ID A0A1M6HXZ9_9BACE Unreviewed; 666 AA.
AC A0A1M6HXZ9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:SHJ26984.1};
GN ORFNames=SAMN05444350_12043 {ECO:0000313|EMBL:SHJ26984.1};
OS Bacteroides stercorirosoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871324 {ECO:0000313|EMBL:SHJ26984.1, ECO:0000313|Proteomes:UP000184192};
RN [1] {ECO:0000313|EMBL:SHJ26984.1, ECO:0000313|Proteomes:UP000184192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26884 {ECO:0000313|EMBL:SHJ26984.1,
RC ECO:0000313|Proteomes:UP000184192};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQZN01000020; SHJ26984.1; -; Genomic_DNA.
DR RefSeq; WP_025831483.1; NZ_FQZN01000020.1.
DR AlphaFoldDB; A0A1M6HXZ9; -.
DR eggNOG; COG4948; Bacteria.
DR Proteomes; UP000184192; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..666
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009918249"
FT DOMAIN 26..295
FT /note="Glycosyl-hydrolase 97 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14508"
FT DOMAIN 300..566
FT /note="Glycosyl-hydrolase 97 catalytic"
FT /evidence="ECO:0000259|Pfam:PF10566"
FT DOMAIN 568..663
FT /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF14509"
SQ SEQUENCE 666 AA; 76014 MW; 46F767F51ECB0216 CRC64;
MRRFCLTLTF LSAFLSFSIA QKQYQLKSPN GKLKLSIEAG DKICYSLKHE NTAIIVSSPI
SMSLSNNKIL GVKSKVKNVR RRVVDENITT AIYKRSEIRN RCNELSLTFR DGFQLEFRAY
DEGVAYRFVV TENKPFNVIA EEATFNFDDD YMTYIPYVRG GKNKKVEDQF FNSFENVYTH
VNLSEMGTNQ LAFTPVVVEL KDGKKLCIAE SDVESYPGMF VRNANQSNSL KGVFAPYPKE
TIQGGHNKLQ KLVTAREDYI AKCSGRRSFP WRIAIVSSDD KELLDNDMVY KLAAPSRLED
TSWIKPGKVA WEWWNSCGLS GVDFKAGVNN VTYKAYIDFA SKHGIEYVIL DEGWAVNLKA
DLFQVVPEID LKELVAYADS KHVGLILWAG YYAFERDLES ICKHYSELGI KGFKVDFMDR
DDQAMVDFHY RGAEIAAKYH LMLDYHGTYK PTGMNRTYPN VINFEGVHGL EQLKFSGSEK
VDQVTYDVTM PFIRMIAGPV DYTQGAMKNG NKRNFRAVNE EPMSMGTRCR QLAEYVIFEA
PLSMLCDSPV LYERESECTS YISDIPTVWD ETKALNGKIG EYISMARRKG DVWYVGALTN
WKKRTMEFDF SFLGEGEWTI ELYKDGINAD KIASDYRKSV IFVPQNRKLT VNLAEGGGCA
MKIYKK
//
