ID A0A059AHE5_EUCGR Unreviewed; 991 AA.
AC A0A059AHE5;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=EUGRSUZ_J02460 {ECO:0000313|EMBL:KCW53184.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW53184.1};
RN [1] {ECO:0000313|EMBL:KCW53184.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW53184.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) 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; KK198762; KCW53184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059AHE5; -.
DR EnsemblPlants; KCW53184; KCW53184; EUGRSUZ_J02460.
DR Gramene; KCW53184; KCW53184; EUGRSUZ_J02460.
DR eggNOG; KOG1959; Eukaryota.
DR InParanoid; A0A059AHE5; -.
DR OMA; GANNTIA; -.
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: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};
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..25
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT CHAIN 26..991
FT /note="Alpha-mannosidase"
FT /evidence="ECO:0000256|RuleBase:RU361199"
FT /id="PRO_5017846459"
FT DOMAIN 360..434
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
SQ SEQUENCE 991 AA; 110874 MW; 007FD6CEC007B887 CRC64;
MGTLVASCFV IVILEVAWLY GGVDGAYVKY NTVAGVVEGK LNVHLVPHSH DDVGWLKTID
QYYVGSNNSI QGACIENVLD SVIKALARDP NRKFVFAEMA FFQRWWLEQS PETQEQVRKL
VNAGQFEFIN GGWCMHDEAT THYIDMIDQT TLGHGLIKSQ FNKVPRVGWQ IDPFGHSADL
LGAEIGFDSM HFARIDYQYR ANRKNDKSLE VIWRGSKTFG SSSQIFANAF PVHYSPPEGF
NFEVSNDFEP VQIFKLQDNN LLYDYNVEKR VNDFIGAAMT QANVTRTNHI MWTMGDDFVY
QYAESWFKQM DKFIHYVNKD GRVNALYSTP SIYMDAKNAA NVSWPLKTDD YLPYADRKDA
HWTGFFTNRP ALKGYVRMLS GYYLAARQLE FLVGRRSSGP STYRLGDALG LVQHHDALTG
TAKQHTTNDY EKGLAIGASE AEAVVDDALS CLVSKKPGGQ CSLPVLNFSQ CPLLNISFCP
ATEEDIPDGK SLVTNSNFVI RDSSGHTVEA QLIDLDNVTI NLRNFYVKAY LGLSPQQIPK
YWLVFQVSLP PLGWNTYFIS KAATEGESKT SFLSTLGDPQ NDTIEVGPGD LKMLFSSTSG
QLVRMFNSKT GVDVPVQQSY LYYSSSIGGT DDSPASNLYI FRPNGAHPTI VSRKVPLKVV
RGPLVDEVHQ QFSSWIYQVT RLHKDKEHAD VEFTIGPIPT DDGVGKEVIT QMTANMATEK
TFYTDSNGRD FIKRVRDYRP DWSLTVTQPV SGNYYPINLG IFTMDNKTEF SVLVDRAAGG
ASIEDGQIEL MLHRKIPYNT GVVGPPNETV CISNSTCKGL TVRGHYYIGI NKPGTGARWR
RTIGQEVYSP LVLAFAHEKM EEWTGSYVTS GTAMDSSYSL PQNVALITLQ ELDDGSALLR
LAHLYEVGED AEYSTLAKVE LKRMFAGRTI REVKEMSLSA NQEKSEMKRM TWKVEGEAAA
EPTPLRGGPV DVLDLIVELG PMEIRTFLLK F
//