ID   A0A1I7I0S3_9FLAO        Unreviewed;       668 AA.
AC   A0A1I7I0S3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:SFU66559.1};
GN   ORFNames=SAMN05216480_11243 {ECO:0000313|EMBL:SFU66559.1};
OS   Pustulibacterium marinum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pustulibacterium.
OX   NCBI_TaxID=1224947 {ECO:0000313|EMBL:SFU66559.1, ECO:0000313|Proteomes:UP000199138};
RN   [1] {ECO:0000313|EMBL:SFU66559.1, ECO:0000313|Proteomes:UP000199138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12333 {ECO:0000313|EMBL:SFU66559.1,
RC   ECO:0000313|Proteomes:UP000199138};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; FPBK01000012; SFU66559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7I0S3; -.
DR   STRING; 1224947.SAMN05216480_11243; -.
DR   OrthoDB; 57532at2; -.
DR   Proteomes; UP000199138; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 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   PANTHER; PTHR35803:SF1; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB; 1.
DR   PANTHER; PTHR35803; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB-RELATED; 1.
DR   Pfam; PF14509; GH97_C; 1.
DR   Pfam; PF14508; GH97_N; 1.
DR   Pfam; PF10566; Glyco_hydro_97; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199138};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..668
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011465385"
FT   DOMAIN          30..277
FT                   /note="Glycosyl-hydrolase 97 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14508"
FT   DOMAIN          282..564
FT                   /note="Glycosyl-hydrolase 97 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF10566"
FT   DOMAIN          566..666
FT                   /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14509"
SQ   SEQUENCE   668 AA;  76389 MW;  8ADF0B468FC7C035 CRC64;
     MIKKSLVIST LALAIVSCSQ ETTQEKTFTV ASPEGANAIT FSLENNFPTY SVKHGETSVI
     TPSKLGFVFK DQDSIASNLE IIDTEESSFD ETWEQVWGEK HNIRNHYNQL TVHLQEKTEK
     KRKLDIEFRA FDDGIAFRYV FPKQGVNDSI IIMNELTEFN LKDDGDSWWI PAYKSNRYEH
     LFTQTKVSAI DTVHTPYTIK SDDGLYLSFH EADLKNYASY TIAKKEGTKL DLDLMPWHDG
     VKVRTTESFQ TPWRTLQIGQ KPGDLVESYL ILNLNEPNKL EDLSYIETYK YTGMWWGMHI
     SKYTFWEGPK HGASTENCIQ DIKETNELGI HHMLIEGWNK GWTPAWYENK MHEFSFTEPT
     DDFDYQTVVD FANKNDVKII GYHETGSNII NYKKQIDAGM QLYKDLGIHD VKIGQVGDKL
     NMKEWHGSQF GVEYYRWVLE KAAEYQLTVN FHEPIKDTGE RRTYPNMMAR EGARGQEYNA
     WSEGNPPNHT VLLPFTRMLA GPMDFTPGVL DIMETKGFNN RRINSTAAKQ LALYVVIYSP
     IQMLADLPEN YIGHPAFQFL ADVPTDWEDT KVLNAEIGEY VTTVRKDLNS DDWYLGSITN
     KKARDFELDL SFLGEGTYEA QMYTDAEGTD IDNNPAAVGI SKKEVKATDK LPLHLGAGGG
     AAIRFKKL
//