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Q01411

- MANB_SALMO

UniProt

Q01411 - MANB_SALMO

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Protein

Phosphomannomutase

Gene

manB

Organism
Salmonella montevideo
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 intermediateBy similarity
Metal bindingi98 – 981Magnesium; 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:rfbL
OrganismiSalmonella montevideo
Taxonomic identifieri115981 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456PhosphomannomutasePRO_0000147821Add
BLAST

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ01411.
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.

Q01411-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNLTCFKAY DIRGRLGEEL NEDIAWRIGR AYGEYLKPKT IVLGGDVRLT
60 70 80 90 100
SEALKLALAK GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN
110 120 130 140 150
PMDYNGMKLV REGARPISGD TGLRDVQRLA EAGDFPPVND AARGSYRQIS
160 170 180 190 200
LRDAYIDHLL AYISVNNLTP LKLVVNSGNG 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
VAELVCLKGQ SLGELVRDRM AAFPASGEIN SRLAEPAAAI ARVEAHFAEE
410 420 430 440 450
AQAVDRTDGL SMSFADWRFN LRSSNTEPVV RLNVESRGDI PLMEARTKEI

LQLLNS
Length:456
Mass (Da):49,900
Last modified:April 1, 1993 - v1
Checksum:iF2443A7B6CA83460
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84642 Genomic DNA. Translation: AAB49391.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84642 Genomic DNA. Translation: AAB49391.1 .

3D structure databases

ProteinModelPortali Q01411.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00126 ; UER00424 .
UPA00281 .

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

  1. "Sequence and structural analysis of the rfb (O antigen) gene cluster from a group C1 Salmonella enterica strain."
    Lee S.J., Romana L.K., Reeves P.R.
    J. Gen. Microbiol. 138:1843-1855(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M40.

Entry informationi

Entry nameiMANB_SALMO
AccessioniPrimary (citable) accession number: Q01411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 1, 2014
This is version 83 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