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Protein

Alpha-mannosidase

Gene

AMS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Degrades free oligosaccharides in the vacuole.1 Publication

Catalytic activityi

Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi298 – 2981ZincBy similarity
Metal bindingi300 – 3001ZincBy similarity
Active sitei411 – 4111NucleophileBy similarity
Metal bindingi411 – 4111ZincBy similarity
Metal bindingi626 – 6261ZincBy similarity

GO - Molecular functioni

  1. alpha-mannosidase activity Source: SGD
  2. carbohydrate binding Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: SGD
  2. mannose metabolic process Source: InterPro
  3. oligosaccharide catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:YGL156W-MONOMER.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-mannosidase (EC:3.2.1.24)
Alternative name(s):
Alpha-D-mannoside mannohydrolase
Gene namesi
Name:AMS1
Ordered Locus Names:YGL156W
ORF Names:G1861
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGL156w.
SGDiS000003124. AMS1.

Subcellular locationi

Vacuole 2 Publications
Note: Localizes to the inner surface of the vacuolar membrane. Under nutrient-rich conditions, the protein is delivered to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway. Under starvation conditions, the protein is localized through autophagy.

GO - Cellular componenti

  1. fungal-type vacuole membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10831082Alpha-mannosidasePRO_0000206910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP22855.
PaxDbiP22855.
PeptideAtlasiP22855.

Expressioni

Gene expression databases

GenevestigatoriP22855.

Interactioni

Subunit structurei

Composed of isoforms with three constituent polypeptides described as [(107 kDa)-n (73 kDa)-(6-n) (31 kDa)-(6-n)], where n is 0-6. The 73 kDa and the 31 kDa polypeptides may be proteolytic derivatives of the 107 kDa polypeptide in the vacuole. Oligomerizes in the cytoplasm and retains its oligomeric form during import into the vacuole.

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG34Q122923EBI-10398,EBI-36362

Protein-protein interaction databases

BioGridi33098. 16 interactions.
DIPiDIP-5497N.
IntActiP22855. 8 interactions.
MINTiMINT-484580.
STRINGi4932.YGL156W.

Structurei

3D structure databases

ProteinModelPortaliP22855.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 38 family.Curated

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00390000006338.
HOGENOMiHOG000048425.
InParanoidiP22855.
KOiK01191.
OMAiKRSVTQH.
OrthoDBiEOG79SF5G.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. 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.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22855-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEDIIYDP QFKPVQGIYE NRLRQFIDTG GDYHDLNLPK FYDKKRISLD
60 70 80 90 100
HDHVKVWWYQ VSFERGSSPV SPDKRPSWKS IIERDKKGEL EFREANINQP
110 120 130 140 150
FGPSWSTTWF KVKISLPEDW VKSNEQLLFQ WDCSNEGIVI DPKTLIPVTA
160 170 180 190 200
FSGGERTEYV LPKTSDGKHF FYIEAGNNGM FGCGAGSTIN PPDDNRFFHL
210 220 230 240 250
RKADIVWPDL DARALYIDFW MLGDAARELP GDSWQKHQAR QLGNAVMNLF
260 270 280 290 300
DPNDRSSVRK CRELLQREYF DSFLESSKVY EQGESQVLTN VYGIGNCHID
310 320 330 340 350
TAWLWPFAET RRKIVRSWSS QCTLMDRFPE YKFVASQAQQ FKWLLEDHPE
360 370 380 390 400
FFNKVLIPKI QQSQFFAVGG TWVENDTNIP SGESLARQFF FGQRFFLKHF
410 420 430 440 450
GLKSKIFWLP DTFGYSSQMP QLCRLSGIDK FLTQKLSWNN INSFPHSTFN
460 470 480 490 500
WAGIDGSQLL THMPPGNTYT ADSHFGDVLR TAKQNKTPEY YGSGLMLYGK
510 520 530 540 550
GDGGGGPTEE MLQKMRRIRS MNNRNGNVIP KLQVGITVDE FYDDILKRTN
560 570 580 590 600
QGHDLPTWSG ELYFEFHRGT YTSQAQTKKL MRLSEIKLHD LEWIAAKTSV
610 620 630 640 650
LYPDSYKYPS KQINELWENV LLCQFHDVLP GSCIEMVYKY EAVPMLHNVV
660 670 680 690 700
KECTSLIDKT VQFLQSQSKA DLVEMRTLTW SKPEKVSEEC SLNGSYTSSV
710 720 730 740 750
TGYDDYIVLA NGKLKVIICK KTGVITSITD ETLGVEYLDT EHGRNKLGAN
760 770 780 790 800
QFVIYDDKPL GWQAWDTELY SVNQYKYVTK PKKVQVSCNT KEKCAVEVIF
810 820 830 840 850
QISEKCKIKS VISLNATAVT DAKLSKVDIS TTVENWDARN KFLKVEFPVN
860 870 880 890 900
IRNDFASYET QFGITKRPTH YNTSWDVAKF EVCHHKFADY SEYSKGVSIL
910 920 930 940 950
NDCKYGFSTH GNLMRLSLLR SPKAPDAHAD MGTHEIKYAI YPHRGALSSD
960 970 980 990 1000
TVKLAHEFNY CFKYKLPKDI GMNFDDIISI SGDENVILSN IKRGEDDSAV
1010 1020 1030 1040 1050
KSNYSLNPRD EQSIVVRVYE SLGGESFASL NTTLNLKRIE KVDNLEMKVY
1060 1070 1080
KSLTATRDES NHAINRIPIK LRPFEIASFR LYF
Length:1,083
Mass (Da):124,499
Last modified:January 31, 1996 - v2
Checksum:i624C818040FF5127
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti786 – 7861V → L in AAA34423 (PubMed:2675832).Curated
Sequence conflicti798 – 7981V → A in AAA34423 (PubMed:2675832).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29146 Genomic DNA. Translation: AAA34423.1.
Z48618 Genomic DNA. Translation: CAA88536.1.
Z72678 Genomic DNA. Translation: CAA96868.1.
BK006941 Genomic DNA. Translation: DAA07956.1.
PIRiS60420. S53048.
RefSeqiNP_011359.1. NM_001181021.1.

