ID   A0A126PEM5_9BACT        Unreviewed;       702 AA.
AC   A0A126PEM5;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:AMJ67469.1};
GN   ORFNames=AXW84_20130 {ECO:0000313|EMBL:AMJ67469.1};
OS   Hymenobacter sp. PAMC 26628.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ67469.1, ECO:0000313|Proteomes:UP000059956};
RN   [1] {ECO:0000313|EMBL:AMJ67469.1, ECO:0000313|Proteomes:UP000059956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ67469.1,
RC   ECO:0000313|Proteomes:UP000059956};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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; CP014304; AMJ67469.1; -; Genomic_DNA.
DR   RefSeq; WP_068237544.1; NZ_CP014304.1.
DR   AlphaFoldDB; A0A126PEM5; -.
DR   STRING; 1484118.AXW84_20130; -.
DR   KEGG; hyz:AXW84_20130; -.
DR   OrthoDB; 57532at2; -.
DR   Proteomes; UP000059956; Chromosome.
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   InterPro; IPR017853; Glycoside_hydrolase_SF.
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   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059956};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..702
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007271761"
FT   DOMAIN          30..292
FT                   /note="Glycosyl-hydrolase 97 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14508"
FT   DOMAIN          297..595
FT                   /note="Glycosyl-hydrolase 97 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF10566"
FT   DOMAIN          597..697
FT                   /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14509"
SQ   SEQUENCE   702 AA;  78012 MW;  556F48EFF2291082 CRC64;
     MKKYLFLLLL AAGAPAAAQP AGPLAASLGS VKLAFALNAA GQPTYSVAYG QKPVVNASRL
     GIALADGPGF DGPLVLLGSE RKDADDTWQP VWGEVKDIRD HYQQLTVHLR QAAAPGRRLD
     VVFRVFADGV GFRYEFPRQL ALGNFVVSDE LTEFALPADH QAFWIPGDYD TNEYYYTHSR
     LSAVDGAPQV KASTEIAVRE APDPQAVATP LMLKADDGLY VNIHEAAQVD YPALQLHVDR
     ASHRLTARLV PDAVGNKAFL HAPCRTPWRT IIVSDRAPDI LASKLILNLN EPSKIADTGW
     IKPMKFVGVW WEMQIGRTDW KYANSADTLD ARGQLIPTGR HGANTANVKR YIDFAARHGI
     AGVLVEGWNV GWEDWFGNWK ENVFDFVTPY PDFDVQQISR YAKAKGVQMI MHNETSGAAT
     NYEQHFDTAY QFMNKYGYPA VKTGYVGRII PRGEHHDGQW MSNHFVRVAK AAARYRVVVD
     MHEAVRPTGL SRTYPNWMAS EAGRGNEYNA FSTGSPPDHE TIMPFTRLMG GPMDYTPGIF
     KLKNYEPTGK RQVRTTLAKQ LALYVTMYSP LQMAADLPEN YEQHLDAFQF IADVPVDWDD
     TRILAAEPGD YLTTVRKAKG KDEWYLGSIT DENARQQPVK LDFLTPGQRY EAILYADGKG
     ADWQKNPTAY QITKRVVTSK LVLTLKLAPG GGAAVSFRPV GK
//