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Protein

Mannose-6-phosphate isomerase

Gene

PMI1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: 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: GDP-alpha-D-mannose biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Mannose-6-phosphate isomerase (PMI1), Mannose-6-phosphate isomerase (PMI1)
  2. Phosphomannomutase (PMM1)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi111Zinc1
Metal bindingi113Zinc1
Metal bindingi138Zinc1
Sitei150Its modification inactivates the enzyme1
Metal bindingi285Zinc1
Active sitei3041 Publication1

GO - Molecular functioni

  • mannose-6-phosphate isomerase activity Source: CGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • fungal-type cell wall organization Source: CGD
  • 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
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000189115. PMI1.
EuPathDBiFungiDB:C2_09640W_A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCurated
ChainiPRO_00001942412 – 441Mannose-6-phosphate isomeraseAdd BLAST440

Proteomic databases

PRIDEiP34948.

Interactioni

Subunit structurei

Monomer.

Chemistry databases

BindingDBiP34948.

Structurei

Secondary structure

1441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi19 – 21Combined sources3
Helixi22 – 24Combined sources3
Helixi26 – 34Combined sources9
Beta strandi44 – 46Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi59 – 61Combined sources3
Turni62 – 66Combined sources5
Helixi69 – 75Combined sources7
Helixi77 – 80Combined sources4
Helixi83 – 89Combined sources7
Beta strandi92 – 94Combined sources3
Beta strandi96 – 106Combined sources11
Beta strandi110 – 112Combined sources3
Helixi116 – 125Combined sources10
Turni127 – 129Combined sources3
Beta strandi138 – 144Combined sources7
Beta strandi146 – 152Combined sources7
Helixi155 – 164Combined sources10
Helixi166 – 172Combined sources7
Helixi174 – 183Combined sources10
Helixi193 – 210Combined sources18
Helixi214 – 230Combined sources17
Helixi232 – 236Combined sources5
Helixi242 – 252Combined sources11
Helixi258 – 261Combined sources4
Turni262 – 265Combined sources4
Beta strandi266 – 271Combined sources6
Beta strandi276 – 279Combined sources4
Beta strandi285 – 298Combined sources14
Beta strandi303 – 307Combined sources5
Helixi314 – 320Combined sources7
Helixi328 – 331Combined sources4
Beta strandi341 – 344Combined sources4
Beta strandi346 – 351Combined sources6
Beta strandi354 – 357Combined sources4
Beta strandi359 – 364Combined sources6
Turni367 – 369Combined sources3
Beta strandi372 – 375Combined sources4
Beta strandi382 – 395Combined sources14
Beta strandi398 – 406Combined sources9
Beta strandi410 – 413Combined sources4
Beta strandi419 – 423Combined sources5
Beta strandi433 – 438Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP34948.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

InParanoidiP34948.
KOiK01809.
OrthoDBiEOG092C3NWF.

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

EnsemblFungiiEAK95509; EAK95509; CaO19.1390.
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.
PIRiS55354.
RefSeqiXP_714562.1. XM_709469.1.

3D structure databases

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

Chemistry databases

BindingDBiP34948.
ChEMBLiCHEMBL3946.

Proteomic databases

PRIDEiP34948.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAK95509; EAK95509; CaO19.1390.
GeneIDi3643795.
KEGGical:CaO19.1390.

Organism-specific databases

CGDiCAL0000189115. PMI1.
EuPathDBiFungiDB:C2_09640W_A.

Phylogenomic databases

InParanoidiP34948.
KOiK01809.
OrthoDBiEOG092C3NWF.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00423.

Miscellaneous databases

EvolutionaryTraceiP34948.

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]
ProtoNetiSearch...

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 30, 2016
This is version 128 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

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 one 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.