ID W6U3Z8_9SPHI Unreviewed; 654 AA.
AC W6U3Z8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:ETZ19971.1};
GN ORFNames=N824_07105 {ECO:0000313|EMBL:ETZ19971.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ19971.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ19971.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ19971.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
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:ETZ19971.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWRU01000032; ETZ19971.1; -; Genomic_DNA.
DR RefSeq; WP_048907400.1; NZ_AWRU01000032.1.
DR AlphaFoldDB; W6U3Z8; -.
DR STRING; 509635.N824_07105; -.
DR PATRIC; fig|509635.5.peg.4865; -.
DR eggNOG; COG4948; Bacteria.
DR OrthoDB; 57532at2; -.
DR Proteomes; UP000019145; 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}.
FT DOMAIN 30..288
FT /note="Glycosyl-hydrolase 97 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14508"
FT DOMAIN 293..553
FT /note="Glycosyl-hydrolase 97 catalytic"
FT /evidence="ECO:0000259|Pfam:PF10566"
FT DOMAIN 555..653
FT /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF14509"
SQ SEQUENCE 654 AA; 74240 MW; 5F2572AD0E03E6D3 CRC64;
MNFINKLVLI IVAVFGLSAV SKAQTKGIEL KSPNGGLKVS INISDKIYYS IFSGEDLLLE
NNHLQMNLRN EILGQNPKLT SSKKGQGNEI ITPYVSLKFS TVKSNYNALT FNFKGNYAVE
FRAFDDGIAY RFITRKKGSV EVMNEEFSVN FPGDYMLHLQ QPGGFKTAYE ELYSQVRSKD
WKPENKMSTL PVLIDTKKKY KILISESDLT DYPCLFLKGT GNNGMSSAFP KVPLEFGDDG
DRSLKILKEA DYIAKTSGTR NFPWRYFVVT SNDKQLLENT MTLKLASPSV LKDPSWVKPG
QASWEWWNDA APYGPDVNFI SGYNLATYKY YIDFAAKFGI PYIIMDEGWA KSTTDPYTPN
PDVDVHELIR YGKEKNVGVV LWLTWLTVHK NMELFKTFQE WGVKGVKIDF MDRSDQWIVN
YYEDVAKEAA KHKLFVDFHG AFKPAGLEYK YPNVISYEGV RGMEQMGGCY PDNSLYLPFM
RNAVGPMDYT PGAMISMQPD AYRAERPNAA SIGTRAYQLA LFVVFESGIQ MLADNPTLYY
RNLDCTEFIT SVPTTWDETK ALEAKMGEVA VVAKRKKDKW FVGAITNGKE KERTVSLNFD
FLEKGKTYTM TYFEDGINAG RQAMDYRKKT VQVKSGDKID IKMVRNGGWA AVIM
//
