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P34948

- MPI_CANAL

UniProt

P34948 - MPI_CANAL

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Protein

Mannose-6-phosphate isomerase

Gene

PMI1

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

Zn2+Note: 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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. fungal-type cell wall organization Source: CGD
  3. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
ProteomesiUP000000559: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0003967. PMI1.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedCurated
Chaini2 – 441440Mannose-6-phosphate isomerasePRO_0000194241Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi5476.CAL0003967.

Structurei

Secondary structure

1
441
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 118Combined sources
Beta strandi19 – 213Combined sources
Helixi22 – 243Combined sources
Helixi26 – 349Combined sources
Beta strandi44 – 463Combined sources
Beta strandi48 – 525Combined sources
Beta strandi59 – 613Combined sources
Turni62 – 665Combined sources
Helixi69 – 757Combined sources
Helixi77 – 804Combined sources
Helixi83 – 897Combined sources
Beta strandi92 – 943Combined sources
Beta strandi96 – 10611Combined sources
Beta strandi110 – 1123Combined sources
Helixi116 – 12510Combined sources
Turni127 – 1293Combined sources
Beta strandi138 – 1447Combined sources
Beta strandi146 – 1527Combined sources
Helixi155 – 16410Combined sources
Helixi166 – 1727Combined sources
Helixi174 – 18310Combined sources
Helixi193 – 21018Combined sources
Helixi214 – 23017Combined sources
Helixi232 – 2365Combined sources
Helixi242 – 25211Combined sources
Helixi258 – 2614Combined sources
Turni262 – 2654Combined sources
Beta strandi266 – 2716Combined sources
Beta strandi276 – 2794Combined sources
Beta strandi285 – 29814Combined sources
Beta strandi303 – 3075Combined sources
Helixi314 – 3207Combined sources
Helixi328 – 3314Combined sources
Beta strandi341 – 3444Combined sources
Beta strandi346 – 3516Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi359 – 3646Combined sources
Turni367 – 3693Combined sources
Beta strandi372 – 3754Combined sources
Beta strandi382 – 39514Combined sources
Beta strandi398 – 4069Combined sources
Beta strandi410 – 4134Combined sources
Beta strandi419 – 4235Combined sources
Beta strandi433 – 4386Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PMIX-ray1.70A2-441[»]
ProteinModelPortaliP34948.
SMRiP34948. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34948.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
InParanoidiP34948.
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

        10         20         30         40         50
MSSEKLFRIQ CGYQNYDWGK IGSSSAVAQF VHNSDPSITI DETKPYAELW
60 70 80 90 100
MGTHPSVPSK AIDLNNQTLR DLVTAKPQEY LGESIITKFG SSKELPFLFK
110 120 130 140 150
VLSIEKVLSI QAHPDKKLGA QLHAADPKNY PDDNHKPEMA IAVTDFEGFC
160 170 180 190 200
GFKPLDQLAK TLATVPELNE IIGQELVDEF ISGIKLPAEV GSQDDVNNRK
210 220 230 240 250
LLQKVFGKLM NTDDDVIKQQ TAKLLERTDR EPQVFKDIDS RLPELIQRLN
260 270 280 290 300
KQFPNDIGLF CGCLLLNHVG LNKGEAMFLQ AKDPHAYISG DIIECMAASD
310 320 330 340 350
NVVRAGFTPK FKDVKNLVEM LTYSYESVEK QKMPLQEFPR SKGDAVKSVL
360 370 380 390 400
YDPPIAEFSV LQTIFDKSKG GKQVIEGLNG PSIVIATNGK GTIQITGDDS
410 420 430 440
TKQKIDTGYV FFVAPGSSIE LTADSANQDQ DFTTYRAFVE A
Length:441
Mass (Da):48,867
Last modified:January 23, 2007 - v2
Checksum:iAEDDE2AE9EDAD5EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi 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.
InParanoidi P34948.
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: November 26, 2014
This is version 115 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