Reviewed, UniProtKB/Swiss-Prot P0C7J2 (XANA_XANCP)

Names and origin

Protein names

Recommended name:
    Phosphohexose mutases
Including the following 2 domains:
    1- Recommended name:
            Phosphoglucomutase
                Short name=PGM
              EC=5.4.2.2
        Alternative name(s):
            Glucose phosphomutase
    2- Recommended name:
            Phosphomannomutase
                Short name=PMM
              EC=5.4.2.8

Gene names

Name:	xanA
Ordered Locus Names:	XCC0626

Organism

Xanthomonas campestris pv. campestris [Complete proteome] [HAMAP]

Taxonomic identifier

340 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Involved in xanthan production By similarity.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Exopolysaccharide synthesis Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Inferred from electronic annotation. Source: EC phosphomannomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 448	448	Phosphohexose mutases		PRO_0000147817
Sites
	Active site	97	1	Phosphoserine intermediate By similarity
	Metal binding	97	1	Magnesium; via phosphate group By similarity
	Metal binding	237	1	Magnesium By similarity
	Metal binding	239	1	Magnesium By similarity
	Metal binding	241	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C7J2-1 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: 44C25C25F6939F5C	FASTA	448	48,891
	10 20 30 40 50 60 MTLPAFKAYD IRGRVPDELN EDLARRIGVA LAAQLDQGPV VLGHDVRLAS PALQEALSAG 70 80 90 100 110 120 LRASGREVID IGLCGTEEVY FQTDHLKAAG GVMVTASHNP MDYNGMKLVR EQARPISSDT 130 140 150 160 170 180 GLFAIRDTVA ADTAAAGEPT AAEHSRTDKT AYLEHLLSYV DRSTLKPLKL VVNAGNGGAG 190 200 210 220 230 240 LIVDLLAPHL PFEFVRVFHE PDGNFPNGIP NPLLPENRDA TAKAVKEHGA DFGIAWDGDF 250 260 270 280 290 300 DRCFFFDHTG RFIEGYYLVG LLAQAILAKQ PGGKVVHDPR LTWNTVEMVE DAGGIPVLCK 310 320 330 340 350 360 SGHAFIKEKM RSENAVYGGE MSAHHYFREF AYADSGMIPW LLIAELVSQS GRSLADLVEA 370 380 390 400 410 420 RMQKFPCSGE INFKVDDAKA AVARVMAHYG DQSPELDYTD GISADFGQWR FNLRSSNTEP 430 440 LLRLNVETRG DAALLETRTQ EISNLLRG

References

[1]

"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities." da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P. , Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P. Nature 417:459-463(2002) [PubMed: 12024217] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008922 Genomic DNA. Translation: AAM39942.1. Different initiation.
RefSeq	NP_636018.1.
3D structure databases
HSSP	HSSP built from PDB template 1K2Y based on UniProtKB P26276.
ModBase	Search...
Genome annotation databases
GeneID	999354.
GenomeReviews	Gene locus XCC0626 in contig AE008922_GR.
KEGG	xcc:XCC0626.
Organism-specific databases
CMR	Search...
Family and domain databases
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XANA_XANCP

Accession

Primary (citable) accession number: P0C7J2
Secondary accession number(s): P29955

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	October 13, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)