Genome annotation databases

EnsemblFungiiYGL156W; YGL156W; YGL156W.
GeneIDi852721.
KEGGisce:YGL156W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29146 Genomic DNA. Translation: AAA34423.1.
Z48618 Genomic DNA. Translation: CAA88536.1.
Z72678 Genomic DNA. Translation: CAA96868.1.
BK006941 Genomic DNA. Translation: DAA07956.1.
PIRiS60420. S53048.
RefSeqiNP_011359.1. NM_001181021.1.

3D structure databases

ProteinModelPortaliP22855.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33098. 16 interactions.
DIPiDIP-5497N.
IntActiP22855. 8 interactions.
MINTiMINT-484580.
STRINGi4932.YGL156W.

Protein family/group databases

CAZyiGH38. Glycoside Hydrolase Family 38.

Proteomic databases

MaxQBiP22855.
PaxDbiP22855.
PeptideAtlasiP22855.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL156W; YGL156W; YGL156W.
GeneIDi852721.
KEGGisce:YGL156W.

Organism-specific databases

CYGDiYGL156w.
SGDiS000003124. AMS1.

Phylogenomic databases

eggNOGiCOG0383.
GeneTreeiENSGT00390000006338.
HOGENOMiHOG000048425.
InParanoidiP22855.
KOiK01191.
OMAiKRSVTQH.
OrthoDBiEOG79SF5G.

Enzyme and pathway databases

BioCyciYEAST:YGL156W-MONOMER.

Miscellaneous databases

NextBioi972102.
PROiP22855.

Gene expression databases

GenevestigatoriP22855.

Family and domain databases

Gene3Di1.20.1270.50. 1 hit.
3.20.110.10. 1 hit.
InterProiIPR011013. 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.
IPR000602. Glyco_hydro_38_N.
IPR028995. Glyco_hydro_57/38_cen.
[Graphical view]
PfamiPF09261. Alpha-mann_mid. 1 hit.
PF01074. Glyco_hydro_38. 1 hit.
PF07748. Glyco_hydro_38C. 1 hit.
[Graphical view]
SMARTiSM00872. Alpha-mann_mid. 1 hit.
[Graphical view]
SUPFAMiSSF74650. SSF74650. 1 hit.
SSF88688. SSF88688. 1 hit.
SSF88713. SSF88713. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of AMS1, the structure gene of vacuolar alpha-mannosidase of Saccharomyces cerevisiae."
    Yoshihisa T., Anraku Y.
    Biochem. Biophys. Res. Commun. 163:908-915(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43."
    James C.M., Indge K.J., Oliver S.G.
    Yeast 11:1413-1419(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "A novel pathway of import of alpha-mannosidase, a marker enzyme of vacuolar membrane, in Saccharomyces cerevisiae."
    Yoshihisa T., Anraku Y.
    J. Biol. Chem. 265:22418-22425(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae."
    Hutchins M.U., Klionsky D.J.
    J. Biol. Chem. 276:20491-20498(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p)."
    Chantret I., Frenoy J.-P., Moore S.E.H.
    Biochem. J. 373:901-908(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAN1_YEAST
AccessioniPrimary (citable) accession number: P22855
Secondary accession number(s): D6VTZ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1991
Last sequence update: January 31, 1996
Last modified: January 6, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

It is not specific for the 1,2-alpha-mannosidic linkage.
Present with 319 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.