ID   ERYH_BRUAB              Reviewed;         256 AA.
AC   P0C119; Q578Z0; Q9ZB27;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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, tpiA-2;
GN   OrderedLocusNames=BruAb2_0363;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017224; AAX75794.1; -; Genomic_DNA.
DR   RefSeq; WP_002965777.1; NC_006933.1.
DR   AlphaFoldDB; P0C119; -.
DR   SMR; P0C119; -.
DR   PRIDE; P0C119; -.
DR   EnsemblBacteria; AAX75794; AAX75794; BruAb2_0363.
DR   GeneID; 45053873; -.
DR   GeneID; 55592508; -.
DR   KEGG; bmb:BruAb2_0363; -.
DR   HOGENOM; CLU_024251_2_3_5; -.
DR   OMA; VWAIGEH; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000000540; 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_0000090189"
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