ID Q10A54_ORYSJ Unreviewed; 815 AA.
AC Q10A54;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN OrderedLocusNames=LOC_Os10g05069 {ECO:0000313|EMBL:ABG65905.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000313|EMBL:ABG65905.1};
RN [1] {ECO:0000313|EMBL:ABG65905.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12791992; DOI=10.1126/science.1083523;
RG Rice Chromosome 10 Sequencing Consortium;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2] {ECO:0000313|EMBL:ABG65905.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell C.R., Wing R.A., McCombie W.R., Messing J., Yuan Q., Ouyang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABG65905.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell R.;
RL Submitted (JUL-2006) 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; DP000086; ABG65905.1; -; Genomic_DNA.
DR RefSeq; XP_015614376.1; XM_015758890.1.
DR AlphaFoldDB; Q10A54; -.
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 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|RuleBase:RU361199, ECO:0000313|EMBL:ABG65905.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT DOMAIN 166..240
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 815 AA; 91528 MW; CACB089B9B3E2BA1 CRC64;
MHFARIDYQD RAKRKGDKGL EVIWRGSRTF GSSSQIFTNA FPVHYSPPDG FGFEIFDDFV
PVQDDMLLFD YNLKERVNDF VAAALKQANV TRTNHIMWTM GDDFNYQYAE SWFRNMDRLI
NYVNKDGRVH ALYSTPSIYT DAKHASNESW PLKYDDYFPY ADAKNAYWTG YFTSRPTFKR
YIRMISGYYL AARQLEFLVG RSSLGLFTSS LEDPLGIAQH HDAVSGTAKQ HTTDDYSKRL
AIGVSQVEKG VNTALSCLTS SKGTCTATKF SQCQLLNISY CPSTEEGISS AKSLVIVVYN
PLGWERSDFV RVPVNDANLI VKTSDGTSLE SQLVEVDIVT ARLRKLYIKA YLGITSDKPP
KYWLVFQASV PPLGWNTYFI SKSTGTGSNG MGYVSTMVSP SNDTIEIGPG PLKMSYSSKS
GQLKRMFNSI SAVDLPIQQS FLWYASSTGD SEDSQASGAY IFRPNRTTPT IVSGMAPLKV
IHGPLVDEVH QQFSSWIYQV TRLYKNKEHA EVEYTIGPIP VDDDDDIGKE VVTRLTTNMA
TNKIFYTDSN GRDFLERVRN HRDDWDLNLS QPVAGNYYPV NQGIYVADGK YELSVLVDHA
VGASSIQDGQ IEVMLHRRLS ADDGRGVGEP LNEVVCVDQK CDGLVARATY YINVNKKGHG
AHWRRTYSQQ VYSPFLVAFA HEDERSWKSN NIAKASTVEG NYSLPDNVAI ITLQSLDDGT
TLLRLAHLFQ AQEDTQYSVM AKVELRKLFG KRIIKDLTET SLSANQKKSE MKKLNWRVTG
ESKTDPAPLK GGPVDSHALV VELGPMEIRT FLLKF
//
