ID   C0CX09_9FIRM            Unreviewed;       888 AA.
AC   C0CX09;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Alpha-mannosidase MngB {ECO:0000313|EMBL:EEG56381.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:EEG56381.1};
GN   Name=mngB {ECO:0000313|EMBL:EEG56381.1};
GN   ORFNames=CLOSTASPAR_01530 {ECO:0000313|EMBL:EEG56381.1};
OS   [Clostridium] asparagiforme DSM 15981.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Enterocloster.
OX   NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG56381.1, ECO:0000313|Proteomes:UP000004756};
RN   [1] {ECO:0000313|EMBL:EEG56381.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56381.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG56381.1, ECO:0000313|Proteomes:UP000004756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG56381.1,
RC   ECO:0000313|Proteomes:UP000004756};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL   Submitted (FEB-2009) 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:EEG56381.1}.
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DR   EMBL; ACCJ01000072; EEG56381.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0CX09; -.
DR   HOGENOM; CLU_003442_2_1_9; -.
DR   Proteomes; UP000004756; 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; cd10815; GH38N_AMII_EcMngB_like; 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:SF2; MANNOSYLGLYCERATE HYDROLASE; 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:EEG56381.1};
KW   Hydrolase {ECO:0000313|EMBL:EEG56381.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          276..354
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   888 AA;  100935 MW;  85A9CD440F806636 CRC64;
     MADKVHVVPH FHWDREWYFT AEESKILLVN DMEEVLTMLE TREDYPYFVL DGQTSVLEDY
     FSVSPENRER VRELVQRGKL IIGPWYTQTD EMVVGGESIV RNLLYGMKDC REFGSPMMIG
     YLPDSFGQSA RMPQILRGFN IENSMFWRGT SERMGTDKTE FFWEDDDGSR VAVQLLPLGY
     AIGKYLPVEK EALRKRMEKY MPVLERGTAT GHLLVPNGHD QMPLQNDIFQ VMETMRELYP
     DKQFFLSRYE DVFAAIGRQG NLDTLRGEFL DGRYMRVHRS IFSSRADLKA ANTRIENKVT
     NLLEPLASIA YKLGFPYHHG LLEAIWKELM KNHAHDSIGC CCSDKVHRAI ADRYFLAEER
     ADRLIEFYMR KIVDAMDCSR ALDKLTVFNL LPYEREGMIR GKIVTKMKRF ALERADGSRL
     KYEITDRRIV DAGLIDRQIV HYGDYEPFVE YTLEFCDRIP AMGFTTYLVR EAEALAGESP
     AVSMAAGTGE NPAVEPADLG GNCRLASPAA NTLENEYLSV TVEPNGSLTV LDQQKGQCYR
     DVLLLEDGSD DGDGYDYSPA ANDWVLTSKE ETADIRCQHG TYSHKARVRV SMAVPAGLES
     RSERRRDGRV DVEFELELKA GSPVLEVRVT VDNQADSHRL RLLVPGQENE GFSVSDNQFG
     RIRRPVRDEA MDVWEKEGWS ERPDSIYPFL SWVSGCGERG LAVLTNSVRE YEMTGPDYGV
     LAVTLFRSVG VLGKEGLLRR PGRPSGIKME TPDSQLRGRR TYEIALTACR DHLARTAKEY
     VTPFISYNKM PYNAMKLNPS EVKVPYAFSL LSETEGRVVL SALKKAEDED KLIARFYNGC
     GEKAPMRLKD GNGDLTVDVV KLNETDVLSG HVTGDQWVGY NQIVTCKF
//