ID   ERYH_BRUME              Reviewed;         256 AA.
AC   Q8YCV3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=BMEII0425;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL53667.1; -; Genomic_DNA.
DR   PIR; AH3562; AH3562.
DR   RefSeq; WP_004682245.1; NZ_GG703779.1.
DR   AlphaFoldDB; Q8YCV3; -.
DR   SMR; Q8YCV3; -.
DR   STRING; 224914.BMEII0425; -.
DR   EnsemblBacteria; AAL53667; AAL53667; BMEII0425.
DR   GeneID; 29595239; -.
DR   KEGG; bme:BMEII0425; -.
DR   PATRIC; fig|224914.52.peg.2950; -.
DR   eggNOG; COG0149; Bacteria.
DR   OMA; VWAIGEH; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000000419; 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_0000090192"
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;  27848 MW;  89F049D4B1306707 CRC64;
     MTKFWIGTSW KMNKTLAEAR LFAEALKAAD AGRSPDIQRF VIPPFTAVRE VKEILSGTSV
     KVGAQNMHWA DQGTWTGEIS PLMLKDCNLD IVELGHSERR EHFGETNETV GLKVEAAVRH
     GLIPLICIGE TLEDCESGRA AAVLEEEVRG ALSKLSEAQK QAEILFAYEP VWAIGENGIP
     ASADYADARQ AEIIAVAQSV LARRVPCLYG GSVNPGNCEE LIACPHIDGL FIGRSAWNVE
     GYLDILARCA TKVQAN