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P34948

- MPI_CANAL

UniProt

P34948 - MPI_CANAL

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Protein
Mannose-6-phosphate isomerase
Gene
PMI1, MANA, CaO19.1390
Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111Zinc
Metal bindingi113 – 1131Zinc
Metal bindingi138 – 1381Zinc
Sitei150 – 1501Its modification inactivates the enzyme
Metal bindingi285 – 2851Zinc
Active sitei304 – 30411 Publication

GO - Molecular functioni

  1. mannose-6-phosphate isomerase activity Source: CGD
  2. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  2. fungal-type cell wall biogenesis Source: CGD
  3. fungal-type cell wall organization Source: CGD
  4. protein glycosylation Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00126; UER00423.

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:PMI1
Synonyms:MANA
ORF Names:CaO19.1390
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0003967. PMI1.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed Inferred
Chaini2 – 441440Mannose-6-phosphate isomerase
PRO_0000194241Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi5476.CAL0003967.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118
Beta strandi19 – 213
Helixi22 – 243
Helixi26 – 349
Beta strandi44 – 463
Beta strandi48 – 525
Beta strandi59 – 613
Turni62 – 665
Helixi69 – 757
Helixi77 – 804
Helixi83 – 897
Beta strandi92 – 943
Beta strandi96 – 10611
Beta strandi110 – 1123
Helixi116 – 12510
Turni127 – 1293
Beta strandi138 – 1447
Beta strandi146 – 1527
Helixi155 – 16410
Helixi166 – 1727
Helixi174 – 18310
Helixi193 – 21018
Helixi214 – 23017
Helixi232 – 2365
Helixi242 – 25211
Helixi258 – 2614
Turni262 – 2654
Beta strandi266 – 2716
Beta strandi276 – 2794
Beta strandi285 – 29814
Beta strandi303 – 3075
Helixi314 – 3207
Helixi328 – 3314
Beta strandi341 – 3444
Beta strandi346 – 3516
Beta strandi354 – 3574
Beta strandi359 – 3646
Turni367 – 3693
Beta strandi372 – 3754
Beta strandi382 – 39514
Beta strandi398 – 4069
Beta strandi410 – 4134
Beta strandi419 – 4235
Beta strandi433 – 4386

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMIX-ray1.70A2-441[»]
ProteinModelPortaliP34948.
SMRiP34948. Positions 2-441.

Miscellaneous databases

EvolutionaryTraceiP34948.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
KOiK01809.
OrthoDBiEOG7WDNCR.

Family and domain databases

Gene3Di2.60.120.10. 3 hits.
InterProiIPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PANTHERiPTHR10309. PTHR10309. 1 hit.
PfamiPF01238. PMI_typeI. 1 hit.
[Graphical view]
PIRSFiPIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSiPR00714. MAN6PISMRASE.
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR00218. manA. 1 hit.
PROSITEiPS00965. PMI_I_1. 1 hit.
PS00966. PMI_I_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34948-1 [UniParc]FASTAAdd to Basket

« Hide

MSSEKLFRIQ CGYQNYDWGK IGSSSAVAQF VHNSDPSITI DETKPYAELW    50
MGTHPSVPSK AIDLNNQTLR DLVTAKPQEY LGESIITKFG SSKELPFLFK 100
VLSIEKVLSI QAHPDKKLGA QLHAADPKNY PDDNHKPEMA IAVTDFEGFC 150
GFKPLDQLAK TLATVPELNE IIGQELVDEF ISGIKLPAEV GSQDDVNNRK 200
LLQKVFGKLM NTDDDVIKQQ TAKLLERTDR EPQVFKDIDS RLPELIQRLN 250
KQFPNDIGLF CGCLLLNHVG LNKGEAMFLQ AKDPHAYISG DIIECMAASD 300
NVVRAGFTPK FKDVKNLVEM LTYSYESVEK QKMPLQEFPR SKGDAVKSVL 350
YDPPIAEFSV LQTIFDKSKG GKQVIEGLNG PSIVIATNGK GTIQITGDDS 400
TKQKIDTGYV FFVAPGSSIE LTADSANQDQ DFTTYRAFVE A 441
Length:441
Mass (Da):48,867
Last modified:January 23, 2007 - v2
Checksum:iAEDDE2AE9EDAD5EC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82024 Genomic DNA. Translation: CAA57548.1.
AACQ01000101 Genomic DNA. Translation: EAK95509.1.
PIRiS55354.
RefSeqiXP_714562.1. XM_709469.1.

Genome annotation databases

GeneIDi3643795.
KEGGical:CaO19.1390.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X82024 Genomic DNA. Translation: CAA57548.1 .
AACQ01000101 Genomic DNA. Translation: EAK95509.1 .
PIRi S55354.
RefSeqi XP_714562.1. XM_709469.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1PMI X-ray 1.70 A 2-441 [» ]
ProteinModelPortali P34948.
SMRi P34948. Positions 2-441.
ModBasei Search...

Protein-protein interaction databases

STRINGi 5476.CAL0003967.

Chemistry

BindingDBi P34948.
ChEMBLi CHEMBL3946.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3643795.
KEGGi cal:CaO19.1390.

Organism-specific databases

CGDi CAL0003967. PMI1.

Phylogenomic databases

eggNOGi COG1482.
KOi K01809.
OrthoDBi EOG7WDNCR.

Enzyme and pathway databases

UniPathwayi UPA00126 ; UER00423 .

Miscellaneous databases

EvolutionaryTracei P34948.

Family and domain databases

Gene3Di 2.60.120.10. 3 hits.
InterProi IPR001250. Man6P_Isoase-1.
IPR016305. Mannose-6-P_Isomerase.
IPR018050. Pmannose_isomerase-type1_CS.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
PANTHERi PTHR10309. PTHR10309. 1 hit.
Pfami PF01238. PMI_typeI. 1 hit.
[Graphical view ]
PIRSFi PIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTSi PR00714. MAN6PISMRASE.
SUPFAMi SSF51182. SSF51182. 1 hit.
TIGRFAMsi TIGR00218. manA. 1 hit.
PROSITEi PS00965. PMI_I_1. 1 hit.
PS00966. PMI_I_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and heterologous expression of the Candida albicans gene PMI 1 encoding phosphomannose isomerase."
    Smith D.J., Proudfoot A.E.I., de Tiani M., Wells T.N.C., Payton M.A.
    Yeast 11:301-310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 1006.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  3. "Identification of Cys-150 in the active site of phosphomannose isomerase from Candida albicans."
    Coulin F., Magnenat E., Proudfoot A.E.I., Payton M.A., Scully P., Wells T.N.C.
    Biochemistry 32:14139-14144(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHEMICAL LABELLING OF CYS-150, PARTIAL PROTEIN SEQUENCE.
  4. "Arginine 304 is an active site residue in phosphomannose isomerase from Candida albicans."
    Wells T.N.C., Scully P., Magnenat E.
    Biochemistry 33:5777-5782(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE ARG-304, PROTEIN SEQUENCE OF 300-312.
  5. "The X-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7-A resolution."
    Cleasby A., Wonacott A., Skarzynski T., Hubbard R.E., Davies G.J., Proudfoot A.E.I., Bernard A.R., Payton M.A., Wells T.N.C.
    Nat. Struct. Biol. 3:470-479(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Entry informationi

Entry nameiMPI_CANAL
AccessioniPrimary (citable) accession number: P34948
Secondary accession number(s): Q59YD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: December 11, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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