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Database: UniProt
Entry: U5D7B5_AMBTC
LinkDB: U5D7B5_AMBTC
Original site: U5D7B5_AMBTC 
ID   U5D7B5_AMBTC            Unreviewed;       921 AA.
AC   U5D7B5;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=AMTR_s00055p00209810 {ECO:0000313|EMBL:ERN18359.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN18359.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(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; KI392237; ERN18359.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5D7B5; -.
DR   STRING; 13333.U5D7B5; -.
DR   EnsemblPlants; ERN18359; ERN18359; AMTR_s00055p00209810.
DR   Gramene; ERN18359; ERN18359; AMTR_s00055p00209810.
DR   eggNOG; KOG1958; Eukaryota.
DR   HOGENOM; CLU_004690_1_0_1; -.
DR   OMA; GHQWLKY; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
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:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblPlants.
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; 1.
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   PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR   PANTHER; PTHR11607:SF3; LYSOSOMAL 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   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   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:UP000017836};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   DOMAIN          245..330
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   921 AA;  105332 MW;  0B577C4077925816 CRC64;
     MMEGNMWLKD TIGVIPKNAW AIDPFGYSST MAYLLRRMGF ENMLIQRTHY EVKKELALHQ
     NLEYIWRQSW DAEETTDIFV HMMPFYSYDI PHTCGPEPAV CCQFDFARTP GFFYEACPWR
     INPVETDSNN VRERALLLLD QYKKKSTLYR TNTLLIPLGD DFRYVSVDEA EAQFRNYQLI
     FDYINSNPDL KAEAKFGTLE DYFQTLRSEA ERINFSRAGE VGSREVEGFP SLSGDFFTYA
     DREKDYWSGY YVSRPFFKAV DRVLEETLRS SEIMMALLLG YCQRLPCAKL PISFAHKFTA
     ARRNLALFQH HDGVTGTAKD HVVVDYGGRM HTSLHDLQIF MAKAVEALLN IRHEKVGKST
     QPSLFEPAKL RSRYDVQPMY KTITVLEGSV QSVIFFNPLE QTRDEVVMVV VDNPSMCVLY
     SNWSSVTSQV VPEWQHGKDG LFTGRHRLYW QASVPPMGLQ TYYVANGFVG CEKARPSKLK
     VHSGSKPLPC PQPYVCSKLE ESMAEVRNQH QTLTFDVKKG MLQKLKVHKD GTETIIGEEI
     GIYSTWESGA YLFKPNGEAE PIIREGGMMI ISEGLLVNEA FSFPKTLWSK SPVSHSTRIF
     NGEDMLQKFL IEKEYHVELL DHDFNDKELI VRFKTDIDNG HVFYTDLNGF QMSRRETYKK
     IPLQGNYYPM PSHAFLHGSD GRRFSVHSRQ SLGAASLKNG WLEIMVDRRL TRDDGRGLGQ
     GVLDNRPINV LFHILTETNK SSTPIPTSLS LPLNPSLLSH LVGAHINYPM HAFIGKPEET
     SSQLPPPKHF SPLAASLPCD VHIVSFKVPR PLKFSQLSSD YPRFLLILRR RGLDSSYCRK
     GGLNCTTLGD RQINVFSMFK DFAVLDAKAT SLNLLHDDDM ERLGYYEHPH RKDLGGGTRD
     GHVLLLPMEL QAYKLELRSN L
//
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