ID   XANA_XANCP              Reviewed;         448 AA.
AC   P0C7J2; P29955;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=XCC0626;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- FUNCTION: Involved in xanthan production. {ECO:0000250}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM39942.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008922; AAM39942.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_636018.1; NC_003902.1.
DR   RefSeq; WP_014506571.1; NC_003902.1.
DR   AlphaFoldDB; P0C7J2; -.
DR   SMR; P0C7J2; -.
DR   STRING; 190485.XCC0626; -.
DR   EnsemblBacteria; AAM39942; AAM39942; XCC0626.
DR   GeneID; 58014817; -.
DR   KEGG; xcc:XCC0626; -.
DR   PATRIC; fig|190485.4.peg.687; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_9_2_6; -.
DR   OrthoDB; 9803322at2; -.
DR   UniPathway; UPA00126; UER00424.
DR   Proteomes; UP000001010; 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   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1.
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; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Exopolysaccharide synthesis; Isomerase; Lipopolysaccharide biosynthesis;
KW   Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..448
FT                   /note="Phosphohexose mutases"
FT                   /id="PRO_0000147817"
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;  48891 MW;  44C25C25F6939F5C CRC64;
     MTLPAFKAYD IRGRVPDELN EDLARRIGVA LAAQLDQGPV VLGHDVRLAS PALQEALSAG
     LRASGREVID IGLCGTEEVY FQTDHLKAAG GVMVTASHNP MDYNGMKLVR EQARPISSDT
     GLFAIRDTVA ADTAAAGEPT AAEHSRTDKT AYLEHLLSYV DRSTLKPLKL VVNAGNGGAG
     LIVDLLAPHL PFEFVRVFHE PDGNFPNGIP NPLLPENRDA TAKAVKEHGA DFGIAWDGDF
     DRCFFFDHTG RFIEGYYLVG LLAQAILAKQ PGGKVVHDPR LTWNTVEMVE DAGGIPVLCK
     SGHAFIKEKM RSENAVYGGE MSAHHYFREF AYADSGMIPW LLIAELVSQS GRSLADLVEA
     RMQKFPCSGE INFKVDDAKA AVARVMAHYG DQSPELDYTD GISADFGQWR FNLRSSNTEP
     LLRLNVETRG DAALLETRTQ EISNLLRG
//