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Protein

Mannose-6-phosphate isomerase

Gene

pmi

Organism
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi95 – 951ZincBy similarity
Metal bindingi97 – 971ZincBy similarity
Metal bindingi114 – 1141ZincBy similarity
Metal bindingi171 – 1711ZincBy similarity
Active sitei191 – 1911By similarity

GO - Molecular functioni

  1. mannose-6-phosphate isomerase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1741-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannose-6-phosphate isomerase (EC:5.3.1.8)
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name:
PMI
Gene namesi
Name:pmi
Synonyms:manA
Ordered Locus Names:SMU_1839
OrganismiStreptococcus mutans serotype c (strain ATCC 700610 / UA159)
Taxonomic identifieri210007 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000002512 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Mannose-6-phosphate isomerasePRO_0000194229Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi210007.SMU.1839.

Structurei

3D structure databases

ProteinModelPortaliQ59935.
SMRiQ59935. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
KOiK01809.
OMAiPKAKEFP.
OrthoDBiEOG66MQQS.
PhylomeDBiQ59935.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFiPIRSF036894. PMI_Firm_short. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR00218. manA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPLFLQSQ MHKKIWGGNR LRKEFGYDIP SETTGEYWAI SAHPNGVSVV
60 70 80 90 100
KNGVYKGVPL DELYAEHREL FGNSKSSVFP LLTKILDAND WLSVQVHPDN
110 120 130 140 150
AYALEHEGEL GKTECWYVIS ADEGAEIIYG HEAKSKEELR QMIAAGDWDH
160 170 180 190 200
LLTKIPVKAG DFFYVPSGTM HAIGKGIMIL ETQQSSDTTY RVYDFDRKDD
210 220 230 240 250
QGRKRALHIE QSIDVLTIGK PANATPAWLS LQGLETTVLV SSPFFTVYKW
260 270 280 290 300
QISGSVKMQQ TAPYLLVSVL AGQGRITVGL EQYALRKGDH LILPNTIKSW
310
QFDGDLEIIA SHSNEC
Length:316
Mass (Da):35,374
Last modified:November 28, 2002 - v2
Checksum:i1DBF0411DA6CCF33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AE → EG in BAA04021 (PubMed:8293960).Curated
Sequence conflicti175 – 1751K → R in BAA04021 (PubMed:8293960).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16594 Genomic DNA. Translation: BAA04021.1.
AE014133 Genomic DNA. Translation: AAN59462.1.
RefSeqiNP_722156.1. NC_004350.2.

Genome annotation databases

EnsemblBacteriaiAAN59462; AAN59462; SMU_1839.
GeneIDi1029052.
KEGGismu:SMU_1839.
PATRICi19665675. VBIStrMut61772_1642.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16594 Genomic DNA. Translation: BAA04021.1.
AE014133 Genomic DNA. Translation: AAN59462.1.
RefSeqiNP_722156.1. NC_004350.2.

3D structure databases

ProteinModelPortaliQ59935.
SMRiQ59935. Positions 2-312.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi210007.SMU.1839.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN59462; AAN59462; SMU_1839.
GeneIDi1029052.
KEGGismu:SMU_1839.
PATRICi19665675. VBIStrMut61772_1642.

Phylogenomic databases

eggNOGiCOG1482.
KOiK01809.
OMAiPKAKEFP.
OrthoDBiEOG66MQQS.
PhylomeDBiQ59935.

Enzyme and pathway databases

BioCyciSMUT210007:GC7Z-1741-MONOMER.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR001250. Man6P_Isoase-1.
IPR014628. Man6P_isomerase_Firm_short.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFiPIRSF036894. PMI_Firm_short. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR00218. manA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700610 / UA159.

Entry informationi

Entry nameiMANA_STRMU
AccessioniPrimary (citable) accession number: Q59935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: January 7, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.