ID   ERYC_BRUA2              Reviewed;         310 AA.
AC   Q2YIQ3; Q9ZB30;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=D-erythrulose 1-phosphate 3-epimerase {ECO:0000305};
DE            EC=5.1.3.38 {ECO:0000269|PubMed:25453104};
DE   AltName: Full=3-tetrulose-4-phosphate racemase {ECO:0000303|PubMed:25453104};
GN   Name=eryC {ECO:0000303|PubMed:10708387};
GN   OrderedLocusNames=BAB2_0370 {ECO:0000312|EMBL:CAJ12536.1};
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], AND INDUCTION.
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, AND PATHWAY.
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 racemization of D-erythrulose 1-phosphate to L-
CC       erythrulose 1-phosphate. {ECO:0000269|PubMed:25453104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrulose 1-phosphate = L-erythrulose 1-phosphate;
CC         Xref=Rhea:RHEA:49584, ChEBI:CHEBI:58002, ChEBI:CHEBI:131767;
CC         EC=5.1.3.38; Evidence={ECO:0000269|PubMed:25453104};
CC   -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC       {ECO:0000269|PubMed:25453104}.
CC   -!- INDUCTION: Induced by erythritol and repressed by EryD.
CC       {ECO:0000269|PubMed:10708387}.
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DR   EMBL; U57100; AAD11521.1; -; Genomic_DNA.
DR   EMBL; AM040265; CAJ12536.1; -; Genomic_DNA.
DR   RefSeq; WP_002965780.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YIQ3; -.
DR   SMR; Q2YIQ3; -.
DR   STRING; 359391.BAB2_0370; -.
DR   EnsemblBacteria; CAJ12536; CAJ12536; BAB2_0370.
DR   GeneID; 45126182; -.
DR   KEGG; bmf:BAB2_0370; -.
DR   PATRIC; fig|359391.11.peg.2322; -.
DR   HOGENOM; CLU_076068_0_0_5; -.
DR   OMA; IKQSSMN; -.
DR   PhylomeDB; Q2YIQ3; -.
DR   BioCyc; MetaCyc:MON-19886; -.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036237; Xyl_isomerase-like_sf.
DR   InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR   Pfam; PF01261; AP_endonuc_2; 1.
DR   SUPFAM; SSF51658; SSF51658; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..310
FT                   /note="D-erythrulose 1-phosphate 3-epimerase"
FT                   /id="PRO_0000446539"
FT   CONFLICT        106
FT                   /note="G -> A (in Ref. 1; AAD11521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262..263
FT                   /note="EG -> D (in Ref. 1; AAD11521)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   310 AA;  35011 MW;  1E94EEA7C3D09DD5 CRC64;
     MALTLSLNTN PLVNRFAEPD DLIETVARDL RLRDLQLTHE FINPSWQAST IRRLTRDMDR
     ALQRTGVRVT SGMTGPYGRL NHFGHPDRDV RRYYVDWFKT FADIIGDLGG KSVGTQFAIF
     TYKDFDDPAR REELIKIAID CWAEVAEHAA GAGLDYVFWE PMSIGREFGE TIAECMKLQD
     RLTAANMAIP MWMMADIDHG DVTSANPDDY DPYAWARTVP KVSPIIHIKQ SLMDKGGHRP
     FTAAFNAKGR IQPEPLLKAF AEGGAVDNEI CLELSFKERE PNDREVIPQI AESVAFWAPH
     IDTGAKDLKI