ID A0A3B6LWV5_WHEAT Unreviewed; 984 AA.
AC A0A3B6LWV5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752, ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=CFC21_074532 {ECO:0000313|EMBL:KAF7068808.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS5B02G496400.2};
RN [1] {ECO:0000313|EMBL:KAF7068808.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7068808.1};
RX PubMed=29069494;
RA Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT "The first near-complete assembly of the hexaploid bread wheat genome,
RT Triticum aestivum.";
RL Gigascience 6:1-7(2017).
RN [2] {ECO:0000313|EnsemblPlants:TraesCS5B02G496400.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring
RC {ECO:0000313|EnsemblPlants:TraesCS5B02G496400.2};
RX PubMed=30115783; DOI=10.1126/science.aar7191;
RG International wheat genome sequencing consortium (IWGSC);
RT "Shifting the limits in wheat research and breeding using a fully annotated
RT reference genome.";
RL Science 361:EAAR7191-EAAR7191(2018).
RN [3] {ECO:0000313|EnsemblPlants:TraesCS5B02G496400.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (OCT-2018) to UniProtKB.
RN [4] {ECO:0000313|EMBL:KAF7068808.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:KAF7068808.1};
RA Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT aestivum) genome.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
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; CM022224; KAF7068808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B6LWV5; -.
DR EnsemblPlants; TraesCS5B02G496400.2; TraesCS5B02G496400.2; TraesCS5B02G496400.
DR Gramene; TraesCS5B02G496400.2; TraesCS5B02G496400.2; TraesCS5B02G496400.
DR Gramene; TraesCS5B03G1205400.2; TraesCS5B03G1205400.2.CDS; TraesCS5B03G1205400.
DR Proteomes; UP000019116; Chromosome 5B.
DR Proteomes; UP000815260; Chromosome 5B.
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 GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProt.
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; 2.
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; IPR041147; GH38_C.
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:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF17677; Glyco_hydro38C2; 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:UP000019116};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 25..984
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5040519740"
FT DOMAIN 324..398
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 984 AA; 110056 MW; 15B341C55ABF3BB4 CRC64;
MGPVRLALLL LAAAAAVLLG GGEAVYIPYN TSAGVVNGKL NVHVVPHTHD DVGWLKTVDQ
YYVGSNNSIQ NACVQNVLDS LVPALLKDEN RKFIYVEQAF FQRWWRQQSD MIDQTTLGHR
FIKEEFGQIP RIGWQIDPFG HSAVQAYLLG AEVGFDALYF FRIDYQDRDT RNVTKELEVV
WRGSKTFGSS ADIFAGIFPK NYEPPPGEFY FEVDDTSPVV QDDPLLFDYN VEQRVNDFVA
AALAQANVTR TNHIMFTMGT DFKYQYAESW FRQMDKLIHY VNKDGRVNAL YSTPSIYTDA
KFSANEPWPL KTNDFFPYAD NPNAYWTGYF TSRPALKRYV RMMSGYYLAA RQLEFFIGRS
KSGSTTDSLG DALALAQHHD AVTGTEKQHV ANDYAKRLSI GYKKAEELVS TSLGCLSESD
SNSRCSSPTT KFGQCPLLNI TYCPPSEMNL SQGKSLVVLV YNSLGWKRED VLRIPVMSDS
IVVHDSEGRE IESQLLPIAN ASSHLRDRHV KAYLGTSPAA SPKFWVAFPA SVPPLGFSTY
FISSGKRSAS ISSTSTLNSQ GSESRNLQVG QGHLKLQYDA AGALSQYSDS KTQVEANFEQ
KYKYYIGQDG GGDDPQASGA YIFRPKDVVP IKTDGQVPPM ILRGPILDEV HQQINPWIYQ
ITRVYKGKDY METEFIVGPI PIDDENGKEL STEIITSMAT NKTFYIDSSG RDFIKRVRDY
RSEWKIQVNQ PVAGNYYPIN LGIYVEDGSK ELSILVDRSV GGSSIKDGQI EIMLHRRLLN
DDGRGVAEAL EEKVCLDDQC EGLVIQGKYY LKIDPQGDGA RWRRTFGQEL YSPLLLAFAE
KDGGNWANSH VSSFSAMDPT YSLPENVALL TLEELEDGSV LLRLAHLYEA GEHKDLSAPA
SVDLKRVFPD KKIGKIIETS LSANQERAAM EKKRLKWKVA GPPPKENVVR GGPVDPSKLV
VELAPMEIRT FVINFDHRLA AHPI
//
