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
//