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O85343

- MANB_ECO57

UniProt

O85343 - MANB_ECO57

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Protein

Phosphomannomutase

Gene
manB, Z3194, ECs2835
Organism
Escherichia coli O157:H7
Status
Reviewed - 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 O antigen.

Catalytic activityi

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

Cofactori

Binds 1 magnesium ion per subunit By similarity.

Pathwayi

Sites

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

BioCyciECOL386585:GJFA-2797-MONOMER.
ECOO157:MANB-MONOMER.
UniPathwayiUPA00126; UER00424.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
Name:manB
Ordered Locus Names:Z3194, ECs2835
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456PhosphomannomutasePRO_0000147819Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi155864.Z3194.

Structurei

3D structure databases

ProteinModelPortaliO85343.
SMRiO85343. Positions 1-456.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1109.
HOGENOMiHOG000268679.
KOiK01840.
OMAiRLAIICE.
OrthoDBiEOG6W9X55.

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.

O85343-1 [UniParc]FASTAAdd to Basket

« Hide

MKSLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT    50
SEALKLALAK GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN 100
PMDYNGMKLV REGARPISGD TGLRDVQRLA EANDFPPVDE TKRGRYQQIN 150
LRDAYVDHLF GYINVKNLTP LKLVINSGNG AAGPVVDAIE ARFKALGAPV 200
ELIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIKHGADM GIAFDGDFDR 250
CFLFDEKGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA 300
GGTPVMSKTG HAFIKERMRK EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL 350
VAELVCLKGK TLGEMVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE 400
ALAVDRTDGI SMTFADWRFN LRSSNTEPVV RLNVESRGDV KLMEKKTKAL 450
LKLLSE 456
Length:456
Mass (Da):50,340
Last modified:November 1, 1998 - v1
Checksum:i6845D9D2DD7628B7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF061251 Genomic DNA. Translation: AAC32349.1.
AB008676 Genomic DNA. Translation: BAA77734.1.
AE005174 Genomic DNA. Translation: AAG57090.1.
BA000007 Genomic DNA. Translation: BAB36258.1.
PIRiC90983.
F85828.
RefSeqiNP_288536.1. NC_002655.2.
NP_310862.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG57090; AAG57090; Z3194.
BAB36258; BAB36258; BAB36258.
GeneIDi913941.
962089.
KEGGiece:Z3194.
ecs:ECs2835.
PATRICi18355054. VBIEscCol44059_2728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF061251 Genomic DNA. Translation: AAC32349.1 .
AB008676 Genomic DNA. Translation: BAA77734.1 .
AE005174 Genomic DNA. Translation: AAG57090.1 .
BA000007 Genomic DNA. Translation: BAB36258.1 .
PIRi C90983.
F85828.
RefSeqi NP_288536.1. NC_002655.2.
NP_310862.1. NC_002695.1.

3D structure databases

ProteinModelPortali O85343.
SMRi O85343. Positions 1-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z3194.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG57090 ; AAG57090 ; Z3194 .
BAB36258 ; BAB36258 ; BAB36258 .
GeneIDi 913941.
962089.
KEGGi ece:Z3194.
ecs:ECs2835.
PATRICi 18355054. VBIEscCol44059_2728.

Phylogenomic databases

eggNOGi COG1109.
HOGENOMi HOG000268679.
KOi K01840.
OMAi RLAIICE.
OrthoDBi EOG6W9X55.

Enzyme and pathway databases

UniPathwayi UPA00126 ; UER00424 .
UPA00281 .
BioCyci ECOL386585:GJFA-2797-MONOMER.
ECOO157:MANB-MONOMER.

Family and domain databases

Gene3Di 3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProi IPR005844. 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 ]
Pfami PF02878. 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 ]
PRINTSi PR00509. PGMPMM.
SUPFAMi SSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEi PS00710. PGM_PMM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Organization of Escherichia coli O157 O antigen gene cluster and identification of its specific genes."
    Wang L., Reeves P.R.
    Infect. Immun. 66:3545-3551(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O157:H7 / C664-1992 / EHEC.
  2. "Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157."
    Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y.
    Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: O157:H- / 184 / EHEC.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  4. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiMANB_ECO57
AccessioniPrimary (citable) accession number: O85343
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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