ID   A0A0X3XNG8_9ACTN        Unreviewed;      1002 AA.
AC   A0A0X3XNG8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KUL73050.1};
GN   ORFNames=ADL34_20935 {ECO:0000313|EMBL:KUL73050.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL73050.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL73050.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL73050.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
RL   Submitted (OCT-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:KUL73050.1}.
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DR   EMBL; LLZN01000064; KUL73050.1; -; Genomic_DNA.
DR   RefSeq; WP_062670975.1; NZ_LLZN01000064.1.
DR   AlphaFoldDB; A0A0X3XNG8; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000052945; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:InterPro.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052945}.
FT   DOMAIN          519..597
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
FT   REGION          632..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1002 AA;  110913 MW;  D93FFD3FD023FFD8 CRC64;
     MHDDRTLVEA RLKRVLDERV RPAVYPESVP LDVAVWHAPD EPVPVAEGLA AIPEPIQVGA
     RWGAPWGTSW FRVSGTVPEA WAGRTVEALL DLGFDENMPG FQCEGLVYRP DGTPVKGLNP
     RNQWVRVAAP AEGGEEVRLH IEAASNPVIL DYHPFLPTRL GDKETAGSEP QYTLARMDLA
     VFDEEVWQLV VDLEVLGELM AELPVESARR WDLLRAVERA LDALDLQDVN GTAAAARARL
     TDVLAAPAVP SAHRVSAVGH AHIDSAWLWP LRETVRKVAR TTSNMTALVE DEPDFVFAMS
     QAQQWAWVKE HRPEVWARVK KAVAEGRFVP AGGMWVESDT NMPGSEAMAR QFVHGKRFFL
     DEFGIENDEA WLPDTFGFAA GLPQIIKAAG SKWLLTQKIS WSQTNKFPHH TFWWEGIDGT
     RIFTHFPPVD TYNCSMKGAE IAHAARNFKD KGRARRSLAP TGWGDGGGGT TREMIAKAAR
     MRDLEGSATV VWETPDAFFR KAEAEYPDAP VWVGELYLEL HRATLTSQAG TKQGNRRSEH
     LLREAELWAA TAAVRTGFPY PYEELDRIWK TVLLHQFHDI LPGSSIAWVH REARATYARL
     AGDLEAIVDA AQRALAGEGT TELVFNAAPH PRAGVPAGGA RPPVSEDRTA LTPRPDGGYV
     LDNGLLRVEI DARGLVVSAY DVEADRETVA PGGAAGLLQL HPDFPNMWDA WDVDAFYRHT
     VTDLTDVDEI TAGDGEVRIV RSFGDSRVTQ RLSLAPGERR VLFDTEVDWH ETEKFLKLAF
     PLDVHAERYA SETQFGHFHR PTHTNTSWEA AKFEACNHRF VHVEEPGWGA AVVNDSTYGH
     DVTRTVRTDG DLGTTTTVRV SLLRAPRFPD PETDQGVHRF RHALVPGAGI GDAVREGWRI
     NLPERRLAGA REVAPLVTVD RDAVVVTAVK LADDGSGDVV VRLHEAHGGR VRATLTAGFE
     VADVTATDLL ERPLPETPEH TGREVALRLR PFELVTLRLR RG
//