ID A0A1T5K1L5_9BACT Unreviewed; 658 AA.
AC A0A1T5K1L5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:SKC57398.1};
GN ORFNames=SAMN06298215_1712 {ECO:0000313|EMBL:SKC57398.1};
OS Bacteroidales bacterium WCE2008.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1945891 {ECO:0000313|EMBL:SKC57398.1, ECO:0000313|Proteomes:UP000190446};
RN [1] {ECO:0000313|EMBL:SKC57398.1, ECO:0000313|Proteomes:UP000190446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCE2008 {ECO:0000313|EMBL:SKC57398.1,
RC ECO:0000313|Proteomes:UP000190446};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUZM01000005; SKC57398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5K1L5; -.
DR STRING; 1945891.SAMN06298215_1712; -.
DR Proteomes; UP000190446; 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:UP000190446};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..658
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010547701"
FT DOMAIN 32..291
FT /note="Glycosyl-hydrolase 97 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14508"
FT DOMAIN 297..557
FT /note="Glycosyl-hydrolase 97 catalytic"
FT /evidence="ECO:0000259|Pfam:PF10566"
FT DOMAIN 560..656
FT /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF14509"
SQ SEQUENCE 658 AA; 74836 MW; 1019FDD7637E696F CRC64;
MNFNKAFIML GIAFLSQAGL HNSFAANKPQ TVQSPDGHLK IEVNTTGDLS YDVYAGEKAI
MTGNTLSIKI GDKVYGHDAR LVKATRKSVN ETFQPFLAFK SSTVENKYNQ LLLKFKGGYS
VEFRAYDDGI AYRFLTNLPG KVEVLDEEIG VRFPEAFRMT LQQCDRFKTS YEERYSHPLS
SEWKEGDKMA HLPILAQTGE GCNIMFSETN LFDYPGAFFR SKGDNGFTSI FPKYPAKQVQ
EPDRDRSLKI EEEAEYIALT DGKREFPWRY FVITKEDGDL LTTTLPVRLA ERSAIEDTSW
IKPGQASWEW WNGAIPYGPD VNFKSGCNLE TYKYFIDFAS KYGIEYIVMD EGWAKNTRDP
FTPNPDVDLH ELIRYGKEKN VGIILWLTWL CVENNPAVFE TFEKWGVAGI KIDFMDRSDQ
WMVNFYERTV AEAAKHHLFI DYHGAYKPSG LEYKYPNLLS YEGVTGMEQM GGCKPENSVY
LPFLRNVTGA MEYTPGAMIS MQPEYYSARR PNSASIGTRA YQMALFVVFE SGIQMLADNP
TLYYRNDECT KFISDVPVLW DETKALAAEI GQYVLVAKRK GDKWFIGGMT SERNEPLVIE
FPLDFLGEGS YTMTSFEDGI NADVQAMDYR KNTKKVAKGD KITVSMVRNG GFAAVIEQ
//
