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Database: UniProt
Entry: I1N814_SOYBN
LinkDB: I1N814_SOYBN
Original site: I1N814_SOYBN 
ID   I1N814_SOYBN            Unreviewed;      1024 AA.
AC   I1N814;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE            EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN   Name=100795651 {ECO:0000313|EnsemblPlants:KRG94704};
GN   ORFNames=GLYMA_19G103200 {ECO:0000313|EMBL:KRG94704.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EMBL:KRG94704.1};
RN   [1] {ECO:0000313|EMBL:KRG94704.1, ECO:0000313|EnsemblPlants:KRG94704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRG94704};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG94704.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRG94704}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRG94704};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRG94704.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRG94704.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) 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; CM000852; KRG94704.1; -; Genomic_DNA.
DR   RefSeq; XP_003553307.2; XM_003553259.3.
DR   AlphaFoldDB; I1N814; -.
DR   SMR; I1N814; -.
DR   STRING; 3847.I1N814; -.
DR   PaxDb; 3847-GLYMA19G27660-1; -.
DR   EnsemblPlants; KRG94704; KRG94704; GLYMA_19G103200.
DR   GeneID; 100795651; -.
DR   Gramene; KRG94704; KRG94704; GLYMA_19G103200.
DR   KEGG; gmx:100795651; -.
DR   eggNOG; KOG1959; Eukaryota.
DR   InParanoid; I1N814; -.
DR   OrthoDB; 5474711at2759; -.
DR   Proteomes; UP000008827; Chromosome 19.
DR   ExpressionAtlas; I1N814; 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: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:UP000008827};
KW   Signal {ECO:0000256|RuleBase:RU361199};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT   CHAIN           23..1024
FT                   /note="Alpha-mannosidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361199"
FT                   /id="PRO_5014579342"
FT   DOMAIN          355..429
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1024 AA;  115731 MW;  CB90C6430A500330 CRC64;
     MMVNAVAVVF AVLVAAIWVA ESEYIEYNTT QRIVPDKLNV HLVPHSHDDV GWLKTVDQYY
     VGANNSIRGA CVQNVLDSVI SALLEDKNRK FIYVEMAFFQ RWWRQQSKAT KIKVKELVNS
     GQLEFINGGM CMHDEATPHY IDLIDQTTLG HQFIKEEFDK VPRVGWQIDP FGHSAVQAYL
     LGAELGFDSH FFARIDYQDR AKRLKEKTLE VIWQGSRSLG SSSQIFTGIF PRHYDPPDGF
     TFEINDVSPP IQDDILLFDY NVQERVNDFV SAALAQANVT KTNHIMWAMG TDFRYQYANS
     WFRQMDKFIH YVNQDGRVNA LYSTPSIYTD AKYAADEYWP LKVDDFFPYA DHPNAYWTGY
     FTSRPALKGY VRFMSAYYQA ARQLEYFKGR NETGPNTDAL ADALAIAQHH DAVSGTERQH
     VASDYALRLS MGYEEAERLV ASALASLVNQ RLSSYGVNPV TDIQQCPLLN ISYCPPAEAT
     LINGKSLVIV VYNPLAWKRE DVIRIPVSTG QVFVQDFSGN KIESQILPLS NATLTMRKHY
     VRAYIGKAPG GDTLKSWLAF PVSVPPLGFS TYIVSSSKQS SHSSTISKIY ISEGSTNKSI
     EVGKGNLKLL YSENEGRLTH YVNSRTLVTT SVEQSYSYYS GNDGTDKDPQ ASGAYVFRPN
     GSFSIKSDHQ ASFTVLRGPI LDEVHQQLNP WVSQITRIFK AKEHAEIEFT VGPIPVDDDI
     GKEIITQFKT TMKTNKTFYT DSNGRDFIKR IRDFRTDWDL QVNQPIAGNY YPVNLGIYVQ
     DSSMELSVLV DRSVGGSSLE DGQVELMLHR RLLHDDARGV GEVLNETVCV ADKCEGLTIQ
     GKLYLRIDHK GEAAKWRRTV GQELYSPLLL AFTEQDGDNW LHFSPSTFSG IDSSYSLPDN
     TALLTLQEFK NGKVLLRLAH LYEIGEDKNY SLTASVELKK LFPNKKINKV TEMSLSANQE
     RAQMEKRKLD WKVEGSTEEP KVVRGGPVDP TKLVVELAPM EIRTFFIEFD PLQTVPVPEN
     HVAM
//
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