Mannose-6-phosphate isomerase - Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565)

Contribute

Send feedback

Read comments (?) or add your own

Q9HFU4 (MPI_CRYNJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mannose-6-phosphate isomerase
EC=5.3.1.8

Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI

Gene names

Name:	MAN1
Ordered Locus Names:	CNI02370

Organism

Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) (Filobasidiella neoformans) [Reference proteome]

Taxonomic identifier

214684 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Tremellomycetes › Tremellales › Tremellaceae › Filobasidiella › Filobasidiella/Cryptococcus neoformans species complex ›

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions By similarity.
Catalytic activity	D-mannose 6-phosphate = D-fructose 6-phosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the mannose-6-phosphate isomerase type 1 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 434

434

Mannose-6-phosphate isomerase

PRO_0000194243

Sites

Active site

310

By similarity

Metal binding

109

Zinc By similarity

Metal binding

111

Zinc By similarity

Metal binding

136

Zinc By similarity

Metal binding

291

Zinc By similarity

Experimental info

Sequence conflict

S → A in AAG10203. Ref.1

Sequence conflict

K → R in AAG10203. Ref.1

Sequence conflict

K → R in AAG10203. Ref.1

Sequence conflict

79 – 80

SS → TT in AAG10203. Ref.1

Sequence conflict

154

S → P in AAG10203. Ref.1

Sequence conflict

183

G → D in AAG10203. Ref.1

Sequence conflict

192

T → S in AAG10203. Ref.1

Sequence conflict

224

L → H in AAG10203. Ref.1

Sequence conflict

237

Q → K in AAG10203. Ref.1

Sequence conflict

248

S → D in AAG10203. Ref.1

Sequence conflict

343

P → S in AAG10203. Ref.1

Sequence conflict

396

N → D in AAG10203. Ref.1

Sequence conflict

400 – 401

RS → QT in AAG10203. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9HFU4 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 4C2541EEFE9793FF
Show »

FASTA

434

47,590

        10         20         30         40         50         60 
MSPSVFKISP GINSYDWGKK GSASLAAQLA TTSIPDFSID EDKAYAELWM GTHPNNPSRL 

        70         80         90        100        110        120 
SDNTLLSEHL KSHPELIGSS VSSKFEDCKD GSLPFLFKVL SIGTALSIQA HPDKPLAKKL 

       130        140        150        160        170        180 
FDEKPDVYKD PNHKPEMAIA LTPFLAFLNF LPLSVLLLHL LTVPELQEFV DSSLTESLAS 

       190        200        210        220        230        240 
SLGLPTSQPP DTSLFKPTES PATAEQKDIL KQIFAALMSA DKKLVEEAIS KLIKRYQAKR 

       250        260        270        280        290        300 
DIKENEKSLV DLALRLNDQY PGDVGVLCVF LLNVVELKRG EAAFLGANEP HAYIEGDIIE 

       310        320        330        340        350        360 
CMATSDNVVR AGLTPKLRDV DTLVSMLTYE AAPGNKQLLQ PTPFQKGDDT TKLYDPPIAE 

       370        380        390        400        410        420 
FSVLRTELSK GMKTSHRPVE GPSLCVITEG EGVVRNGNDR SEFVRGDVIF VGAGKEVEWE 

       430 
AIKGLEMFRA YVEA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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. 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF291701 Genomic DNA. Translation: AAG10203.1. AE017349 Genomic DNA. Translation: AAW45398.1.
RefSeq	XP_572705.1. XM_572705.1.
3D structure databases
ProteinModelPortal	Q9HFU4.
ModBase	Search...
Protein-protein interaction databases
STRING	214684.CNI02370.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3259465.
KEGG	cne:CNI02370.
Phylogenomic databases
eggNOG	COG1482.
KO	K01809.
OrthoDB	EOG4TF3V5.
Enzyme and pathway databases
UniPathway	UPA00126; UER00423.
Family and domain databases
Gene3D	2.60.120.10. 3 hits.
InterPro	IPR001250. Man6P_Isoase-1. IPR016305. Mannose-6-P_Isomerase. IPR018050. Pmannose_isomerase-type1_CS. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR10309. PTHR10309. 1 hit.
Pfam	PF01238. PMI_typeI. 1 hit. [Graphical view]
PIRSF	PIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTS	PR00714. MAN6PISMRASE.
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR00218. manA. 1 hit.
PROSITE	PS00965. PMI_I_1. 1 hit. PS00966. PMI_I_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MPI_CRYNJ

Accession

Primary (citable) accession number: Q9HFU4
Secondary accession number(s): Q5KBJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	June 21, 2005
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents