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Database: UniProt
Entry: F8X2H5_9BACT
LinkDB: F8X2H5_9BACT
Original site: F8X2H5_9BACT 
ID   F8X2H5_9BACT            Unreviewed;       665 AA.
AC   F8X2H5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Alpha-glucosidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF9456_02575 {ECO:0000313|EMBL:EGK05773.1};
OS   Dysgonomonas mossii DSM 22836.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Dysgonomonas.
OX   NCBI_TaxID=742767 {ECO:0000313|EMBL:EGK05773.1, ECO:0000313|Proteomes:UP000006420};
RN   [1] {ECO:0000313|EMBL:EGK05773.1, ECO:0000313|Proteomes:UP000006420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22836 {ECO:0000313|EMBL:EGK05773.1,
RC   ECO:0000313|Proteomes:UP000006420};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Pudlo N., Martens E.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Dysgonomonas mossii DSM 22836.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:EGK05773.1}.
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DR   EMBL; ADLW01000013; EGK05773.1; -; Genomic_DNA.
DR   RefSeq; WP_006843940.1; NZ_GL892008.1.
DR   AlphaFoldDB; F8X2H5; -.
DR   STRING; 742767.HMPREF9456_02575; -.
DR   GeneID; 78083201; -.
DR   eggNOG; COG4948; Bacteria.
DR   HOGENOM; CLU_011166_0_0_10; -.
DR   OrthoDB; 1109141at2; -.
DR   Proteomes; UP000006420; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR029483; GH97_C.
DR   InterPro; IPR019563; GH97_catalytic.
DR   InterPro; IPR029486; GH97_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35803; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB-RELATED; 1.
DR   PANTHER; PTHR35803:SF2; RETAINING ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF14509; GH97_C; 1.
DR   Pfam; PF14508; GH97_N; 1.
DR   Pfam; PF10566; Glyco_hydro_97; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006420};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..665
FT                   /note="Alpha-glucosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003386048"
FT   DOMAIN          29..297
FT                   /note="Glycosyl-hydrolase 97 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14508"
FT   DOMAIN          301..565
FT                   /note="Glycosyl-hydrolase 97 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF10566"
FT   DOMAIN          567..662
FT                   /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14509"
SQ   SEQUENCE   665 AA;  75277 MW;  DF1E148D029BCF13 CRC64;
     MKKNYLIILA VFCTALFSMT VSAQKLFNLK SPNGKLEAVI NVGKTVDYSV LHNGDLMLDK
     STISMSLSDG TFYGKDAKLS GSSTKTVNQT ISAQVYKRKQ IKDNYNELTL KFKDHSILFR
     AYDDGIAYRF VSASKKPFAV QGEQVEFNFP ADSKAFINYT NKQESATFDE QFFNSFEQPY
     VHNLLSEWNK KRLAISPLVV EGVKSKKVCI VEADLLNYPG MFLYPGDKAN ILKGIFAPYP
     KDVEQGGHNN LQMVVKSREN FLAKFDGATN FPWRVVIVSE KDSDLADSDM VYKLATPSQG
     DYSWVKPGKV AWDWWNDWNL YNVDFKTGVN NQTYKYYIDF ASKYGIEYVI LDEGWAVNLK
     ADLFQVVPEI NLPELVAYAK SKNVGLILWA GFHAFDRDME AVCKHYSEMG IKGFKVDFMD
     RDDQVVVDFH RRGAETAAKY KMMLDYHGTY KPTGLQRTYP NVINFEGVNG LEQMKWAENL
     DQVTYDVTIP FIRQVAGPMD YTQGAMRNAT KGNYRSVNNE AMSQGTRCRQ LAEYVIFESP
     LNMLCDSPSN YMAEQECTEF IAAVPTVWDN TVALNGEIAK YVAIARQKGD AWYVGALTNW
     DARTMELDLS FLGEGNFKGE VFKDGVNADR VAKDYKKEII DIPADRKLPI SMAPGGGYVV
     KITKK
//
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