ID   ERYB_BRUA2              Reviewed;         502 AA.
AC   Q2YIQ2; Q9ZB31;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=D-erythritol 1-phosphate dehydrogenase {ECO:0000303|PubMed:163226};
DE            EC=1.1.1.402 {ECO:0000269|PubMed:163226, ECO:0000269|PubMed:25453104};
GN   Name=eryB {ECO:0000303|PubMed:10708387};
GN   OrderedLocusNames=BAB2_0371 {ECO:0000312|EMBL:CAJ12537.1};
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, AND CATALYTIC ACTIVITY.
RC   STRAIN=19;
RX   PubMed=163226; DOI=10.1128/jb.121.2.619-630.1975;
RA   Sperry J.F., Robertson D.C.;
RT   "Erythritol catabolism by Brucella abortus.";
RL   J. Bacteriol. 121:619-630(1975).
RN   [4]
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 oxydation of D-erythritol 1-phosphate to D-
CC       erythrulose 1-phosphate. {ECO:0000269|PubMed:163226,
CC       ECO:0000269|PubMed:25453104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythritol 1-phosphate + NADP(+) = D-erythrulose 1-phosphate
CC         + H(+) + NADPH; Xref=Rhea:RHEA:49620, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:131767,
CC         ChEBI:CHEBI:131849; EC=1.1.1.402;
CC         Evidence={ECO:0000269|PubMed:163226, ECO:0000269|PubMed:25453104};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P13035};
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}.
CC   -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; U57100; AAD11520.1; -; Genomic_DNA.
DR   EMBL; AM040265; CAJ12537.1; -; Genomic_DNA.
DR   RefSeq; WP_002965781.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YIQ2; -.
DR   SMR; Q2YIQ2; -.
DR   STRING; 359391.BAB2_0371; -.
DR   EnsemblBacteria; CAJ12537; CAJ12537; BAB2_0371.
DR   GeneID; 3827518; -.
DR   KEGG; bmf:BAB2_0371; -.
DR   PATRIC; fig|359391.11.peg.2323; -.
DR   HOGENOM; CLU_015740_5_0_5; -.
DR   OMA; FAYSDCW; -.
DR   PhylomeDB; Q2YIQ2; -.
DR   BioCyc; MetaCyc:MON-19885; -.
DR   UniPathway; UPA01066; -.
DR   PRO; PR:Q2YIQ2; -.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:InterPro.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.8.870; -; 1.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR031656; DAO_C.
DR   InterPro; IPR038299; DAO_C_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000447; G3P_DH_FAD-dep.
DR   PANTHER; PTHR11985; PTHR11985; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF16901; DAO_C; 1.
DR   PRINTS; PR01001; FADG3PDH.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00977; FAD_G3PDH_1; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..502
FT                   /note="D-erythritol 1-phosphate dehydrogenase"
FT                   /id="PRO_0000446538"
FT   BINDING         8..36
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        47
FT                   /note="R -> A (in Ref. 1; AAD11520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="D -> I (in Ref. 1; AAD11520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166..170
FT                   /note="AEKGA -> RRKGS (in Ref. 1; AAD11520)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   502 AA;  56191 MW;  F3D0FAE51B352540 CRC64;
     MAEPETCDLF VIGGGINGAG VARDAAGRGL KVVLAEKDDL AQGTSSRSGK LVHGGLRYLE
     YYEFRLVREA LIEREVLLNA APHIIWPMRF VLPHSPQDRP AWLVRLGLFL YDHLGGRKKL
     PGTRTLDLKR DPEGTPILDQ YTKGFEYSDC WVDDARLVAL NAVGAAEKGA TILTRTPVVS
     ARRENGGWIV ETRNSDTGET RTFRARCIVN CAGPWVTDVI HNVAASTSSR NVRLVKGSHI
     IVPKFWSGAN AYLVQNHDKR VIFINPYEGD KALIGTTDIA YEGRAEDVAA DEKEIDYLIT
     AVNRYFKEKL RREDVLHSFS GVRPLFDDGK GNPSAVTRDY VFDLDETGGA PLLNVFGGKI
     TTFRELAERG MHRLKHIFPQ MGGDWTHDAP LPGGEIANAD YETFANTLRD TYPWMPRTLV
     HHYGRLYGAR TKDVVAGAQN LEGLGRHFGG DFHEAEVRYL VAREWAKTAE DILYRRTKHY
     LHLTEAERAA FVEWFDNANL VA