ID   ERYA_BRUA2              Reviewed;         520 AA.
AC   Q2YIQ1; Q578Y5; Q9ZB32;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Erythritol kinase;
DE            EC=2.7.1.215 {ECO:0000269|PubMed:12639570};
GN   Name=eryA {ECO:0000303|PubMed:10708387}; OrderedLocusNames=BAB2_0372;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   STRAIN=2308;
RX   PubMed=12639570; DOI=10.1016/s0960-894x(02)01032-6;
RA   Lillo A.M., Tetzlaff C.N., Sangari F.J., Cane D.E.;
RT   "Functional expression and characterization of EryA, the erythritol kinase
RT   of Brucella abortus, and enzymatic synthesis of L-erythritol-4-phosphate.";
RL   Bioorg. Med. Chem. Lett. 13:737-739(2003).
CC   -!- FUNCTION: Catalyzes the phosphorylation of erythritol to D-erythritol-
CC       1-phosphate. {ECO:0000269|PubMed:12639570}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + erythritol = ADP + D-erythritol 1-phosphate + H(+);
CC         Xref=Rhea:RHEA:49624, ChEBI:CHEBI:15378, ChEBI:CHEBI:17113,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:131849, ChEBI:CHEBI:456216;
CC         EC=2.7.1.215; Evidence={ECO:0000269|PubMed:12639570};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.26 mM for erythritol {ECO:0000269|PubMed:12639570};
CC         KM=9.8 mM for ATP {ECO:0000269|PubMed:12639570};
CC   -!- PATHWAY: Carbohydrate metabolism; erythritol degradation.
CC       {ECO:0000269|PubMed:12639570}.
CC   -!- INDUCTION: Induced by erythritol and repressed by EryD.
CC       {ECO:0000269|PubMed:10708387}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ12538.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U57100; AAD11519.2; -; Genomic_DNA.
DR   EMBL; AM040265; CAJ12538.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2YIQ1; -.
DR   SMR; Q2YIQ1; -.
DR   STRING; 359391.BAB2_0372; -.
DR   PRIDE; Q2YIQ1; -.
DR   EnsemblBacteria; CAJ12538; CAJ12538; BAB2_0372.
DR   KEGG; bmf:BAB2_0372; -.
DR   HOGENOM; CLU_009281_3_1_5; -.
DR   BioCyc; MetaCyc:MON-19884; -.
DR   BRENDA; 2.7.1.215; 994.
DR   UniPathway; UPA01066; -.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047878; F:erythritol kinase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..520
FT                   /note="Erythritol kinase"
FT                   /id="PRO_0000418773"
SQ   SEQUENCE   520 AA;  54632 MW;  4F809172A55DA01A CRC64;
     MSAMREKGDI IIGIDAGTSV LKAVAFDFSG RQIESAAVRN TYVTGDHGAV TQSLAQTWQD
     CARALRDLGA KLPGLAQRTA AIAVTGQGDG TWLVGKDNRP VGDAWIWLDA RAASTVTRLA
     AGPMNRARFE ATGTGLNTCQ QGAQMAHMDT IAPELLDNAE AALHCKDWLY LNLTGVRATD
     PSEASFTFGN FRTRQYDDVV IEALGLQKRR NLLPEIIDGS QSQHPLSAEA AAATGLLAGT
     PVSLGYVDMA MTALGAGVCG GTAGAGCSTI GSTGVHMRAK PVADIHLNKE GTGYVIALPI
     PGIVTQVQTN MGATINIDWI LQVAADLMST PEKPVSLGDL IPRLDDWFNA SRPGAILYHP
     YISEAGERGP FVNANARAGF IGLSSRDRFP ELVRSVVEGL GMATRDCYAA MGEMPAELRI
     TGGAARSKAL RGTLSAAVNA PVRVSAREEA GAAGAAMMAA VAIGAYPAMD DCIAEWVEPL
     LGASEAPDAA RAHQYEELFV AYREARLALA PVWDKLASGK