Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q59935 (MANA_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mannose-6-phosphate isomerase

EC=5.3.1.8
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI
Gene names
Name:pmi
Synonyms:manA
Ordered Locus Names:SMU_1839
OrganismStreptococcus mutans serotype c (strain ATCC 700610 / UA159) [Complete proteome] [HAMAP]
Taxonomic identifier210007 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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

Sequences

Sequence LengthMass (Da)Tools
Q59935 [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

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16594 Genomic DNA. Translation: BAA04021.1.
AE014133 Genomic DNA. Translation: AAN59462.1.
RefSeqNP_722156.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ59935.
SMRQ59935. Positions 2-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING210007.SMU.1839.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN59462; AAN59462; SMU_1839.
GeneID1029052.
KEGGsmu:SMU_1839.
PATRIC19665675. VBIStrMut61772_1642.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1482.
KOK01809.
OMAPKAKEFP.
OrthoDBEOG66MQQS.
PhylomeDBQ59935.

Enzyme and pathway databases

BioCycSMUT210007:GC7Z-1741-MONOMER.

Family and domain databases

Gene3D2.60.120.10. 2 hits.
InterProIPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFPIRSF036894. PMI_Firm_short. 1 hit.
SUPFAMSSF51182. SSF51182. 1 hit.
TIGRFAMsTIGR00218. manA. 1 hit.
ProtoNetSearch...

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: July 9, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families