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Protein

Phosphomannomutase/phosphoglucomutase

Gene

algC

Organism
Pseudomonas syringae pv. tomato (strain DC3000)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

The phosphomannomutase activity produces a precursor for alginate polymerization. The alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core-LPS biosynthesis due to its phosphoglucomutase activity. Essential for biofilm production (By similarity).By similarity

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei110 – 1101Phosphoserine intermediateBy similarity
Metal bindingi110 – 1101Magnesium; via phosphate groupBy similarity
Metal bindingi244 – 2441MagnesiumBy similarity
Metal bindingi246 – 2461MagnesiumBy similarity
Metal bindingi248 – 2481MagnesiumBy similarity
Binding sitei327 – 3271SubstrateBy similarity
Binding sitei329 – 3291SubstrateBy similarity
Binding sitei331 – 3311SubstrateBy similarity
Sitei423 – 4231Interacts with the biphosphorylated intermediateBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphoglucomutase activity Source: UniProtKB-EC
  3. phosphomannomutase activity Source: JCVI

GO - Biological processi

  1. alginic acid biosynthetic process Source: UniProtKB-KW
  2. carbohydrate metabolic process Source: JCVI
  3. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  4. lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Alginate biosynthesis, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciPSYR223283:GJIX-83-MONOMER.
UniPathwayiUPA00030.
UPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase/phosphoglucomutase (EC:5.4.2.2, EC:5.4.2.8)
Short name:
PMM / PGM
Gene namesi
Name:algC
Ordered Locus Names:PSPTO_0083
OrganismiPseudomonas syringae pv. tomato (strain DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002515 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465Phosphomannomutase/phosphoglucomutasePRO_0000147816Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi223283.PSPTO_0083.

Structurei

3D structure databases

ProteinModelPortaliQ88BD4.
SMRiQ88BD4. Positions 11-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
KOiK15778.
OMAiAWFNLRA.
OrthoDBiEOG6W9X55.
PhylomeDBiQ88BD4.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q88BD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSPASVAPI LPDTIFRAYD IRGVVEDTLN AETAYWIGRA IGSESLAQNE
60 70 80 90 100
PNVSVGRDGR LSGPELVQQL IQGLHDSGCH VSDVGLVPTP ALYYAANVLA
110 120 130 140 150
GKTGVMLTGS HNPKDYNGFK IVIAGDTLAN EQIQALHERI KTNNLTSQKG
160 170 180 190 200
SITQVNILDR YFKQIKDDIV MARKLKVVVD CGNGAAGVIA PQLIEALGCE
210 220 230 240 250
VISLFAEVDG NFPNHHPDPG KLENLQDLIA KVKETGADLG LAFDGDGDRV
260 270 280 290 300
GVVTNAGNVV YPDRLLMLFA LDVLKRNPGA DIIFDVKCTR RLTPLISEHG
310 320 330 340 350
GRPVMWKTGH SLIKKEMKKS GALLAGEMSG HIFFKERWFG FDDGIYSAAR
360 370 380 390 400
LLEILSQEPA NAEDLFETFP NDISTPEINI KVTDVTKFSI IEALEKDAQW
410 420 430 440 450
GDAKLTTIDG VRVDYPKGWG LVRASNTTPV LVLRFEAETQ AELERIQGVF
460
HAELKKVAPD LDLPF
Length:465
Mass (Da):50,692
Last modified:May 31, 2003 - v1
Checksum:iA078D8A974111C2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016853 Genomic DNA. Translation: AAO53637.1.
RefSeqiNP_789942.1. NC_004578.1.

Genome annotation databases

EnsemblBacteriaiAAO53637; AAO53637; PSPTO_0083.
GeneIDi1181691.
KEGGipst:PSPTO_0083.
PATRICi19991314. VBIPseSyr93040_0087.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016853 Genomic DNA. Translation: AAO53637.1.
RefSeqiNP_789942.1. NC_004578.1.

3D structure databases

ProteinModelPortaliQ88BD4.
SMRiQ88BD4. Positions 11-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223283.PSPTO_0083.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO53637; AAO53637; PSPTO_0083.
GeneIDi1181691.
KEGGipst:PSPTO_0083.
PATRICi19991314. VBIPseSyr93040_0087.

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
KOiK15778.
OMAiAWFNLRA.
OrthoDBiEOG6W9X55.
PhylomeDBiQ88BD4.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00126; UER00424.
BioCyciPSYR223283:GJIX-83-MONOMER.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DC3000.

Entry informationi

Entry nameiALGC_PSESM
AccessioniPrimary (citable) accession number: Q88BD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2003
Last sequence update: May 31, 2003
Last modified: January 6, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.