ID   A0A0N0NBZ9_9ACTN        Unreviewed;      1023 AA.
AC   A0A0N0NBZ9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KPI27799.1};
DE            EC=3.2.1.24 {ECO:0000313|EMBL:KPI27799.1};
GN   ORFNames=OV320_5847 {ECO:0000313|EMBL:KPI27799.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI27799.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI27799.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI27799.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI27799.1}.
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DR   EMBL; LJCX01000027; KPI27799.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0NBZ9; -.
DR   PATRIC; fig|1592329.3.peg.5148; -.
DR   Proteomes; UP000037870; Unassembled WGS sequence.
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   CDD; cd10789; GH38N_AMII_ER_cytosolic; 1.
DR   Gene3D; 2.60.40.2220; -; 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; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041147; GH38_C.
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   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 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   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KPI27799.1};
KW   Hydrolase {ECO:0000313|EMBL:KPI27799.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT   DOMAIN          519..598
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1023 AA;  112888 MW;  2327320BBDF61284 CRC64;
     MHDERRRIEE RVERVHNQRI KPAIYAASVP FEVEAWQAPG EPVPFAEAAA AAYEPFAMDT
     PGGPPWGTTW FRMRGQVPAE WAGKRVEAVI DLGFVGDWPG NQAEALVHRT DGTPLKAVNP
     LNHYVPIGNP VTGGESIDYL VEAASNPDIL ANDFAGPTLL GDVLTAGDRP LYTFRRADIA
     VLDEEVWHLD LDLQVLRELM VHLGEHEPRR HEIMHALDRA MDALDLDDVS GSAAAVREVL
     APVLASPAHA SAHTISGVGH AHIDSAWLWP IRETKRKTSR TFSNVTSLAE EYDDFIFACS
     QAQQYEWVRD NYPQVWARIQ ESVKKGQWAP VGGMWVESDG NLPGGEAIAR QLVHGKRFFI
     EHFGIETKGV WLPDSFGYNA AYPQLAKLAG NDWFLTQKIS WNQTNKFPHH TFWWEGIDGT
     RIFTHFPPVD TYNARFSGEE MDRAVRNYSE KGGGTRSLAP FGWGDGGGGP TREIMERARR
     LADLEGSPKV VVEHPDTFFA KARAEYQDAP VWVGELYLEL HRATYTTQAR TKQGNRRSEH
     KLREAELWAT TAALHAPGYA YPYAKLDRLW KTVLLHQFHD ILPGSSIAWV HREAEAEYAR
     VAEELEVLTA EAVAALGGGR QGGALRVFNT SPFRRAEVVR TPQGAPAYVE VPASGSAPLT
     GAQPPRPVTV SGRVLDNGLV RVQVAEDGTL SSVFDLRANR EVLADQGNLL RLHTDLPNYW
     DAWDIDKHYR NRYTDLLEPD AVTVVEEDPL VGAIRVTRSF GKGSTITQTI TLRAGSPRVD
     FETDIDWHEA EKILKAAFPV DVRAPHSSAE IQFGHIQRPT HTNTSWEAAR FEVSGHRWVH
     IGEPGYGVAV INDSTYGHDV SRTVREDGGT TTTVRLSLVR APRIPDPEAD QGRHRFSYAL
     LPGASIEDAV AEGYSLNLPL RVADAADTTP EPVVSVDGAG VTVEAVKLAD DESGDVVVRL
     YESSGGRSTG TLRTGFPLAG AQVTDLLERP LEPAAVGEDG TVAVVLRPFQ ILTLRLERAA
     TGR
//