MAN1_SCHPO
ID MAN1_SCHPO Reviewed; 1077 AA.
AC Q9UT61;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Alpha-mannosidase;
DE EC=3.2.1.24;
DE AltName: Full=Alpha-D-mannoside mannohydrolase;
GN Name=ams1; Synonyms=mns2; ORFNames=SPAC513.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Degrades free oligosaccharides in the vacuole. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues
CC in alpha-D-mannosides.; EC=3.2.1.24;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Vacuole
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB58728.1; -; Genomic_DNA.
DR PIR; T38900; T38900.
DR RefSeq; NP_593979.1; NM_001019405.2.
DR PDB; 6LZ1; EM; 3.20 A; A/B/C/D=1-1077.
DR PDB; 7DD9; EM; 2.40 A; A/C/E/G=1-1077.
DR PDBsum; 6LZ1; -.
DR PDBsum; 7DD9; -.
DR AlphaFoldDB; Q9UT61; -.
DR SMR; Q9UT61; -.
DR BioGRID; 279905; 1.
DR STRING; 4896.SPAC513.05.1; -.
DR CAZy; GH38; Glycoside Hydrolase Family 38.
DR iPTMnet; Q9UT61; -.
DR MaxQB; Q9UT61; -.
DR PaxDb; Q9UT61; -.
DR PRIDE; Q9UT61; -.
DR EnsemblFungi; SPAC513.05.1; SPAC513.05.1:pep; SPAC513.05.
DR GeneID; 2543485; -.
DR KEGG; spo:SPAC513.05; -.
DR PomBase; SPAC513.05; ams1.
DR VEuPathDB; FungiDB:SPAC513.05; -.
DR eggNOG; KOG4342; Eukaryota.
DR HOGENOM; CLU_003442_0_1_1; -.
DR InParanoid; Q9UT61; -.
DR OMA; GQYWDAW; -.
DR PhylomeDB; Q9UT61; -.
DR Reactome; R-SPO-8853383; Lysosomal oligosaccharide catabolism.
DR PRO; PR:Q9UT61; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0052767; F:mannosyl-oligosaccharide 1,6-alpha-mannosidase activity; ISS:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR Gene3D; 1.20.1270.50; -; 1.
DR Gene3D; 3.20.110.10; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR041147; GH38_C.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF88688; SSF88688; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycosidase; Hydrolase; Metal-binding;
KW Reference proteome; Vacuole; Zinc.
FT CHAIN 1..1077
FT /note="Alpha-mannosidase"
FT /id="PRO_0000363389"
FT ACT_SITE 402
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 79..84
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:6LZ1"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 205..223
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 229..244
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 282..288
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 299..319
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 341..352
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 373..390
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 447..453
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 466..474
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 477..481
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 500..515
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 528..538
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 539..544
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 565..591
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 599..611
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 615..620
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 624..652
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 663..665
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 666..669
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 678..686
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 688..692
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 697..702
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 720..723
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 725..731
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 737..742
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 743..746
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:6LZ1"
FT STRAND 753..756
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 761..768
FT /evidence="ECO:0007829|PDB:7DD9"
FT TURN 775..777
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 781..785
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 786..790
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 794..800
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 802..814
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 817..826
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 828..830
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 831..833
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 837..845
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 848..857
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 863..869
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 872..879
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 883..887
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 889..892
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 894..900
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 905..912
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 915..919
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 922..929
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 941..956
FT /evidence="ECO:0007829|PDB:7DD9"
FT HELIX 958..967
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 972..977
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 988..993
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 997..1004
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1006..1009
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1011..1021
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1023..1029
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1034..1040
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1046..1050
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1061..1065
FT /evidence="ECO:0007829|PDB:7DD9"
FT STRAND 1070..1077
FT /evidence="ECO:0007829|PDB:7DD9"
SQ SEQUENCE 1077 AA; 122438 MW; 8774DDF4A2194A46 CRC64;
MTLFPVLNNT PVGKQVDSIY ESRLDQFLSE GQYRDFNLPS VYDHARIDNP SGDVNNDLSK
GFVDLKVYRV PDLSRPSFNE VVGHKKFDET ASKGDTFGPS WATFWFEVHI RLPKSWAKYE
QVIFQWNCDN EGLVYSQDGV PLQAFSGSER TDFILPDSWK TTEDTFYIEM ACNGMFGTGA
GSQIAPPDPN RYFTLTKADL VAPNLPAMAL AYDFLLMQQC VKQLPSNCWQ KYKARQICND
IMNTFHPNDL STINECRNLA KAFLGNDIDS EAVFEKNNDK ANVFAIGHCH IDTAWLWPFA
ETRRKIVRSW ATQMNIMDRY PEYQFVCSQA LQYLWLKEDH PDVFEKLKEY VNQNKFIPIG
GSWVEHDTNI PNGESLIRQF LLGQHFFEKE FGVRCRTFWL PDTFGYSSQI PQICRLCGMD
RFLTQKLSWN NINSFPTSTF NWVALDGSQV ICHMPPANTY TADTNVNDVL HSIDQHKNLV
NDQAGLLVFG IGDGGGGPTP EMLEKLRRCK GIANTVGYLP NVKLGNTVDE FFDGILKRTN
AGQTLPSWNG ELYFEFHRGT YTTQAELKKL MRKVEIALHD AEYVSTLASI FSKDYSYPKE
SLQDLWRDTL LCQFHDVLPG SCIEMVYKDA IPIMSKVLKN TEALLWQAIE QLGFKKASSS
DNKEQLCLLN TLPWNVRGVI TETEENKLVY FESCDGKGIL TAAHTSLKHP AAAYQKDDNF
ILVNDHLRVT IAPNGLILSL FDLHKEREIL DLKSGKNHAG ANQYVLFEDT PLSWQAWDTE
VFSLEKYEVL DKGKVSIKES GPLRASVVVD IPISELSHMK ATISLEGYND CSEFTGVNFT
CEVDWHESCK FLKVEFPVDI HSEFASYETQ FGITKRPTHY NTSWDVAKFE VCHQKFADYS
DFTYGVSVLN DCKYGFSTHG NLMRLSLLRS PKQPDAHADM GKHTIRYAVY PHSKPLDSST
VRAAHKFNSN FRLLTRASDT ANLDIFDAFQ LVGEPNVILS HIKMAEKGKS IILRVYESLG
GKSRARLVIK SLTVASVTKC NGLEEDLEEL CTLKSNDYYE VPIELRAFEI ATFKVNL
