090275"
FT   ACT_SITE        97
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
SQ   SEQUENCE   254 AA;  27199 MW;  336F73D7EB87F653 CRC64;
     MRVVYWVGTS WKMNKTLAEA LDFAERLAGF IPGFDDRIQP FVIPPFTAVR EVKRALSSTR
     IKVGAQNMHW ADAGAWTGEI SPPMLRDCGL DLVELGHSER REHFGETDRT VGLKTAAAVK
     HGMIPLICVG ETLAERESGQ ADAVLSAQVE GALQFLEGEA KTAKILFAYE PVWAIGDKGI
     PASADYADKQ QALIKTVAGA LLPSVPPVLY GGSVNPGNAA ELVGQPNIDG LFIGRSAWQA
     DGYIDILGRA SAAI