ID   XANA_XANCB              Reviewed;         448 AA.
AC   B0RVK5; P29955;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Phosphohexose mutases;
DE   Includes:
DE     RecName: Full=Phosphoglucomutase;
DE              Short=PGM;
DE              EC=5.4.2.2;
DE     AltName: Full=Glucose phosphomutase;
DE   Includes:
DE     RecName: Full=Phosphomannomutase;
DE              Short=PMM;
DE              EC=5.4.2.8;
GN   Name=xanA; OrderedLocusNames=xcc-b100_3729;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1370280; DOI=10.1128/jb.174.1.191-199.1992;
RA   Koeplin R., Arnold W., Hoette B., Simon R., Wang G., Puehler A.;
RT   "Genetics of xanthan production in Xanthomonas campestris: the xanA and
RT   xanB genes are involved in UDP-glucose and GDP-mannose biosynthesis.";
RL   J. Bacteriol. 174:191-199(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
CC   -!- FUNCTION: Involved in xanthan production.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC         Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC         EC=5.4.2.8;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 2/2.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; AF204145; AAA27610.1; -; Genomic_DNA.
DR   EMBL; AM920689; CAP53096.1; -; Genomic_DNA.
DR   PIR; A43304; A43304.
DR   AlphaFoldDB; B0RVK5; -.
DR   SMR; B0RVK5; -.
DR   PRIDE; B0RVK5; -.
DR   KEGG; xca:xcc-b100_3729; -.
DR   HOGENOM; CLU_016950_9_2_6; -.
DR   OMA; PITCFKA; -.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000001188; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Isomerase; Lipopolysaccharide biosynthesis;
KW   Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN           1..448
FT                   /note="Phosphohexose mutases"
FT                   /id="PRO_0000333186"
FT   ACT_SITE        97
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  48922 MW;  221961862CAEAB8F CRC64;
     MTLPAFKAYD IRGRVPDELN EDLARRIGVA LAAQLDQGPV VLGHDVRLAS PALQEALSAG
     LRASGREVID IGLCGTEEVY FQTDHLKAAG GVMVTASHNP MDYNGMKLVR EQARPISSDT
     GLFAIRDTVA ADTAAAGEPT AAEHSRTDKT AYLEHLLSYV DRSTLKPLKL VVNAGNGGAG
     LIVDLLAPHL PFEFVRVFHE PDGNFPNGIP NPLLQENRDA TAKAVKEHGA DFGIAWDGDF
     DRCFFFDHTG RFIEGYYLVG LLAQAILAKQ PGGKVVHDPR LTWNTVEMVE DAGGIPVLCK
     SGHAFIKEKM RSENAVYGGE MSAHHYFREF AYADSGMIPW LLIAELVSQS GRSLADLVEA
     RMQKFPCSGE INFKVDDAKA AVARVMAHYG DQSPELDYTD GISADFGQWR FNLRSSNTEP
     LLRLNVETRG DAALLETRTQ EISNLLRG