ID   A8F3F3_PSELT            Unreviewed;      1020 AA.
AC   A8F3F3;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   04-NOV-2026, entry version 88.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:ABV32687.1};
DE            EC=3.2.1.24 {ECO:0000313|EMBL:ABV32687.1};
GN   OrderedLocusNames=Tlet_0117 {ECO:0000313|EMBL:ABV32687.1};
OS   Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS   TMO) (Thermotoga lettingae).
OC   Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
OC   Thermotogaceae; Pseudothermotoga.
OX   NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV32687.1, ECO:0000313|Proteomes:UP000002016};
RN   [1] {ECO:0000313|EMBL:ABV32687.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga lettingae TMO.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABV32687.1, ECO:0000313|Proteomes:UP000002016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC   {ECO:0000313|Proteomes:UP000002016};
RX   PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA   Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA   DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA   Noll K.M.;
RT   "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT   the Thermotogales.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; CP000812; ABV32687.1; -; Genomic_DNA.
DR   RefSeq; WP_012002168.1; NC_009828.1.
DR   AlphaFoldDB; A8F3F3; -.
DR   STRING; 416591.Tlet_0117; -.
DR   KEGG; tle:Tlet_0117; -.
DR   eggNOG; COG0383; Bacteria.
DR   HOGENOM; CLU_003442_1_0_0; -.
DR   OMA; AADWHFH; -.
DR   OrthoDB; 9772207at2; -.
DR   Proteomes; UP000002016; Chromosome.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IEA:TreeGrafter.
DR   CDD; cd10789; GH38N_AMII_ER_cytosolic; 1.
DR   FunFam; 3.20.110.10:FF:000002; alpha-mannosidase 2C1 isoform X1; 1.
DR   FunFam; 2.70.98.30:FF:000010; Cytosolic alpha-mannosidase; 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; 2.70.98.30; Golgi alpha-mannosidase II, domain 4; 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:ABV32687.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABV32687.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002016}.
FT   DOMAIN          523..596
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1020 AA;  119062 MW;  F419615C60952910 CRC64;
     MDKKFFYRLL KSISEILPYT ISEQRPLKAW YFTNGPIEEK PLDYEKTITF PFKWDFEKSP
     VWFMKDLEPV LLQENQRAYL KLWFGGESLI LVDGKPYGEI NEYHKLLNIT PLCDGKTHRV
     EAQVMPRGLF GKPQEPVFSE AFLLIIDEEI SEILKTVEIT VRAANILEEP VSKKLSDICD
     EFLSNVWVPR DTKTYLKTAQ QDIGVKGEIE SVWNTPKFEE FTGIKLQEEL KEQLINKYKV
     FKSKLEKLKR EHPPVGTIHL VGHSHIDYAW LWPVEETKRK IARTFANAVM LSKMFPEFVF
     SQSSAQIYQD LKEKYPELYE TVKQLVEQNK WEPVGGMWVE SDCNVPTIES LIRQFYYGQK
     FFEREFGKKS RVCWLPDVFG FSWVLPQILK QADIEYFVTT KLNWNDTTEF PYDLCIWRGI
     DGSEVLYCSF NNPNEGYNGR IDPDTVYKTW KNFRQKELTD KVLLSFGYGD GGGGPTEEML
     QNYRILKEFP DLPKLEIQSV EKYFESLELQ KNLPIWDDEL YLECHRGTYT SQSNIKKLHK
     DAEDALYFSE VVSVFCKHNY SDELDELWKI VLRNEFHDIL PGSSIKEVYQ DAERELSYVK
     EKATEIFEKA INSITKKNKS IISILNLSSF PKRCVFSLNE NLKLSLDREV VFSQKTFDGR
     YIYFVDRKIE PFSKIELKIS GADDEQPEQS LTKDNLSMEN EYLKISVKED GSVQVYDKEL
     GKFAFDKCGN ILKMHKNIPY YWDNWDIADG VEKTGFTLKA SKIMKIESGP IREIIRVEYE
     AEGSKIIQDY ILAKKSKRLD IKTKIDWHTR RALLRAYFPV NVLTRKAIFD ISGGFIERSS
     HKNTKYEQAR FEVPAHRWAD LSQTDFGVTI LNDGKYGYSV HQNTIALSLI KAGIFPDFFA
     DEGLHEFTYS VYTHHSEIKA IVEESEDLNK PLTVIKGELE IPHTILKITP NNFKVTCFRK
     NTQGNIVLRL VEIFGTSGKL SLEMPWHKGN ISLSDILEEK RQQVSFPMNY HPFKIYTLIL
//