ID   B1BSS1_CLOPF            Unreviewed;      1044 AA.
AC   B1BSS1;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Putative alpha-mannosidase {ECO:0000313|EMBL:EDT15325.1};
GN   ORFNames=AC3_2668 {ECO:0000313|EMBL:EDT15325.1};
OS   Clostridium perfringens E str. JGS1987.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=451755 {ECO:0000313|EMBL:EDT15325.1, ECO:0000313|Proteomes:UP000005337};
RN   [1] {ECO:0000313|EMBL:EDT15325.1, ECO:0000313|Proteomes:UP000005337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E str. JGS1987 {ECO:0000313|Proteomes:UP000005337};
RA   Paulsen I., Sebastian Y.;
RT   "Annotation of Clostridium perfringens E str. JGS1987.";
RL   Submitted (JUL-2007) 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:EDT15325.1}.
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DR   EMBL; ABDW01000011; EDT15325.1; -; Genomic_DNA.
DR   RefSeq; WP_003463203.1; NZ_ABDW01000011.1.
DR   AlphaFoldDB; B1BSS1; -.
DR   Proteomes; UP000005337; 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}.
FT   DOMAIN          516..593
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1044 AA;  121234 MW;  BF0ADDFED8569519 CRC64;
     MRFISERIRK TYEEIGRYVY SNTLNIDNYK FIAGNYDNID EIKNAPEEGW IDFKTGDLWG
     EESHGWFKTS VKVPEEFAGQ TIALSFHTFL GDWDNTTNPQ FILYVNGEHI QGLDVNHQET
     ILTHNAVAGE VYDIDLHAHI GRIEGKKSTL HGKLVTIDEE ARKLYFNLSV PHIVATKLHE
     EDKRRIDMLT VLNDTINLID LRRPFTKEYN ESLKIANKYI EENFYDKMCG HEDMVATCVG
     HTHIDVAWLW TVAQTREKVA RSFSTVLKLM EEYPEYIFMS SQPQLYKFLK EDHPKVYEKV
     KEKVREGVWE PEGAMWLEAD CNVTSGESLI RQILHGKRFF KEEFNVDNEI LWLPDVFGYS
     AALPQILKKS DVNYFMTTKI SWNQINKMPY DTFMWKGIDG TEILTHFITT TYPDQDPFKE
     TMTTYCGNIH PGSIMGAWNR YQQKNINNDV LVAFGFGDGG GGATYEMLEN GKRLSRGIPG
     APKVKIGKAK DYFKKLEDTV KDNNKLPKWV GELYLEYHRG TYTSMGRNKR DNRVCENLYT
     SAEKFNSMAM LLGKNYPLAD LNAAWETILL NQFHDILPGS SIKEVYDVTK EEYKDLIEKG
     NNFVGSALDN ITSEINLKER SVVVFNSLGF ERDDIATFDV PEDIENPAVL DGEEEIICQR
     IEDGEKAIFF AKGIPANGYK SFKIIESTNK EVENVSLNEK EAENDFLRIK FNEEGNIVSL
     FDKRAEREVL KEGTLGNRIQ AFEDKPMEYS NWDIDIYYKE KMWNVDDVQS IEVVEEGPVR
     STLRIERKFL ESTIVQNIYV YKDLDRIDFN SYVDWKEHEV LLKTSFPIDL NATEATYEIQ
     YGNVKRPTHS NTSWDEARFE VCGQKWADLS EGDFGVSLLN NCKYGHDIQD GDMRLTLLKS
     GTHPWTETDQ EEHFFTYSIY PHMGTWKEAH TVQKAYELNQ PLYTKVCEKH EGILEDTLGL
     VKVNKDNIMI EVIKKAEDTD HLIIRMYEFF NSRTKSTLEF SREIEEAFEC NLMERNLEEA
     KFEGEKIEFT INPFEIKTFK VKLK
//