ID S3BCZ2_9FLAO Unreviewed; 700 AA.
AC S3BCZ2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Alpha-glucosidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1528_02063 {ECO:0000313|EMBL:EPD98301.1};
OS Capnocytophaga sp. oral taxon 336 str. F0502.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1203603 {ECO:0000313|EMBL:EPD98301.1, ECO:0000313|Proteomes:UP000014404};
RN [1] {ECO:0000313|EMBL:EPD98301.1, ECO:0000313|Proteomes:UP000014404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0502 {ECO:0000313|EMBL:EPD98301.1,
RC ECO:0000313|Proteomes:UP000014404};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Tanner A.C.,
RA Dewhirst F.D., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capnocytophaga sp. oral taxon 336 F0502.";
RL Submitted (MAY-2013) 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:EPD98301.1}.
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DR EMBL; ATCI01000023; EPD98301.1; -; Genomic_DNA.
DR RefSeq; WP_016479672.1; NZ_KE150492.1.
DR AlphaFoldDB; S3BCZ2; -.
DR PATRIC; fig|1203603.3.peg.2021; -.
DR HOGENOM; CLU_011166_2_0_10; -.
DR Proteomes; UP000014404; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR35803:SF1; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB; 1.
DR PANTHER; PTHR35803; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB-RELATED; 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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..700
FT /note="Alpha-glucosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004506148"
FT DOMAIN 24..290
FT /note="Glycosyl-hydrolase 97 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14508"
FT DOMAIN 295..596
FT /note="Glycosyl-hydrolase 97 catalytic"
FT /evidence="ECO:0000259|Pfam:PF10566"
FT DOMAIN 599..700
FT /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT /evidence="ECO:0000259|Pfam:PF14509"
SQ SEQUENCE 700 AA; 79456 MW; 2D8ED02756218618 CRC64;
MKKFIITIVC MLCAAPLLFA QTLLSPNENL KLSFRLTEKG TPTYALTFKG KTVISESALG
FVINQKEDFN SNFEITDVQF AEANSVWQPV LGENKEIRDH HKEMLVHLSQ KNSGRQLLLR
FRLFNDGLGF RYEFPLQDNF RHFRIQEELT VFQLSGNHKA FWIPADYDTN EFPITTSAIS
EIPKLIDKVR EEPLAAKAPT PNVAVQTPLM LKSSDGLYIN LHEAALVNYP AMMLNVNATK
HQLSAHLVPD KNGVKGYIQT GSVTPWRTIV VSDDARDILA SNLILNLNDP CKITDTSWIH
PTKYIGVWWE YFIGGGSTWA YSDDRDITIG VTDYTKLKPN GHHGANTEHV KKYINFASQH
GFDAVLVEGW NEGWEDNYAY NKERIYSFTK AYPDFDVQAL HQYAAAKGVK LIMHHETTSS
VVDYERHLHE AFRFMNDNGY DAVKTGYVGP IIPRSEYHDG QWMVNHYNYV AETAAKYRIM
VNSHEAVRPT GMSRTYPNWV AQESARGTEF ESFNGNHPEH TTILPFTRLM GGAMDYTPGI
FEGDLSRYGN NKAKRSTTLV KQLALYVTMY SPLQMAADLP ENYEKHLDAF QFIKDVAADW
DNTYILEAEP GDYITIARKA KGKNEWFVGA ITDENAREAL VDFSFLPKGK TYTATLYTDG
KNADWRTNPN SYSIKTMKVT QKTKLKQRLA PSGGLAISIK
//