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P39841 (MANA3_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Putative mannose-6-phosphate isomerase YvyI

EC=5.3.1.8
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI
Gene names
Name:yvyI
Synonyms:pmi
Ordered Locus Names:BSU35790
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Sequence similarities

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

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 316316Putative mannose-6-phosphate isomerase YvyI
PRO_0000194228

Sites

Active site1931 By similarity
Metal binding981Zinc
Metal binding1161Zinc
Metal binding1731Zinc

Secondary structure

....................................................... 316
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39841 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 21E6FF26E7CF922F

FASTA31635,428
        10         20         30         40         50         60 
MTQSPIFLTP VFKEKIWGGT ALRDRFGYSI PSESTGECWA ISAHPKGPST VANGPYKGKT 

        70         80         90        100        110        120 
LIELWEEHRE VFGGVEGDRF PLLTKLLDVK EDTSIKVHPD DYYAGENEEG ELGKTECWYI 

       130        140        150        160        170        180 
IDCKENAEII YGHTARSKTE LVTMINSGDW EGLLRRIKIK PGDFYYVPSG TLHALCKGAL 

       190        200        210        220        230        240 
VLETQQNSDA TYRVYDYDRL DSNGSPRELH FAKAVNAATV PHVDGYIDES TESRKGITIK 

       250        260        270        280        290        300 
TFVQGEYFSV YKWDINGEAE MAQDESFLIC SVIEGSGLLK YEDKTCPLKK GDHFILPAQM 

       310 
PDFTIKGTCT LIVSHI 

« Hide

References

« Hide 'large scale' references
[1]"The gene of the N-acetylglucosaminidase, a Bacillus subtilis 168 cell wall hydrolase not involved in vegetative cell autolysis."
Margot P., Maueel C., Karamata D.
Mol. Microbiol. 12:535-545(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Glucosaminidase of Bacillus subtilis: cloning, regulation, primary structure and biochemical characterization."
Rashid M.H., Mori M., Sekiguchi J.
Microbiology 141:2391-2404(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / AC327.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Crystal structure analysis of the mannose 6-phosphate isomerase from Bacillus subtilis."
Midwest center for structural genomics (MCSG)
Submitted (JAN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U02562 Genomic DNA. Translation: AAA67856.1.
D45048 Genomic DNA. Translation: BAA08088.1.
AL009126 Genomic DNA. Translation: CAB15596.1.
PIRA69680.
RefSeqNP_391460.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWRX-ray1.80A/B1-316[»]
ProteinModelPortalP39841.
SMRP39841. Positions 2-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP39841. 1 interaction.
STRING224308.BSU35790.

Proteomic databases

PaxDbP39841.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15596; CAB15596; BSU35790.
GeneID936815.
KEGGbsu:BSU35790.
PATRIC18979174. VBIBacSub10457_3749.

Organism-specific databases

GenoListBSU35790.

Phylogenomic databases

eggNOGCOG1482.
HOGENOMHOG000054245.
KOK01809.
OMAIDCKENA.
OrthoDBEOG66MQQS.
PhylomeDBP39841.

Enzyme and pathway databases

BioCycBSUB:BSU35790-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. 2 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP39841.

Entry information

Entry nameMANA3_BACSU
AccessionPrimary (citable) accession number: P39841
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 108 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList