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Protein

Phosphomannomutase

Gene

manB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of the capsular polysaccharide colanic acid.

Catalytic activityi

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

Cofactori

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

Pathway:iGDP-alpha-D-mannose biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphomannomutase (manB), Phosphomannomutase (rfbK)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei98 – 981Phosphoserine intermediateBy similarity
Metal bindingi98 – 981Magnesium; via phosphate groupBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi247 – 2471MagnesiumBy similarity
Metal bindingi249 – 2491MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Capsule biogenesis/degradation, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciSENT99287:GCTI-2116-MONOMER.
UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
Name:manB
Synonyms:cpsG, rfbL
Ordered Locus Names:STM2104
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456PhosphomannomutasePRO_0000147822Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi99287.STM2104.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LLLmodel-A1-456[»]
ProteinModelPortaliP26341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
KOiK01840.
OMAiNRQDTID.
OrthoDBiEOG6W9X55.
PhylomeDBiP26341.

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.

P26341-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKLTCFKAY DIRGRLGEEL NEDIAWRIGR AYGEYLKPKT VVLGGDVRLT
60 70 80 90 100
SEALKLALAK GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN
110 120 130 140 150
PMDYNGMKLV REGARPISGD TGLRDVQRLA EAGDFPPVNE AARGSYRQIS
160 170 180 190 200
LRDAYIDHLL GYISVNNLTP LKLVFNAGNG AAGPVIDAIE ARLKALGAPV
210 220 230 240 250
EFIKIHNTPD GTFPNGIPNP LLPECRDDTR KAVIEHGADM GIAFDGDFDR
260 270 280 290 300
CFLFDEKGQF IEGYYIVGLL AEAFLEKHPG AKIIHDPRLT WNTEAVVTAA
310 320 330 340 350
GGTPVMSKTG HAFIKERMRT EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL
360 370 380 390 400
VAELVCLKRQ SLGELVRDRM AAFPASGEIN SRLAEPAAAI ARVEAHFAEE
410 420 430 440 450
AQAVDRTDGL SMSFADWRFN LRSSNTEPVV RLNVESRGDI PLMEARTRTL

LALLNQ
Length:456
Mass (Da):50,002
Last modified:January 23, 2002 - v2
Checksum:i6E32422242AF2CE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 562KL → NV in CAA42541 (PubMed:1712067).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59886 Genomic DNA. Translation: CAA42541.1.
AE006468 Genomic DNA. Translation: AAL21008.1.
PIRiS16291.
RefSeqiNP_461049.1. NC_003197.1.
WP_000164218.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21008; AAL21008; STM2104.
GeneIDi1253625.
KEGGistm:STM2104.
PATRICi32382791. VBISalEnt20916_2226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59886 Genomic DNA. Translation: CAA42541.1.
AE006468 Genomic DNA. Translation: AAL21008.1.
PIRiS16291.
RefSeqiNP_461049.1. NC_003197.1.
WP_000164218.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LLLmodel-A1-456[»]
ProteinModelPortaliP26341.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21008; AAL21008; STM2104.
GeneIDi1253625.
KEGGistm:STM2104.
PATRICi32382791. VBISalEnt20916_2226.

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
KOiK01840.
OMAiNRQDTID.
OrthoDBiEOG6W9X55.
PhylomeDBiP26341.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
BioCyciSENT99287:GCTI-2116-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

« Hide 'large scale' publications
  1. "The cps gene cluster of Salmonella strain LT2 includes a second mannose pathway: sequence of two genes and relationship to genes in the rfb gene cluster."
    Stevenson G., Lee S.J., Romana L.K., Reeves P.R.
    Mol. Gen. Genet. 227:173-180(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LT2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
  3. "Structure of phosphomannomutase from Salmonella typhimurium."
    Sagajkar R., Muthuvel A., Reddy R.
    Submitted (APR-2003) to the PDB data bank
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiMANB_SALTY
AccessioniPrimary (citable) accession number: P26341
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2002
Last modified: July 22, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.