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Database: UniProt
Entry: A0A1S3USP0_VIGRR
LinkDB: A0A1S3USP0_VIGRR
Original site: A0A1S3USP0_VIGRR 
ID   A0A1S3USP0_VIGRR        Unreviewed;      1008 AA.
AC   A0A1S3USP0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=LOC106768403 {ECO:0000313|RefSeq:XP_014509035.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014509035.1};
RN   [1] {ECO:0000313|RefSeq:XP_014509035.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014509035.1};
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
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   RefSeq; XP_014509035.1; XM_014653549.2.
DR   AlphaFoldDB; A0A1S3USP0; -.
DR   GeneID; 106768403; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000087766; Chromosome 7.
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:SF61; 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:UP000087766};
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..1008
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5017854682"
FT   DOMAIN          357..431
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1008 AA;  112624 MW;  9A5210FE7D60BEC1 CRC64;
     MVAQTLSAFL WLSFCATLVS AKYIRYNTGA AIAPGKLNVH LVPHSHDDVG WLKTVDQYYV
     GSNNSIQGAC VENVLDSVVV SLKKDPNRKF VFAEMAFFHR WWVEQSPETQ EEVRKLVNAG
     QLEIINGGWC MHDEAATHYI DMIDQTTLGH RFIKDEFNKT PTVGWQIDPF GHSAVQAYLL
     GAELGFDSVH FARIDYQDRA KRKADKSLEV VWRASKTFGS SAQIFANAFP VHYSAPNGFN
     FEVNNADVNV VPVQDDPLLF DYNVEQRVKD FIEAATTQAN VTRTNHIMWT MGDDFQYQYA
     ESWFKQMDKL IHYVNKDGRV NALYSTPSIY TNAKNAANQT WPLKTDDYFP YADSANAYWT
     GYFTSRPALK RYVRMTSGYY LATRQLEFFA GKQSAKYNTF GLGDALGIAQ HHDAVSGTAK
     QHTTNDYAKR LAIGVSEAEA VVSSSLACLT SKKSSDQCSE PASAFAQCQL LNISYCPPTE
     DNIPDAKSLV VVVYNPLGWK RTDIVKIPVN DANLVVQDSL GNNIEVQYVD VDDVTTNLRN
     FYVKAYLGVS PKQAPKYWLL FQASVPPLGW STYFISKATG TGSETKNLSN LGSQRGDTVV
     IGPGNLKMSF SSASGQLKRM YNSRTGVDIP IQQSYLYYGS SEGDSDPQAS GAYIFRPNGS
     PPTIISRSVP TKVIRGPLVD EVHQKFSSWI YQVTRLYKGK DHAEVEFTIG PIPTDDGVGK
     EVITRMTANM ATNKEFYTDS NGRDFLKRVR DHRDDWPLQV TQPVAGNYYP INLGIYTKDK
     KSEFSVLVDR ATGGASIKDG EVELMLHRRI LHDDGRGVGE ALDEQVCVNN NKTCEGLTVR
     GNYYISIDKL GAGARWRRTT GQEIYSPFLL AFTHENLESW KSSHWTKGTI LDPNYSLPPN
     VALITLEELD GGVVLLRLAH LYEPSEDAEY STLTKVELKK LIAKKTIKEL KEVSLSANQE
     KSEIKKMTWK VEGDNGQEAQ GLRGGPVSSP NLVVELGPME IRTFLLKL
//
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