ID M5WR08_PRUPE Unreviewed; 1027 AA.
AC M5WR08;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=PRUPE_3G313400 {ECO:0000313|EMBL:ONI20071.1};
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:ONI20071.1, ECO:0000313|Proteomes:UP000006882};
RN [1] {ECO:0000313|EMBL:ONI20071.1, 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; CM007653; ONI20071.1; -; Genomic_DNA.
DR RefSeq; XP_007214915.1; XM_007214853.1.
DR AlphaFoldDB; M5WR08; -.
DR EnsemblPlants; ONI20071; ONI20071; PRUPE_3G313400.
DR GeneID; 18781643; -.
DR Gramene; ONI20071; ONI20071; PRUPE_3G313400.
DR KEGG; pper:18781643; -.
DR eggNOG; KOG1959; Eukaryota.
DR HOGENOM; CLU_004690_2_0_1; -.
DR OMA; LVEIEWQ; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000006882; Chromosome g3.
DR GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
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:SF60; 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|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..32
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 33..1027
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5004074547"
FT DOMAIN 365..439
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1027 AA; 114870 MW; 7600C00EEB46525E CRC64;
MASSTATSML CFTAAAVAAV LLAGLLPLGA KAEYIAYNTT AGIVPGKINV HLVPHSHDDV
GWLKTVDQYY VGANNSIRGA CVQNVLDSVI SALLEDKNRK FIYVEIAFFQ RWWRQQSPAL
KIKVKELVNS GQLEFINGGM CMHDEATPHY IDLIDQTTLG HQFILKEFGK VPRVGWQIDP
FGHSAVQAYL LGAELGFDSL FFARIDYQDR ARRLRDKTLE VIWQGSKSLA SSSQIFTGIF
PRHYDPPDGF TFEINDVSPP IQDDILLFDY NVQDRVNDFV AAAFAQANVT RTNHIMWNMG
TDFRYQYANS WFRQMDKFIH YVNQDGRVNA LYSTPSIYTD AKYAAHEQWP LKTDDFFPYA
DHPNAYWTGY FTSRPALKGY VRTMSSYYQA ARQLEFFRGR SDSGATTGAL ADALAIAQHH
DAVSGTERQH VAADYAMRLS IGYLQAEKLV ASSLAYLSES ESSSGQGHTV TNFQQCPFLN
ISYCPPSEAV LSDGKSLIVV VYNSLGWKRE EVIRIPVSNE AVTVQDSSGR DIEAQLLPLS
KASLSLRSYY VRAYLGKSPS EPPKFWLAFS VTVPPIGFSS YIVSSAKPTG RSSTISNVYT
SEGSTNETIE VGQGSLKLHY SVDEGKLARY VNSRSLVTAS VEQSYSYYTG NDGTDRDPQA
SGAYVFRPNG TVLIKSEQKV PLTVMRGPVL DEVHQQLNPW VSQITRVYKG KEHAEVEFTI
GPIPVDDGIG KEITTQITTA MKTNKTFYTD SNGRDFIKRI RDFRTDWDLQ VNQPIAGNYY
PINLGIYLQD SSTELSVLVD RSVGGSSLVD GQIELMLHRR LFHDDSRGVG EVLNETVCIL
DKCEGLTIQG KFYVRIDNVG EGAKWRRTAG QEINSPLLLA FTEQDENDWM NSHASTFSGI
DPSYALPNNI AVITLQELEN GKVLFRLAHL YETGEDKDYS VLANVELKKL FPRKKISKVT
EMSLSANQER SEMEKKRLVW KAEGSAAKDP KVVRGGPVDP AKLLVELAPM EIRTFLIDFD
YLHMYSI
//
