Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q88C93 (ALGC_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphomannomutase/phosphoglucomutase
Short name=PMM / PGM
EC=5.4.2.2
EC=5.4.2.8
Gene names
Name:algC
Ordered Locus Names:PP_5288
OrganismPseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]
Taxonomic identifier160488 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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

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

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Phosphomannomutase/phosphoglucomutase
PRO_0000147815

Sites

Active site1081Phosphoserine intermediate By similarity
Metal binding1081Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity
Binding site3251Substrate By similarity
Binding site3271Substrate By similarity
Binding site3291Substrate By similarity
Site4211Interacts with the biphosphorylated intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88C93 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: EAABA30BE7E926F1

FASTA46350,272
        10         20         30         40         50         60 
MAHLVPAALP DSIFRAYDIR GVVGKTLHAE TAYWIGRAIG AQSLAQGEPQ VSVGRDGRLS 

        70         80         90        100        110        120 
GPMLVEQLIK GLVDAGCNVS DVGLVPTPAL YYAANVLAGK SGVMLTGSHN PSDYNGFKIV 

       130        140        150        160        170        180 
IAGDTLANEQ IQALLTRLKT NDLTLAQGRV EKVEILDRYF KQIVGDVKLA KKLKVVVDCG 

       190        200        210        220        230        240 
NGAAGVVAPQ LIEALGCEVI PLFCEVDGNF PNHHPDPGKP ENLEDLIAKV KETGADIGLA 

       250        260        270        280        290        300 
FDGDGDRVGV VTNTGSIVYP DRLLMLFAQD VLSRNPGAEI IFDVKCTRRL TPLIEQHGGR 

       310        320        330        340        350        360 
ALMWKTGHSL IKKKMKQTGS LLAGEMSGHI FIKERWYGFD DGIYSAARLL EILSKTEQSA 

       370        380        390        400        410        420 
ENLFAAFPND ISTPEINIDV TDEGKFSIID ALQRDADWGE ANLTTIDGVR VDYANGWGLV 

       430        440        450        460 
RASNTTPVLV LRFEADSDAE LQRIKDVFRT QLLRVEPELQ LPF

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015451 Genomic DNA. Translation: AAN70853.1.
RefSeqNP_747389.1. NC_002947.3.

3D structure databases

ProteinModelPortalQ88C93.
SMRQ88C93. Positions 9-463.
ModBaseSearch...

Protein-protein interaction databases

STRING160488.PP_5288.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN70853; AAN70853; PP_5288.
GeneID1042276.
KEGGppu:PP_5288.
PATRIC19949422. VBIPsePut30601_5640.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268679.
KOK15778.
OMAVRTHSFR.
ProtClustDBCLSK869263.

Enzyme and pathway databases

BioCycPPUT160488:GIXO-5289-MONOMER.
UniPathwayUPA00030.
UPA00126; UER00424.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
InterProIPR005844. 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]
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALGC_PSEPK
AccessionPrimary (citable) accession number: Q88C93
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents