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Database: UniProt
Entry: M5WXQ9_PRUPE
LinkDB: M5WXQ9_PRUPE
Original site: M5WXQ9_PRUPE 
ID   M5WXQ9_PRUPE            Unreviewed;      1014 AA.
AC   M5WXQ9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=PRUPE_5G142600 {ECO:0000313|EMBL:ONI07846.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI07846.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI07846.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361199};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
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DR   EMBL; CM007655; ONI07846.1; -; Genomic_DNA.
DR   RefSeq; XP_007210406.1; XM_007210344.1.
DR   AlphaFoldDB; M5WXQ9; -.
DR   STRING; 3760.M5WXQ9; -.
DR   EnsemblPlants; ONI07846; ONI07846; PRUPE_5G142600.
DR   GeneID; 18776219; -.
DR   Gramene; ONI07846; ONI07846; PRUPE_5G142600.
DR   KEGG; pper:18776219; -.
DR   eggNOG; KOG1959; Eukaryota.
DR   HOGENOM; CLU_004690_2_0_1; -.
DR   OMA; KVEPHAE; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000006882; Chromosome g5.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   CDD; cd10810; GH38N_AMII_LAM_like; 1.
DR   Gene3D; 2.60.40.1360; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
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   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR048534; Man2a1-like_dom.
DR   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF66; ALPHA-MANNOSIDASE; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   Pfam; PF21260; Laman-like_dom; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361199};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           22..1014
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5004074814"
FT   DOMAIN          355..429
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1014 AA;  114721 MW;  3CBE5B56E2D3C61E CRC64;
     MALEACFRLL LLLLLFLIAE PKYVQYNTTS RLVPGKLNVH LVPHTHDDVG WLKTVDQYYV
     GSNNSIQGAC VQNVLDSLVP ALLADKNRKF IYVEQAFFQR WWREQSEGTQ NTVRRLVNNG
     QLELINGGMC MHDEAAPHYI DMIDQTTLGH QFIKEEFNMT PRIGWQIDPF GHSAVQAYLL
     GAEAGFDSLF FARIDYQDRE KRKNEKSLEV VWRGSKSLGS SAQIFAGAFP KNYEPPTDNF
     YFEVNDESPI VQDDMDLFDY NVPDRVNEFV SAAISQANIT RTNHIMWTMG TDFKYQYANS
     WFRQMDKFIH YVNQDGRVNA LYSTPSIYTD AKYAANESWP IKSDDFFPYA DKVNAYWTGY
     FTSRPAIKGY VRALSGYYLA ARQLEFFKGM SKSRPNTDSL ADALAIAQHH DAVSGTEKQH
     VADDYAKRLS IGYNEAEKVV AESLACMTES RSEAGCKSPS TKFQQCPLLN ISYCPPSEAD
     LSNGKSLVIV VYNSLGWKRE DIIKIPVVSA NVTVRDFTGK EIESQLLPLL NASVGIRNDH
     VRAYLGISPS VTPSYWLTFS ATVPPLGFST YIVSSATQTA TSSARRTVYK SEASQNDTIE
     VGPGNLKLIY SGNKGKLTQY FNSRSSVKES IEQSFSYYAG DDGSVDKQAD GAYIFRPNGT
     YPIQSEGQDH LTVLRGPLLD EVHQRINSWI YQVTRVYKEK EHAEIEFTVG PIPIGDGIGK
     EIVTKITTSM ETNKTFYTDS NGRDFIERIR DYRKDWDLQV NQPVAGNYYP INLGIYAKDN
     NTEMSVLVDR SVGGSSIVDG QLELMVHRRL LHDDDRGVEE PLNETVCIQD ICKGLTITGK
     YYLRLDPLGE GAKWRRSFGQ EIYSPFLLAF TEQEGDNWTS SHVTTFSWMD PSYVLPDNVA
     IITLQELEDG KLLFRLAHLY EIEEDKDLSV MASVELKKVF ADKKINKVAE MSLSANQERA
     EMEKKRLTWK VEGSSEEEDA AKVMRGGPVD PTKLVVDVAP MEIRTFIIDF YSKH
//
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