ID   A0A1H8G9R8_9BACL        Unreviewed;       824 AA.
AC   A0A1H8G9R8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:SEN40510.1};
GN   ORFNames=SAMN05444955_110152 {ECO:0000313|EMBL:SEN40510.1};
OS   Lihuaxuella thermophila.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Lihuaxuella.
OX   NCBI_TaxID=1173111 {ECO:0000313|EMBL:SEN40510.1, ECO:0000313|Proteomes:UP000199695};
RN   [1] {ECO:0000313|EMBL:SEN40510.1, ECO:0000313|Proteomes:UP000199695}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46701 {ECO:0000313|EMBL:SEN40510.1,
RC   ECO:0000313|Proteomes:UP000199695};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOCQ01000010; SEN40510.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8G9R8; -.
DR   STRING; 1173111.SAMN05444955_110152; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000199695; 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; 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   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 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   InterPro; IPR013780; Glyco_hydro_b.
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:UP000199695}.
FT   DOMAIN          267..344
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   824 AA;  94632 MW;  1572EFD0AACFE47D CRC64;
     MKDKKLHMIG NAHLDPVWLW QWQEGFQETK ATFRSALDRM KEDDEFLFTS SSAANYEWIE
     KNEPEMFEEI KQRIAEGRWE IVGGWWVEPD CNLPGGESFV RQGLYGQRYF KEKFGVTAKV
     GYNVDSFGHH AMLPQILKKS GMDFYIFMRP NPQEKGLPGR LFWWESDDGS RVLTFRIPFE
     YCTWGKDIEK HVRRTAGELR PPFDELMCFY GVGNHGGGPT RENLASIRRL HADPRFPTLV
     FSTPNRFFAE ISKQDLPFPV VHDDLQHHAS GCYAAHSGIK KWNRQAENLL LAAEKFSILA
     NWTTGQPYPE DFDRAWKNVL FNQFHDILAG TSLEEAYEDA RNMYGEAMSI ASRGLNYAIQ
     SLSWRIGIEQ EEGMLPIVVF NPHSWNAKVN VEQEVNKLKP DAVLVDEKGN QVPVQTVQSH
     ATAGRNRICF IADLPPMGYR VYKIRLQKEK ESFPTVHADN HSLENDRYRI EIDPSTGFLT
     RLFDKEKKLD LLAGPAARPV VIEDKSDTWS HNVLRFDKEV GSFKAKKVYL AEHGPVKSVI
     RVVSEYGKST LIQDFTMYRE LNQIDVHVTV NWQEQFKVLK LKFPVNLIFR KSTYEIPYGH
     IVRENNGEEE PGQSWIDVSG THPETGELVG LSLLNDGKYS FDIHNKEMSL TVLRSPIYAH
     HDPAVPDEEG FYSFIDQGIQ RFTYSLLPHS GSWETAGTVK RAAELNQKPV TLIETYHEGP
     LPQIDSFLTV NQDNVIVTVL KKAEDSDALI VRCVETNHWA SSARIELPKW NRVIEADFKP
     CEIKTFLVPK NAEQPIVETN LLEWTDETDG EGIEEYGNPR LVNR
//