ID A0A1U7ZD79_NELNU Unreviewed; 1017 AA.
AC A0A1U7ZD79;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN Name=LOC104591859 {ECO:0000313|RefSeq:XP_010249229.1};
GN ORFNames=HUJ06_009263 {ECO:0000313|EMBL:DAD30412.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010249229.1};
RN [1] {ECO:0000313|EMBL:DAD30412.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD30412.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010249229.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 EMBL; DUZY01000003; DAD30412.1; -; Genomic_DNA.
DR RefSeq; XP_010249229.1; XM_010250927.2.
DR STRING; 4432.A0A1U7ZD79; -.
DR GeneID; 104591859; -.
DR KEGG; nnu:104591859; -.
DR eggNOG; KOG1959; Eukaryota.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
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:SF60; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Signal {ECO:0000256|RuleBase:RU361199};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 21..1017
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5041474553"
FT DOMAIN 353..427
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 1017 AA; 114526 MW; FE517FA0707F3BD2 CRC64;
MEIGLCSFLV LLASFFCAES KYIAYNTSQR VVPGKLNVHL VPHSHDDVGW LKTVDQYYVG
ANNSIRGACV QNILDSVVSA LLADKNRKFI YVEQAFFQRW WRQQSEAVQS IVRQLVNAGQ
LEFINGGMCM HDEATPHYID MIDQTTLGHR FIKQEFDQIP RVGWQIDPFG HSAVQAYLLG
AELGFDSLFF ARIDYQDRAK RKDEKNLEVV WRGSKSLGSS SQIFTGIFPK HYDTPIGFAF
EFNDDSPPVQ DDVLLFDYNV QERVDDFVNA AIQQANMTRT NHIMWTMGTD FRYQYANTWF
KQMDKLIHYV NKDGRVNALY STPSIYTDAK HEANESWPIK IDDFFPYADR PNAYWTGYFT
SRPAFKRYVR MMSGYYLAAR QLEFFKGRSS SGSHTNTLAD ALAIAQHHDA VSGTQRQHVA
DDYAQRLSIG YIEAEELVAS SLACLAEPSS STGCQNPTTK FQQCPLLNIS YCPPSEIDLS
QGRSLVVVVY NPLGWKREDI VRIPVSSEAV TVRDSSGRET ESQLLPLANA SASIRSYYVK
AYLGKSPGSA PKNSLVFLAS VPPLGFSTYF VSDAKKTGAS STRSTVYTTQ GNEDGTIEVG
QGNLRLIYSL KEGKLIQYVN TRSLVKTSIE QSYIFYSGYG GSDKDPQASG AYIFRPNGTF
SSASEGQAPL TILRGPIVDE VHQQINPWIY QTTRVYKERD HAEVEFIVGP IPVDDGIGKE
IATQITTTMN SNKTFYTDSN GRDFIKRIHD YRTDWELQVD QPVAGNYYPI NLGIYIEDNQ
TELSVLVDRS VGGSSIVDGQ IELMLHRRLI HDDSRGVGEV LDEKVCVLNE CTGLTIQGRF
YLRIDPLGEG SKWRRSVGQE IYSPFLLAFT EQDAGNWTSS HVSTFSAMDP SYSLPDNVAI
ITLQELEDGN VLLRLAHLYE IGEDKDLSVM ARVELKKLFA DKKISKITEM SLSSNQERAE
MEKKKLVWKV DAPQEEAKVV RGGPVDPVRL VVELGPMEIR TFIINFKYIF LVNTVDG
//
