ID   B7LKM6_ESCF3            Unreviewed;       877 AA.
AC   B7LKM6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:CAQ89871.1};
GN   Name=mngB {ECO:0000313|EMBL:CAQ89871.1};
GN   OrderedLocusNames=EFER_2372 {ECO:0000313|EMBL:CAQ89871.1};
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ89871.1, ECO:0000313|Proteomes:UP000000745};
RN   [1] {ECO:0000313|Proteomes:UP000000745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC   JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC   {ECO:0000313|Proteomes:UP000000745};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; CU928158; CAQ89871.1; -; Genomic_DNA.
DR   RefSeq; WP_000648952.1; NC_011740.1.
DR   AlphaFoldDB; B7LKM6; -.
DR   CAZy; GH38; Glycoside Hydrolase Family 38.
DR   GeneID; 75056593; -.
DR   KEGG; efe:EFER_2372; -.
DR   HOGENOM; CLU_003442_2_1_6; -.
DR   OrthoDB; 9764050at2; -.
DR   Proteomes; UP000000745; Chromosome.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          279..357
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   877 AA;  99995 MW;  988D06FFF4C233FB CRC64;
     MKAVSRVHIT PHMHWDREWY FTTEESRILL VNNMEEILCR LEQDNEYKYY VLDGQTAILE
     DYFAVKPENK DRVKKLVEAG KLIIGPWYTQ TDTTIVSAES IVRNLMYGMR DCLAFGEPMK
     IGYLPDSFGM SGQLPHIYNG FGITRTMFWR GCSERHGTDK TEFLWKSSDG SEVTAQVLPL
     GYAIGKYLPA DEDGLRKRLD SYFDVLEKAS VTKEILLPNG HDQMPLQQNI FEVMDKLREI
     YPQRKFVMSR FEEVFEKIEA QRENLATLKG EFIDGKYMRV HRTIGSTRMD IKIAHARIEN
     KIVNLLEPLA TLAWTLGFEY HHGLLEKMWK EILKNHAHDS IGCCCSDKVH REIVARFELA
     EDMADNLIRF YMRKIADNMP QSDADKLVLF NLMPWPREEV INTTVRLRAS QFNLRDDRGQ
     PVPYFIRHAR EIDPGLIDRQ IVHYGNYDPF MEFDIQINQI VPSMGYRTLY IEANQPGNVV
     TSKSEVEGIL ENAFWQIALN EDGSLQLVDK DSGVRFERVL QIEESSDDGD EYDYSPAKEE
     WVITSANAKP QCEITHEAWQ STAVIRYDMA VPLNLSERSA RQSTGRVGVE LVVTLSHNSR
     RIDVDINLDN QADDHRLRIL VPTPFNTDSV LADTQFGSLT RPVSDSAMDV WQQEGWKEAP
     VPVWNMLSYA ALQEERNGLA VFSEGLREFE VIGEKNKSFA ITLLRGVGLL GKEDLLLRPG
     RPSGIKMPVP DSQLRGLLSC RLSLLSYTGT PTAAGVAQQA RAWLTPVQCY NKIPWDAMKL
     NKAGFNVPES YSLLKMPPVG CLISALKKAE DRQEVILRLF NPAESATCDA TVAFSREVIS
     CSETMMDEHI TTEENQGSNL SGPFLPGQSR TFSYRLA
//