Q9UT61 (MAN1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-mannosidase
EC=3.2.1.24

Alternative name(s):
Alpha-D-mannoside mannohydrolase

Gene names

Name:	ams1
Synonyms:	mns2
ORF Names:	SPAC513.05

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	1077 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Degrades free oligosaccharides in the vacuole By similarity.
Catalytic activity	Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm. Vacuole By similarity Ref.2.
Sequence similarities	Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
Cellular component	Cytoplasm Vacuole
Ligand	Metal-binding Zinc
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mannose metabolic process Inferred from electronic annotation. Source: InterPro oligosaccharide catabolic process Inferred from sequence orthology. Source: PomBase
Cellular_component	cytosol Inferred from direct assay Ref.2. Source: PomBase fungal-type vacuole membrane Inferred from sequence orthology. Source: PomBase
Molecular_function	alpha-mannosidase activity Inferred from sequence orthology. Source: PomBase carbohydrate binding Inferred from electronic annotation. Source: InterPro 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 – 1077	1077	Alpha-mannosidase		PRO_0000363389
Sites
	Active site	402	1	Nucleophile By similarity
	Metal binding	290	1	Zinc By similarity
	Metal binding	292	1	Zinc By similarity
	Metal binding	402	1	Zinc By similarity
	Metal binding	615	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9UT61 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8774DDF4A2194A46	FASTA	1,077	122,438
	10 20 30 40 50 60 MTLFPVLNNT PVGKQVDSIY ESRLDQFLSE GQYRDFNLPS VYDHARIDNP SGDVNNDLSK 70 80 90 100 110 120 GFVDLKVYRV PDLSRPSFNE VVGHKKFDET ASKGDTFGPS WATFWFEVHI RLPKSWAKYE 130 140 150 160 170 180 QVIFQWNCDN EGLVYSQDGV PLQAFSGSER TDFILPDSWK TTEDTFYIEM ACNGMFGTGA 190 200 210 220 230 240 GSQIAPPDPN RYFTLTKADL VAPNLPAMAL AYDFLLMQQC VKQLPSNCWQ KYKARQICND 250 260 270 280 290 300 IMNTFHPNDL STINECRNLA KAFLGNDIDS EAVFEKNNDK ANVFAIGHCH IDTAWLWPFA 310 320 330 340 350 360 ETRRKIVRSW ATQMNIMDRY PEYQFVCSQA LQYLWLKEDH PDVFEKLKEY VNQNKFIPIG 370 380 390 400 410 420 GSWVEHDTNI PNGESLIRQF LLGQHFFEKE FGVRCRTFWL PDTFGYSSQI PQICRLCGMD 430 440 450 460 470 480 RFLTQKLSWN NINSFPTSTF NWVALDGSQV ICHMPPANTY TADTNVNDVL HSIDQHKNLV 490 500 510 520 530 540 NDQAGLLVFG IGDGGGGPTP EMLEKLRRCK GIANTVGYLP NVKLGNTVDE FFDGILKRTN 550 560 570 580 590 600 AGQTLPSWNG ELYFEFHRGT YTTQAELKKL MRKVEIALHD AEYVSTLASI FSKDYSYPKE 610 620 630 640 650 660 SLQDLWRDTL LCQFHDVLPG SCIEMVYKDA IPIMSKVLKN TEALLWQAIE QLGFKKASSS 670 680 690 700 710 720 DNKEQLCLLN TLPWNVRGVI TETEENKLVY FESCDGKGIL TAAHTSLKHP AAAYQKDDNF 730 740 750 760 770 780 ILVNDHLRVT IAPNGLILSL FDLHKEREIL DLKSGKNHAG ANQYVLFEDT PLSWQAWDTE 790 800 810 820 830 840 VFSLEKYEVL DKGKVSIKES GPLRASVVVD IPISELSHMK ATISLEGYND CSEFTGVNFT 850 860 870 880 890 900 CEVDWHESCK FLKVEFPVDI HSEFASYETQ FGITKRPTHY NTSWDVAKFE VCHQKFADYS 910 920 930 940 950 960 DFTYGVSVLN DCKYGFSTHG NLMRLSLLRS PKQPDAHADM GKHTIRYAVY PHSKPLDSST 970 980 990 1000 1010 1020 VRAAHKFNSN FRLLTRASDT ANLDIFDAFQ LVGEPNVILS HIKMAEKGKS IILRVYESLG 1030 1040 1050 1060 1070 GKSRARLVIK SLTVASVTKC NGLEEDLEEL CTLKSNDYYE VPIELRAFEI ATFKVNL

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	CU329670 Genomic DNA. Translation: CAB58728.1.
PIR	T38900.
RefSeq	NP_593979.1. NM_001019405.2.
3D structure databases
ProteinModelPortal	Q9UT61.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4709700.
STRING	4896.SPAC513.05-1.
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC513.05.1; SPAC513.05.1:pep; SPAC513.05.
GeneID	2543485.
KEGG	spo:SPAC513.05.
Organism-specific databases
PomBase	SPAC513.05.
Phylogenomic databases
eggNOG	COG0383.
HOGENOM	HOG000048425.
KO	K01191.
OMA	DPEKMFQ.
OrthoDB	EOG4NS6KN.
Family and domain databases
Gene3D	3.20.110.10. 1 hit.
InterPro	IPR011013. Gal_mutarotase_SF_dom. IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR027291. Glyco_hydro_38/57_N. IPR011682. Glyco_hydro_38_C. IPR015341. Glyco_hydro_38_cen_dom. IPR000602. Glyco_hydro_38_N. [Graphical view]
Pfam	PF09261. Alpha-mann_mid. 1 hit. PF01074. Glyco_hydro_38. 1 hit. PF07748. Glyco_hydro_38C. 1 hit. [Graphical view]
SMART	SM00872. Alpha-mann_mid. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...
Other
NextBio	20804497.

Entry information

Entry name

MAN1_SCHPO

Accession

Primary (citable) accession number: Q9UT61

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 10, 2009
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program