ID   A0A1D6KBM7_MAIZE        Unreviewed;      1019 AA.
AC   A0A1D6KBM7;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   ORFNames=ZEAMMB73_Zm00001d030282 {ECO:0000313|EMBL:ONM00740.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM00740.1};
RN   [1] {ECO:0000313|EMBL:ONM00740.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM00740.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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; CM007647; ONM00740.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6KBM7; -.
DR   SMR; A0A1D6KBM7; -.
DR   IntAct; A0A1D6KBM7; 1.
DR   STRING; 4577.A0A1D6KBM7; -.
DR   InParanoid; A0A1D6KBM7; -.
DR   OMA; KVEPHAE; -.
DR   ExpressionAtlas; A0A1D6KBM7; baseline and differential.
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: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:SF62; 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}; Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           19..1019
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5011173711"
FT   DOMAIN          368..442
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1019 AA;  113322 MW;  FA522072FE24E4EA CRC64;
     MAPTLLLVAL VALAVAAATP MVMEASAFTE GCNNRSTPGG GGGTAVGNKL NVHLVPHSHD
     DVGWLMTIDQ YYVGSNNSIQ GACVMNTLDS VVDALAKDPA RKFIVVEQAF FQRWWAQKSL
     TVQATVHKLV DSGQLEFING GWCMHDEAVV HYIDMIDQTT LGHRVIKKQF KKIPRAGWQI
     DPFGHSAVQA YLLGAELGFD SVHFARIDYQ DRATRKANKG LEVIWRGSRP VGSSSQIFTN
     VFPVHYSAPV GFSFEVLAEN VIPVQDDMSL FDYNVQERVD DFVAAAIAQA NVTRTNHIMW
     TMGDDFNYQY AESWFRNMDK LIQYVNKDGR VHALYSTPSI YTDAKHASNE SWPVKYDDYF
     PYADSTNAYW TGYFTSRPTF KRYIRVYSGY YLAARQIEFL MGRSSLGLFT SSLEDAMGIA
     QHHDAISGTA KQHTTDDYSK RIAIGASKVE KGVNAALTCL TNSNKTCVSS VPKFSQCPLL
     NISYCPSTEE AISATKHLVV VVYNPLGWKR SDFIRVPVND EDLVVKSSDG NTVVSQIVVV
     DNVTNNLRKL YVKAYLGVTA NKAPKYWLTF QASVPPMGWN SYFILKSTGS DPGYNNTEHV
     PVVVPPSNNT IEAGQGHLKM SFSSASGQLE RIFNSASGGD LPIQQSFLWY RSSKGDALDP
     QASGAYIFRP DGNTPTIASS SVTLKVIRGP LFDEVHQQFS SWIYQITRLY KNKEHAEVEY
     TIGPIPVDDD VGKEVITQLT ANMSTNSTFY TDSNGRDFLK RVRNYREDWN LQVTQPVAGN
     YYPVNLGVYI VDEKYELSVL VDRAAGASSI QDGQLEIMLH RRLLKDDGRG VAEPLDEVVC
     VDQDCQGLTA RGTYYINVEK LGHGAHWRRT YGQQVYSPFL LAFTHEDATS SKPYSVAKDS
     MMDGNYSLPD NVAIVTLQNL DDGTTLLRLA HLFQAGEDPR YSEVAEVDLK KVFGKRTIKE
     LTETNLSANQ KKSEMKQLNW RVIEDAESGP APVKGGPVDC RALVVALGPM EIRTFLLKF
//