P0C7J2 (XANA_XANCP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphohexose mutases

Including the following 2 domains:

1. Phosphoglucomutase
   Short name=PGM
   EC=5.4.2.2
   Alternative name(s):
   Glucose phosphomutase
2. Phosphomannomutase
   Short name=PMM
   EC=5.4.2.8

Gene names

Name:	xanA
Ordered Locus Names:	XCC0626

Organism

Xanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]

Taxonomic identifier

190485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas › Xanthomonas campestris › Xanthomonas campestris pv. campestris

Protein attributes

Sequence length	448 AA.
Sequence status	Complete.
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.
Sequence caution	The sequence AAM39942.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Exopolysaccharide synthesis Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro 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 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33913 / NCPPB 528 / LMG 568.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008922 Genomic DNA. Translation: AAM39942.1. Different initiation.
RefSeq	NP_636018.1. NC_003902.1.
3D structure databases
ProteinModelPortal	P0C7J2.
ModBase	Search...
Protein-protein interaction databases
STRING	190485.XCC0626.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM39942; AAM39942; XCC0626.
GeneID	999354.
KEGG	xcc:XCC0626.
PATRIC	24071904. VBIXanCam115730_0687.
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268679.
KO	K15778.
OMA	AHDMRES.
ProtClustDB	CLSK881246.
Enzyme and pathway databases
UniPathway	UPA00126; UER00424.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
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. Alpha-D-phosphohexomutase_SF. [Graphical view]
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.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program