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Protein

Putative mannose-6-phosphate isomerase YvyI

Gene

yvyI

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi98 – 981Zinc1 Publication
Metal bindingi116 – 1161Zinc1 Publication
Metal bindingi173 – 1731Zinc1 Publication
Active sitei193 – 1931By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU35790-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative mannose-6-phosphate isomerase YvyI (EC:5.3.1.8)
Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name:
PMI
Gene namesi
Name:yvyI
Synonyms:pmi
Ordered Locus Names:BSU35790
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU35790.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Putative mannose-6-phosphate isomerase YvyIPRO_0000194228Add
BLAST

Proteomic databases

PaxDbiP39841.

Interactioni

Protein-protein interaction databases

IntActiP39841. 1 interaction.
STRINGi224308.Bsubs1_010100019361.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Beta strandi11 – 144Combined sources
Helixi21 – 266Combined sources
Beta strandi31 – 4111Combined sources
Turni55 – 584Combined sources
Helixi61 – 677Combined sources
Helixi69 – 724Combined sources
Beta strandi82 – 9110Combined sources
Beta strandi95 – 973Combined sources
Helixi101 – 1077Combined sources
Turni108 – 1103Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi128 – 1336Combined sources
Helixi138 – 1469Combined sources
Helixi150 – 1534Combined sources
Beta strandi154 – 1585Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 18711Combined sources
Beta strandi192 – 1954Combined sources
Helixi211 – 2177Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi237 – 2448Combined sources
Beta strandi249 – 26113Combined sources
Beta strandi268 – 28114Combined sources
Beta strandi284 – 2896Combined sources
Beta strandi293 – 2964Combined sources
Beta strandi303 – 31513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWRX-ray1.80A/B1-316[»]
ProteinModelPortaliP39841.
SMRiP39841. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39841.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000054245.
InParanoidiP39841.
KOiK01809.
OMAiEYFSVYK.
OrthoDBiEOG66MQQS.
PhylomeDBiP39841.

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. 2 hits.

Sequencei

Sequence statusi: Complete.

P39841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQSPIFLTP VFKEKIWGGT ALRDRFGYSI PSESTGECWA ISAHPKGPST
60 70 80 90 100
VANGPYKGKT LIELWEEHRE VFGGVEGDRF PLLTKLLDVK EDTSIKVHPD
110 120 130 140 150
DYYAGENEEG ELGKTECWYI IDCKENAEII YGHTARSKTE LVTMINSGDW
160 170 180 190 200
EGLLRRIKIK PGDFYYVPSG TLHALCKGAL VLETQQNSDA TYRVYDYDRL
210 220 230 240 250
DSNGSPRELH FAKAVNAATV PHVDGYIDES TESRKGITIK TFVQGEYFSV
260 270 280 290 300
YKWDINGEAE MAQDESFLIC SVIEGSGLLK YEDKTCPLKK GDHFILPAQM
310
PDFTIKGTCT LIVSHI
Length:316
Mass (Da):35,428
Last modified:February 1, 1995 - v1
Checksum:i21E6FF26E7CF922F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02562 Genomic DNA. Translation: AAA67856.1.
D45048 Genomic DNA. Translation: BAA08088.1.
AL009126 Genomic DNA. Translation: CAB15596.1.
PIRiA69680.
RefSeqiNP_391460.1. NC_000964.3.
WP_003244253.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15596; CAB15596; BSU35790.
GeneIDi936815.
KEGGibsu:BSU35790.
PATRICi18979174. VBIBacSub10457_3749.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02562 Genomic DNA. Translation: AAA67856.1.
D45048 Genomic DNA. Translation: BAA08088.1.
AL009126 Genomic DNA. Translation: CAB15596.1.
PIRiA69680.
RefSeqiNP_391460.1. NC_000964.3.
WP_003244253.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWRX-ray1.80A/B1-316[»]
ProteinModelPortaliP39841.
SMRiP39841. Positions 2-316.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP39841. 1 interaction.
STRINGi224308.Bsubs1_010100019361.

Proteomic databases

PaxDbiP39841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15596; CAB15596; BSU35790.
GeneIDi936815.
KEGGibsu:BSU35790.
PATRICi18979174. VBIBacSub10457_3749.

Organism-specific databases

GenoListiBSU35790.

Phylogenomic databases

eggNOGiCOG1482.
HOGENOMiHOG000054245.
InParanoidiP39841.
KOiK01809.
OMAiEYFSVYK.
OrthoDBiEOG66MQQS.
PhylomeDBiP39841.

Enzyme and pathway databases

BioCyciBSUB:BSU35790-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39841.

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. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiMANA3_BACSU
AccessioniPrimary (citable) accession number: P39841
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.