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Reviewed, UniProtKB/Swiss-Prot Q59935 (MANA_STRMU)

Last modified February 9, 2010. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Mannose-6-phosphate isomerase
    EC=5.3.1.8
Alternative name(s):
    Phosphomannose isomerase
      Short name=PMI
    Phosphohexomutase
Gene names
Name: pmi
Synonyms: manA
Ordered Locus Names: SMU_1839
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

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Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

D-mannose 6-phosphate = D-fructose 6-phosphate.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Sequence similarities

Belongs to the mannose-6-phosphate isomerase type 1 family.

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Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmannose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Mannose-6-phosphate isomerase
PRO_0000194229

Sites

Active site1911 By similarity
Metal binding951Zinc By similarity
Metal binding971Zinc By similarity
Metal binding1141Zinc By similarity
Metal binding1711Zinc By similarity

Experimental info

Sequence conflict2 – 32AE → EG in BAA04021. Ref.1
Sequence conflict1751K → R in BAA04021. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q59935-1 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 1DBF0411DA6CCF33

FASTA31635,374
        10         20         30         40         50         60 
MAEPLFLQSQ MHKKIWGGNR LRKEFGYDIP SETTGEYWAI SAHPNGVSVV KNGVYKGVPL 

        70         80         90        100        110        120 
DELYAEHREL FGNSKSSVFP LLTKILDAND WLSVQVHPDN AYALEHEGEL GKTECWYVIS 

       130        140        150        160        170        180 
ADEGAEIIYG HEAKSKEELR QMIAAGDWDH LLTKIPVKAG DFFYVPSGTM HAIGKGIMIL 

       190        200        210        220        230        240 
ETQQSSDTTY RVYDFDRKDD QGRKRALHIE QSIDVLTIGK PANATPAWLS LQGLETTVLV 

       250        260        270        280        290        300 
SSPFFTVYKW QISGSVKMQQ TAPYLLVSVL AGQGRITVGL EQYALRKGDH LILPNTIKSW 

       310 
QFDGDLEIIA SHSNEC

« Hide

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References

« Hide 'large scale' references
[1]"Isolation and sequence analysis of the pmi gene encoding phosphomannose isomerase of Streptococcus mutans."
Sato Y., Yamamoto Y., Kizaki H., Kuramitsu H.K.
FEMS Microbiol. Lett. 114:61-66(1993) [PubMed: 8293960] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: GS-5.
[2]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D16594 Genomic DNA. Translation: BAA04021.1.
AE014133 Genomic DNA. Translation: AAN59462.1.
RefSeqNP_722156.1.

3D structure databases

SMRQ59935. Positions 2-312.
ModBaseSearch...

Genome annotation databases

GeneID1029052.
GenomeReviewsGene locus SMU_1839 in contig AE014133_GR.
KEGGsmu:SMU.1839.
NMPDRfig|210007.1.peg.1669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG729572.
OMAPKIWGGR.

Enzyme and pathway databases

BioCycSMUT210007:SMU_1839-MONOMER.
BRENDA5.3.1.8. 20716.

Family and domain databases

InterProIPR011051. Cupin_RmlC_type.
IPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
Gene3DG3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
PfamPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFPIRSF036894. PMI_Firm_short. 1 hit.
TIGRFAMsTIGR00218. manA. 1 hit.
PROSITEPS00965. PMI_I_1. False negative.
PS00966. PMI_I_2. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameMANA_STRMU
AccessionPrimary (citable) accession number: Q59935
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: February 9, 2010
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents