ID   ERYH_BRUA2              Reviewed;         256 AA.
AC   Q2YIQ6; Q578Z0; Q9ZB27;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=L-erythrulose-1-phosphate isomerase {ECO:0000305|PubMed:25453104};
DE            EC=5.3.1.33 {ECO:0000269|PubMed:25453104};
DE   AltName: Full=D-3-tetrulose-4-phosphate isomerase {ECO:0000303|PubMed:25453104};
GN   Name=eryH {ECO:0000303|PubMed:25453104};
GN   Synonyms=tpiA-2 {ECO:0000312|EMBL:CAJ12533.1}; OrderedLocusNames=BAB2_0367;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=10708387; DOI=10.1099/00221287-146-2-487;
RA   Sangari F.J., Aguero J., Garcia-Lobo J.M.;
RT   "The genes for erythritol catabolism are organized as an inducible operon
RT   in Brucella abortus.";
RL   Microbiology 146:487-495(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=2308;
RX   PubMed=25453104; DOI=10.1073/pnas.1414622111;
RA   Barbier T., Collard F., Zuniga-Ripa A., Moriyon I., Godard T., Becker J.,
RA   Wittmann C., Van Schaftingen E., Letesson J.J.;
RT   "Erythritol feeds the pentose phosphate pathway via three new isomerases
RT   leading to D-erythrose-4-phosphate in Brucella.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:17815-17820(2014).
CC   -!- FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to L-
CC       erythrulose-1P. Involved in the degradation pathway of erythritol, that
CC       allows B.abortus to grow on this compound as the sole carbon source.
CC       {ECO:0000269|PubMed:25453104}.
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:0000269|PubMed:25453104};
CC   -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC       {ECO:0000269|PubMed:25453104}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WG43}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on erythritol
CC       as sole carbon source, in contrast to wild-type.
CC       {ECO:0000269|PubMed:25453104}.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; U57100; AAD11524.1; -; Genomic_DNA.
DR   EMBL; AM040265; CAJ12533.1; -; Genomic_DNA.
DR   RefSeq; WP_002965777.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YIQ6; -.
DR   SMR; Q2YIQ6; -.
DR   STRING; 359391.BAB2_0367; -.
DR   EnsemblBacteria; CAJ12533; CAJ12533; BAB2_0367.
DR   GeneID; 45053873; -.
DR   GeneID; 55592508; -.
DR   KEGG; bmf:BAB2_0367; -.
DR   PATRIC; fig|359391.11.peg.2319; -.
DR   HOGENOM; CLU_024251_2_3_5; -.
DR   OMA; VWAIGEH; -.
DR   PhylomeDB; Q2YIQ6; -.
DR   BioCyc; MetaCyc:MON-19887; -.
DR   BRENDA; 5.3.1.33; 994.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000002719; 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:0005975; P:carbohydrate metabolic process; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN           1..256
FT                   /note="L-erythrulose-1-phosphate isomerase"
FT                   /id="PRO_0000090190"
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