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Protein

Phosphomannomutase

Gene

manB

Organism
Salmonella muenchen
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS group C2 O antigen.

Catalytic activityi

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

Cofactori

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111Phosphoserine intermediateBy similarity
Metal bindingi111 – 1111Magnesium; via phosphate groupBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi247 – 2471MagnesiumBy similarity
Metal bindingi249 – 2491MagnesiumBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  2. O antigen biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
Name:manB
Synonyms:rfbK
OrganismiSalmonella muenchen
Taxonomic identifieri596 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei30 – 4617HelicalSequence AnalysisAdd
BLAST
Transmembranei265 – 28420HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478PhosphomannomutasePRO_0000147825Add
BLAST

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ00330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q00330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNIYNTYDV INKSGINFGT SGARGLVTDF TPEVCARFTI SFLTVMQQRF
60 70 80 90 100
SFTTVALAID NRPSSYAMAQ ACAAALQEKG IKTVYYGVIP TPALAHQSIS
110 120 130 140 150
DKVPAIMVTG SHIPFDRNGL KFYRPDGEIT KDDENAIIHV DASFMQPKLE
160 170 180 190 200
QLTISTIAAR NYILRYTSLF PMPFLKNKRI GIYEHSSAGR DLYKTLFKML
210 220 230 240 250
GATVVSLARS DEFVPIDTEA VSEDDRNKAI TWAKKYQLDA IFSTDGDGDR
260 270 280 290 300
PLIADEYGNW LRGDILGLLC SLELAADAVA IPVSCNSTIS SGNFFKHVER
310 320 330 340 350
TKIGSPYVIA AFAKLSANYN CIAGFEANGG FLLGSDVYIN QRLLKALPTR
360 370 380 390 400
DALLPAIMLL FGSKDKSISE LVKKLPARYT YSNRLQDISV KTSMSLINLG
410 420 430 440 450
LTDQEDFLQY IGFNKHHILH SDVTDGFRIT IDNNNIIHLR PSGNAPELRC
460 470
YAEADSQEDA CNIVETVLSN IKSKLGRA
Length:478
Mass (Da):52,813
Last modified:October 1, 1994 - v1
Checksum:i982E5B885083B893
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61917 Genomic DNA. Translation: CAA43916.1.
PIRiS22622.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61917 Genomic DNA. Translation: CAA43916.1.
PIRiS22622.

3D structure databases

ProteinModelPortaliQ00330.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
UPA00281.

Family and domain databases

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

Publicationsi

  1. "Molecular analysis of the rfb gene cluster of Salmonella serovar muenchen (strain M67): the genetic basis of the polymorphism between groups C2 and B."
    Brown P.K., Romana L.K., Reeves P.R.
    Mol. Microbiol. 6:1385-1394(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M67.

Entry informationi

Entry nameiRFBK_SALMU
AccessioniPrimary (citable) accession number: Q00330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.