ID   ERYH_BRUSU              Reviewed;         256 AA.
AC   Q8FVH2; G0KDN1;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=tpiA-2;
GN   OrderedLocusNames=BRA0869, BS1330_II0862;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014292; AAN34042.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20319.1; -; Genomic_DNA.
DR   RefSeq; WP_002965777.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FVH2; -.
DR   SMR; Q8FVH2; -.
DR   EnsemblBacteria; AEM20319; AEM20319; BS1330_II0862.
DR   GeneID; 45053873; -.
DR   GeneID; 55592508; -.
DR   KEGG; bms:BRA0869; -.
DR   KEGG; bsi:BS1330_II0862; -.
DR   PATRIC; fig|204722.21.peg.440; -.
DR   HOGENOM; CLU_024251_2_3_5; -.
DR   OMA; VWAIGEH; -.
DR   PhylomeDB; Q8FVH2; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000007104; Chromosome II.
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   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..256
FT                   /note="L-erythrulose-1-phosphate isomerase"
FT                   /id="PRO_0000090194"
FT   ACT_SITE        96
FT                   /note="Electrophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   ACT_SITE        169
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
FT   BINDING         212
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WG43"
SQ   SEQUENCE   256 AA;  27871 MW;  809780A0B12568A6 CRC64;
     MTKFWIGTSW KMNKTLAEAR LFAEALKAAD AGRSPDIQRF VIPPFTAVRE VKEILSGTSV
     KVGAQNMHWA DQGAWTGEIS PLMLKDCNLD IVELGHSERR EHFGETNETV GLKVEAAVRH
     GLIPLICIGE TLEDRESGRA AAVLEEEVRG ALSKLSEAQK QAEILFAYEP VWAIGENGIP
     ASADYADARQ AEIIAVAQSV LARRVPCLYG GSVNPGNCEE LIACPHIDGL FIGRSAWNVE
     GYLDILARCA TKVQAN