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Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 4 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 O9 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 sitei98 – 981Phosphoserine intermediateBy similarity
Metal bindingi98 – 981Magnesium; via phosphate groupBy similarity
Metal bindingi246 – 2461MagnesiumBy similarity
Metal bindingi248 – 2481MagnesiumBy similarity
Metal bindingi250 – 2501MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

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, rfbK2
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456PhosphomannomutasePRO_0000147824Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP37755.

Structurei

3D structure databases

ProteinModelPortaliP37755.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

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.

P37755-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQLTCFKAY DIRGELGEEL NEDIAYRIGR AYGEFLKPGK IVVGGDVRLT
60 70 80 90 100
SESLKLALAR GLMDAGTDVL DIGLSGTEEI YFATFHLGVD GGIEVTASHN
110 120 130 140 150
PMNYNGMKLV RENAKPISGD TGLRDIQRLA EENQFPPVDP ARRGTLRQIS
160 170 180 190 200
VLKEYVDHLM GYVDLANFTR PLKLVVNSGN GAAGHVIDEV EKRFAAAGVP
210 220 230 240 250
VTFIKVHHQP DGHFPNGIPN PLLPECRQDT ADAVREHQAD MGIAFDGDFD
260 270 280 290 300
RCFLFDDEAS FIEGYYIVGL LAEAFLQKQP GAKIIHDPRL TWNTVDIVTR
310 320 330 340 350
NGGQPVMSKT GHAFIKERMR QEDAIYGGEM SAHHYFRDFA YCDSGMIPWL
360 370 380 390 400
LVAELLCLKN SSLKSLVADR QAAFPASGEI NRKLGNAAEA IARIRAQYEP
410 420 430 440 450
AAAHIDTTDG ISIEYPEWRF NLRTSNTEPV VRLNVESRAD TALMNAKTEE

ILALLK
Length:456
Mass (Da):50,423
Last modified:October 1, 1994 - v1
Checksum:i40100B6075791BF3
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti392 – 3921A → R.
Natural varianti441 – 4411T → V.
Natural varianti446 – 4461A → E.
Natural varianti449 – 4535EEILA → TELLN.
Natural varianti456 – 4561K → KEELL.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27646 Genomic DNA. Translation: AAA21138.1.
L27632 Genomic DNA. Translation: AAA21140.1.
RefSeqiWP_032248255.1. NZ_JSRJ01000109.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27646 Genomic DNA. Translation: AAA21138.1.
L27632 Genomic DNA. Translation: AAA21140.1.
RefSeqiWP_032248255.1. NZ_JSRJ01000109.1.

3D structure databases

ProteinModelPortaliP37755.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP37755.

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. 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. "Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide."
    Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C.
    J. Bacteriol. 176:3126-3139(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O9:K30:H12 / E69.
  2. Cited for: GENE NAME.

Entry informationi

Entry nameiRFBK9_ECOLX
AccessioniPrimary (citable) accession number: P37755
Secondary accession number(s): P82275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 4, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two duplicated genes for manB and manC in this E.coli strain.

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.