P29952 (MPI_YEAST) 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
Ordered Locus Names:	YER003C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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.
Catalytic activity	D-mannose 6-phosphate = D-fructose 6-phosphate.
Cofactor	Binds 1 zinc ion per subunit.
Enzyme regulation	Can be inhibited by an excess of zinc.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Induction	By D-mannose.
Miscellaneous	Present with 5220 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the mannose-6-phosphate isomerase type 1 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from mutant phenotype Ref.1. Source: SGD cell wall mannoprotein biosynthetic process Inferred from mutant phenotype Ref.1. Source: SGD protein glycosylation Inferred from mutant phenotype Ref.1. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD nucleus Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	mannose-6-phosphate isomerase activity Inferred from direct assay PubMed 8011630. Source: SGD 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
	Initiator methionine	1	1	Removed
	Chain	2 – 429	428	Mannose-6-phosphate isomerase		PRO_0000194247
Sites
	Active site	300	1	By similarity
	Metal binding	109	1	Zinc By similarity
	Metal binding	111	1	Zinc By similarity
	Metal binding	136	1	Zinc By similarity
	Metal binding	281	1	Zinc By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Modified residue	107	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	25	1	A → R in AAA34872. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P29952 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: C95E7C06B348A02F	FASTA	429	48,189
	10 20 30 40 50 60 MSNKLFRLDA GYQQYDWGKI GSSSAVAQFA AHSDPSVQIE QDKPYAELWM GTHSKMPSYN 70 80 90 100 110 120 HESKESLRDI ISKNPSAMLG KDIIDKFHAT NELPFLFKVL SIEKVLSIQA HPDKALGKIL 130 140 150 160 170 180 HAQDPKNYPD DNHKPEMAIA VTDFEGFCGF KPLQEIADEL KRIPELRNIV GEETSRNFIE 190 200 210 220 230 240 NIQPSAQKGS PEDEQNKKLL QAVFSRVMNA SDDKIKIQAR SLVERSKNSP SDFNKPDLPE 250 260 270 280 290 300 LIQRLNKQFP DDVGLFCGCL LLNHCRLNAG EAIFLRAKDP HAYISGDIME CMAASDNVVR 310 320 330 340 350 360 AGFTPKFKDV KNLVSMLTYT YDPVEKQKMQ PLKFDRSSGN GKSVLYNPPI EEFAVLETTF 370 380 390 400 410 420 DEKLGQRHFE GVDGPSILIT TKGNGYIKAD GQKLKAEPGF VFFIAPHLPV DLEAEDEAFT TYRAFVEPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PMI40, an intron-containing gene required for early steps in yeast mannosylation." Smith D.J., Proudfoot A.E.I., Friedli L., Klig L.S., Paravicini G., Payton M.A. Mol. Cell. Biol. 12:2924-2930(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Phosphomannose isomerase from Saccharomyces cerevisiae contains two inhibitory metal ion binding sites." Wells T.N.C., Coulin F., Payton M.A., Proudfoot A.E.I. Biochemistry 32:1294-1301(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INHIBITION BY ZINC.
[5]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M85238 Genomic DNA. Translation: AAA34872.1. U18778 Genomic DNA. Translation: AAB64536.1. BK006939 Genomic DNA. Translation: DAA07653.1.
PIR	S50461.
RefSeq	NP_010918.1. NM_001178894.1.
3D structure databases
ProteinModelPortal	P29952.
SMR	P29952. Positions 2-427.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6619N.
IntAct	P29952. 2 interactions.
MINT	MINT-2786830.
STRING	4932.YER003C.
2D gel databases
UCD-2DPAGE	P29952.
Proteomic databases
PaxDb	P29952.
PeptideAtlas	P29952.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YER003C; YER003C; YER003C.
GeneID	856720.
KEGG	sce:YER003C.
Organism-specific databases
SGD	S000000805. PMI40.
Phylogenomic databases
eggNOG	COG1482.
GeneTree	ENSGT00390000016075.
HOGENOM	HOG000241277.
KO	K01809.
OMA	ITANSAE.
OrthoDB	EOG4TF3V5.
Enzyme and pathway databases
SABIO-RK	P29952.
UniPathway	UPA00126; UER00423.
Gene expression databases
Genevestigator	P29952.
GermOnline	YER003C. Saccharomyces cerevisiae.
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...
Other
NextBio	982811.

Entry information

Entry name

MPI_YEAST

Accession

Primary (citable) accession number: P29952
Secondary accession number(s): D3DLP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 124 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program