XANA_XANCP
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 03-AUG-2022, entry version 74.
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; Proteobacteria; 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; 340.xcc-b100_3729; -.
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 OMA; PITCFKA; -.
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 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; 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
