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Protein

Mannose-6-phosphate isomerase

Gene

MAN1

Organism
Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathway: 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 (MAN1)
  2. Phosphomannomutase (CNH00170)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091ZincBy similarity
Metal bindingi111 – 1111ZincBy similarity
Metal bindingi136 – 1361ZincBy similarity
Metal bindingi291 – 2911ZincBy similarity
Active sitei310 – 3101By similarity

GO - Molecular functioni

GO - Biological processi

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:MAN1
Ordered Locus Names:CNI02370
OrganismiCryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans)
Taxonomic identifieri214684 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesTremellalesTremellaceaeFilobasidiellaFilobasidiella/Cryptococcus neoformans species complex
ProteomesiUP000002149 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiFungiDB:CNI02370.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Mannose-6-phosphate isomerasePRO_0000194243Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi214684.XP_572705.1.

Structurei

3D structure databases

ProteinModelPortaliQ9HFU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1482.
InParanoidiQ9HFU4.
KOiK01809.
OMAiNAECIIE.
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.

Q9HFU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPSVFKISP GINSYDWGKK GSASLAAQLA TTSIPDFSID EDKAYAELWM
60 70 80 90 100
GTHPNNPSRL SDNTLLSEHL KSHPELIGSS VSSKFEDCKD GSLPFLFKVL
110 120 130 140 150
SIGTALSIQA HPDKPLAKKL FDEKPDVYKD PNHKPEMAIA LTPFLAFLNF
160 170 180 190 200
LPLSVLLLHL LTVPELQEFV DSSLTESLAS SLGLPTSQPP DTSLFKPTES
210 220 230 240 250
PATAEQKDIL KQIFAALMSA DKKLVEEAIS KLIKRYQAKR DIKENEKSLV
260 270 280 290 300
DLALRLNDQY PGDVGVLCVF LLNVVELKRG EAAFLGANEP HAYIEGDIIE
310 320 330 340 350
CMATSDNVVR AGLTPKLRDV DTLVSMLTYE AAPGNKQLLQ PTPFQKGDDT
360 370 380 390 400
TKLYDPPIAE FSVLRTELSK GMKTSHRPVE GPSLCVITEG EGVVRNGNDR
410 420 430
SEFVRGDVIF VGAGKEVEWE AIKGLEMFRA YVEA
Length:434
Mass (Da):47,590
Last modified:June 21, 2005 - v2
Checksum:i4C2541EEFE9793FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381S → A in AAG10203 (PubMed:11359567).Curated
Sequence conflicti43 – 431K → R in AAG10203 (PubMed:11359567).Curated
Sequence conflicti71 – 711K → R in AAG10203 (PubMed:11359567).Curated
Sequence conflicti79 – 802SS → TT in AAG10203 (PubMed:11359567).Curated
Sequence conflicti154 – 1541S → P in AAG10203 (PubMed:11359567).Curated
Sequence conflicti183 – 1831G → D in AAG10203 (PubMed:11359567).Curated
Sequence conflicti192 – 1921T → S in AAG10203 (PubMed:11359567).Curated
Sequence conflicti224 – 2241L → H in AAG10203 (PubMed:11359567).Curated
Sequence conflicti237 – 2371Q → K in AAG10203 (PubMed:11359567).Curated
Sequence conflicti248 – 2481S → D in AAG10203 (PubMed:11359567).Curated
Sequence conflicti343 – 3431P → S in AAG10203 (PubMed:11359567).Curated
Sequence conflicti396 – 3961N → D in AAG10203 (PubMed:11359567).Curated
Sequence conflicti400 – 4012RS → QT in AAG10203 (PubMed:11359567).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291701 Genomic DNA. Translation: AAG10203.1.
AE017349 Genomic DNA. Translation: AAW45398.1.
RefSeqiXP_572705.1. XM_572705.1.

Genome annotation databases

EnsemblFungiiAAW45398; AAW45398; CNI02370.
GeneIDi3259465.
KEGGicne:CNI02370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291701 Genomic DNA. Translation: AAG10203.1.
AE017349 Genomic DNA. Translation: AAW45398.1.
RefSeqiXP_572705.1. XM_572705.1.

3D structure databases

ProteinModelPortaliQ9HFU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi214684.XP_572705.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiAAW45398; AAW45398; CNI02370.
GeneIDi3259465.
KEGGicne:CNI02370.

Organism-specific databases

EuPathDBiFungiDB:CNI02370.

Phylogenomic databases

eggNOGiCOG1482.
InParanoidiQ9HFU4.
KOiK01809.
OMAiNAECIIE.
OrthoDBiEOG7WDNCR.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00423.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of the Cryptococcus neoformans phosphomannose isomerase-encoding gene, MAN1, and its impact on pathogenicity."
    Wills E.A., Roberts I.S., Del Poeta M., Rivera J., Casadevall A., Cox G.M., Perfect J.R.
    Mol. Microbiol. 40:610-620(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome of the basidiomycetous yeast and human pathogen Cryptococcus neoformans."
    Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., Fox D.S.
    , Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.
    Science 307:1321-1324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JEC21 / ATCC MYA-565.

Entry informationi

Entry nameiMPI_CRYNJ
AccessioniPrimary (citable) accession number: Q9HFU4
Secondary accession number(s): Q5KBJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 21, 2005
Last modified: June 24, 2015
This is version 94 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.