ID A0A1W6E5A8_9BACT Unreviewed; 652 AA.
AC A0A1W6E5A8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:ARK10571.1};
GN ORFNames=A6C57_09660 {ECO:0000313|EMBL:ARK10571.1};
OS Fibrella sp. ES10-3-2-2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK10571.1, ECO:0000313|Proteomes:UP000193660};
RN [1] {ECO:0000313|Proteomes:UP000193660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL Submitted (APR-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; CP015317; ARK10571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6E5A8; -.
DR STRING; 1834519.A6C57_09660; -.
DR KEGG; fib:A6C57_09660; -.
DR Proteomes; UP000193660; Chromosome.
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:UP000193660};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..652
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012506756"
FT DOMAIN 28..291
FT /note="Glycosyl-hydrolase 97 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14508"
FT DOMAIN 304..560
FT /note="Glycosyl-hydrolase 97 catalytic"
FT /evidence="ECO:0000259|Pfam:PF10566"
FT DOMAIN 562..632
FT /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF14509"
SQ SEQUENCE 652 AA; 72033 MW; FB97C430F1FD859F CRC64;
MKNKLNYTFL LFLIIPFWAS AQPANSVVSS PNGKLLVTLS LDNGMPAYSV SLDGKSFVVK
SPLGLKTNVG DFTEGLSVGK ALAISKLDNT YELPNIKQSR VHYVANEGVI SYSKDNASAI
DITFRVSNND VAFRYKVYPQ KASRSCVINE EKTGFTFPAG TTTFLSAQSK AMVGFARTMP
SYEIPYTVDD TLGKNGRGNG YTFPCLFKVN TNGWVLVSET GVDSRYCGSR LIGHTDGLYT
IGFPMPDENN GIGTSAPGIP LPGETPWRTI TVGETLSPIV ETTVPFDVVE PRYEGSQTYE
YTKGSWSWII GMDGRTVYNE QVRYIDFSAA MGYKTILVDA LWDTQIGKDK IAELAKYGAS
KGVSLYLWYN SNGYWNDAPQ GPRGIMDNTI ARRKEMAWMK KIGVKGIKVD FFGGDKQETM
KLYEDILYDA NDFGILCIFH GSTLPRGWER MYPNYAASEA VLASENLAFS QGSNDREAFN
ATLHPFIRNT VGSMDFGGSA LNKFYNANNT PNRGSKRVTS DVYALATAVL FQSAVQHFAL
APNNLTDAPD WAIDFMKTVP TTWDEVRFID GYPGRYVVLA RRQGRKWYVA GVNAQKEPIK
LKLKLPMLTA GAEYTLYSDD AQLTGKVTTA KLPKNQEVEW VIPTNGAALL VN
//
