ID   A0A369BA59_9BACL        Unreviewed;      1038 AA.
AC   A0A369BA59;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:RCX18195.1};
GN   ORFNames=DFP94_107150 {ECO:0000313|EMBL:RCX18195.1};
OS   Fontibacillus phaseoli.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Fontibacillus.
OX   NCBI_TaxID=1416533 {ECO:0000313|EMBL:RCX18195.1, ECO:0000313|Proteomes:UP000253090};
RN   [1] {ECO:0000313|EMBL:RCX18195.1, ECO:0000313|Proteomes:UP000253090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8333 {ECO:0000313|EMBL:RCX18195.1,
RC   ECO:0000313|Proteomes:UP000253090};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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:RCX18195.1}.
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; QPJW01000007; RCX18195.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369BA59; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000253090; 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:UP000253090}.
FT   DOMAIN          495..576
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1038 AA;  117665 MW;  21628E97601EE600 CRC64;
     MERIKRFIRE LSDVQWLEQI ELREWEITTS VYQVPGKYTE EDNYPEGQHL ERFPSEQGTT
     YFFRMTLAVP EAWRNGHIGL VFASGGEGLL RIGGKSYQGL DRNHTFVTLP VGPGNRPLEM
     EIELFDPIPE PVDPLNRQAV IQPPILSINS RLVLVNRSVQ SLMYTATVIR DSAVLLPEQD
     FRRTRLIEAL HAAMDEFVAL DLAAITEGQA ILELEQRLRE RVKSIGGPAE GLIHMVGQSH
     IDIAWLWPAR ETVRKASRTF STVDALMREY PEYRYAQSQP QLFAYLKEND PELYERVKQR
     IKEGRWELVG GMWVEPDLNL PSGESLMRQM LYGQRFYQEE FGMTSEIEWL PDTFGYCASL
     PQILRHGGVR YFMTTKLGWN DTNVFPYDLF HWVGIDGTPM LSYLNHGVNE NTLPKDIHDH
     WQSYREKAAH PEQMLLYGHG DGGGGVTREM LEYNDRAELM VGQPASEYST AAAFFAGIDA
     AQPELPAWHG DLYLELHRGT YTTHGRNKRN NRKAEILYRE AEVWNTLAAP GMPEERAGEI
     RQAMHEGWKL ILLNQFHDII PGSAITETYG TSEEEYREIF GKGNAGLSQG LESLAGQVAT
     EGEGKPYIVF NSLGWSRDAA VPIRDHGLSG TLGAYDENGK RLILDNASGV HGEDNVIRVH
     VPGIPAFGYK TIWLRSEDAL NAELDHAVHG KTFAGEWETE YYRLKFNERG EIVSLWDKEA
     GREVVKAGEA ANRFHFFHDR PTLWDAWDID SRYERQPAGQ AKLLESRVVA NGAVQDVLRF
     RWSIGQSEIT QDLILYHHDR RIDFETKVSW NEAHKLLKVG FPIDVVTDKA TYEIPFGALE
     RVTHRNTSWE QAQYEVCGHR FVDVSERGYG VSLLNDCKYG YDVQGSTIRL SLLRAPKWPD
     VTADLGDHEF TYSLYPHAGD WQSAHTVRAA AELNLDPAVV AAEAREGSLP PVHSLIGFTG
     EHVVLDTVKP AEDGSGVILR FYESSGGRET VELDWSRTYS GAFLSDALER EIEPLNAAAG
     PIKLDFAPYE IKTLKINK
//