ID A0A2V3PLI5_9BACT Unreviewed; 668 AA.
AC A0A2V3PLI5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:PXV60093.1};
GN ORFNames=CLV62_13113 {ECO:0000313|EMBL:PXV60093.1};
OS Dysgonomonas alginatilytica.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC Dysgonomonas.
OX NCBI_TaxID=1605892 {ECO:0000313|EMBL:PXV60093.1, ECO:0000313|Proteomes:UP000247973};
RN [1] {ECO:0000313|EMBL:PXV60093.1, ECO:0000313|Proteomes:UP000247973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100214 {ECO:0000313|EMBL:PXV60093.1,
RC ECO:0000313|Proteomes:UP000247973};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PXV60093.1}.
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DR EMBL; QICL01000031; PXV60093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3PLI5; -.
DR OrthoDB; 1109141at2; -.
DR Proteomes; UP000247973; 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..668
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015923354"
FT DOMAIN 31..299
FT /note="Glycosyl-hydrolase 97 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14508"
FT DOMAIN 304..569
FT /note="Glycosyl-hydrolase 97 catalytic"
FT /evidence="ECO:0000259|Pfam:PF10566"
FT DOMAIN 572..666
FT /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF14509"
SQ SEQUENCE 668 AA; 76179 MW; C9A6E2FBB608A949 CRC64;
MKSAHKSYVL LLVMCFICSS ITTLAQKPFT VQSPNGKLKV NVSVGNIIEY SLEHDGDLML
KNSPISMVLT DGTSFGVNSK LSGSSTKTVN QTIAASIYKK KEITDNYNEL NLKFKEGFNI
IFRAYNDGIA YRFVSNLKKP FEVKEEQAIF NFPKDEKAYI PYVQRIKEPL EKQFYNSFEN
TYQHINISQW DKKRLAFLPL VVEAPKGKKI CITEADLTSY PGMYLYNSDG SNNLTGVFAP
YPKEIKQGGH NMLQGEVQSQ EPYIAKCNGA NNFPWRTLIV SENDHDLADN DMVYKLATPN
KVTDISWIKP GKVAWDWWND WNLFNVDFKS GINNETYKYY IDFASDHGIE YVILDEGWAV
NLQADLYQVV PAIDLKELVD HANKKNVGLI LWAGYYAFNK DIEGICKHYS EMGIKGFKVD
FMDRDDQPMV DFHYRAAEIA AKHHMLLDYH GTYKPTGLQR TFPNVINFEG VHGLEQMKWS
PESVDQVTYD VTVPFIRMVA GPMDYTQGAM RNASKGNYRP VNSEPMSQGT RCRQLAEYII
FESPLNMLCD NPSNYMLEKE CTEFIANVPT IWDNTIALNG KIGEYITIAR KKDNIWYVGS
LTNWDARALD IDLSFLGEGN YKAEVFKDGI NANRSGHDYK KEIIDIPANR KLQLPMASAG
GYVMKIYK
//
