O43014 (MPI_SCHPO) Reviewed, UniProtKB/Swiss-Prot

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:	pmi40
ORF Names:	SPBC2G2.16

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	412 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. Nucleus Ref.2.
Sequence similarities	Belongs to the mannose-6-phosphate isomerase type 1 family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from sequence orthology. Source: PomBase cell wall mannoprotein biosynthetic process Inferred from sequence orthology. Source: PomBase protein glycosylation Inferred from sequence orthology. Source: PomBase
Cellular_component	cytosol Inferred from direct assay Ref.2. Source: PomBase nucleus Inferred from direct assay Ref.2. Source: PomBase
Molecular_function	mannose-6-phosphate isomerase activity Inferred from sequence orthology. Source: PomBase 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 – 412	412	Mannose-6-phosphate isomerase		PRO_0000314774
Sites
	Active site	284	1	By similarity
	Metal binding	99	1	Zinc By similarity
	Metal binding	101	1	Zinc By similarity
	Metal binding	126	1	Zinc By similarity
	Metal binding	265	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	O43014 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: E1B4685C02B25C89	FASTA	412	45,590
	10 20 30 40 50 60 MYRLKCDVKS YGWGKVGHES LAAKLAEAGY GFEVDPNTPY AELWMGSHPS GPSFVMQTGK 70 80 90 100 110 120 PLSELLTPET VGEKVYKKYG KQLPFLFKVL SINKVLSIQA HPDKPLGKQL HKTNPKEYKD 130 140 150 160 170 180 DNHKPEMAVA LTEFDALCGF RPVKQIEQFL DSIAPLREFV GEEAVRQFKG TVKQDERKAL 190 200 210 220 230 240 ETLFNELMHK DEKRIQEFTP QLVQLAKSDA NNFGGTEYGG KAFSDLIIHL NSQFPDDIGL 250 260 270 280 290 300 FVTPFLNYVR LHPGEAVFLR ALDPHAYVSG NIIECMAASD NVIRLGFTPK FKDIETLVNN 310 320 330 340 350 360 LTYQTADAKS QLTQPVPFAK ACGSGKTLLY DPPIEEFSIL QTKVSPGQKQ CIRGINGPSI 370 380 390 400 410 LLVTEGSGIL NGDKGDVASI SPGFVYFISA NFPLTISATS EPVVVYQAFC EI

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

[2]

"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAA17896.1.
PIR	T40155.
RefSeq	NP_596445.1. NM_001022364.2.
3D structure databases
ProteinModelPortal	O43014.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4674647.
STRING	4896.SPBC2G2.16-1.
Proteomic databases
PaxDb	O43014.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC2G2.16.1; SPBC2G2.16.1:pep; SPBC2G2.16.
GeneID	2540428.
KEGG	spo:SPBC2G2.16.
Organism-specific databases
PomBase	SPBC2G2.16.
Phylogenomic databases
eggNOG	COG1482.
HOGENOM	HOG000241277.
KO	K01809.
OMA	VMKMEVP.
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. [Graphical view]
ProtoNet	Search...
Other
NextBio	20801555.

Entry information

Entry name

MPI_SCHPO

Accession

Primary (citable) accession number: O43014

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 1998
Last modified:	May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program