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Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli
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 O7 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 sitei96 – 961Phosphoserine intermediateBy similarity
Metal bindingi96 – 961Magnesium; via phosphate groupBy similarity
Metal bindingi243 – 2431MagnesiumBy similarity
Metal bindingi245 – 2451MagnesiumBy similarity
Metal bindingi247 – 2471MagnesiumBy 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
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453PhosphomannomutasePRO_0000147823Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP37742.

Structurei

3D structure databases

ProteinModelPortaliP37742.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.

Family and domain databases

Gene3Di3.40.120.10. 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.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTCFKAYDI RGKLGEELNE DIAWRIGRAY GEFLKPKTIV LGGDVRLTSE
60 70 80 90 100
TLKLALAKGL QDAGVDVLDI GMSGTEEIYF ATFHLGVDGG IEVTASHNPM
110 120 130 140 150
DYNGMKLVRE GARPISGDTG LRDVQRLAEA NDFPPVDETK RGRYQQINLR
160 170 180 190 200
DAYVDHLFGY INVKNLTPLK LVINSGNGAA GPVVDAIEAR FKALGAPVEL
210 220 230 240 250
IKVHNTPDGN FPNGIPNPLL PECRDDTRNA VIKHGADMGI AFDGDFDRCF
260 270 280 290 300
LFDEKGQFIE GYYIVGLLAE AFLEKNPGAK IIHDPRLSWN TVDVVTAAGT
310 320 330 340 350
PVMSKTGHAF IKERMRKEDA IYGGEMSAHH YFRDFAYCDT GMIPWLLVAE
360 370 380 390 400
LVCLKGKTLG ELVRDRMAAF PASGEINSKL AHPVEAINRV EQHFSRDAGG
410 420 430 440 450
GSHRWHQHDL CRLAALTCAS SNTEPVVRLN VESRGDVPLM EEKTKLILEL

LNK
Length:453
Mass (Da):49,932
Last modified:October 1, 1994 - v1
Checksum:iF1D1F69F97804391
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125322 Genomic DNA. Translation: AAC27539.1. Sequence problems.
PIRiD40630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125322 Genomic DNA. Translation: AAC27539.1. Sequence problems.
PIRiD40630.

3D structure databases

ProteinModelPortaliP37742.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP37742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG1109.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
UPA00281.

Family and domain databases

Gene3Di3.40.120.10. 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.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification, expression, and DNA sequence of the GDP-mannose biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187 (Escherichia coli O7:K1)."
    Marolda C.L., Valvano M.A.
    J. Bacteriol. 175:148-158(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O7:K1 / VW187.

Entry informationi

Entry nameiRFBK7_ECOLX
AccessioniPrimary (citable) accession number: P37742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 26, 2014
This is version 76 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.