ID S3BJ40_9FLAO Unreviewed; 469 AA.
AC S3BJ40;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:EPE01304.1};
GN ORFNames=HMPREF1528_00134 {ECO:0000313|EMBL:EPE01304.1};
OS Capnocytophaga sp. oral taxon 336 str. F0502.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1203603 {ECO:0000313|EMBL:EPE01304.1, ECO:0000313|Proteomes:UP000014404};
RN [1] {ECO:0000313|EMBL:EPE01304.1, ECO:0000313|Proteomes:UP000014404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0502 {ECO:0000313|EMBL:EPE01304.1,
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:EPE01304.1}.
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DR EMBL; ATCI01000001; EPE01304.1; -; Genomic_DNA.
DR RefSeq; WP_016478214.1; NZ_KE150488.1.
DR AlphaFoldDB; S3BJ40; -.
DR PATRIC; fig|1203603.3.peg.131; -.
DR HOGENOM; CLU_024572_3_0_10; -.
DR Proteomes; UP000014404; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11314; AmyAc_arch_bac_plant_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR015237; Alpha-amylase_C_pro.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR Pfam; PF09154; Alpha-amy_C_pro; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 2.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2}.
FT DOMAIN 43..388
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT ACT_SITE 260
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ SEQUENCE 469 AA; 53759 MW; D8A547B389798E79 CRC64;
MKYYIYLLAG LLAFSCDKKS NKDNPEPQNT VPLDLTKIDN GNRVMMQAFY WDVTPLGEWW
NTITPKLTEW KANGVDRIWL PPASKGASGG LSMGYDPSDY FDFGEYFQHE TTKTRFGSRA
ELENLISKAH ESGLQVIADI VIGHNNGGGK EWNPYRNKET YTLFDETHGN ASGRFNRNYE
CFHPNKYATS DEEENFYPER DLSHKVPYVR EELWEKDNSM AKYYKNTMKF DGWRFDYVKS
FGAWVVRDWL KAVGGFAVGE LWDGNPETLK KWVDESGASA FDFACFYALE KALDRNKDMH
ELMTDTHPML RTLRTEKAVT FTANHDTEKD KIADNTIAPD KKLMAYAYIL THSGYPCIFY
SDYENEAFKA KLQKLMLINR SLAVGEEKFH LASNTEYVAS RLGNEKSPGL VLFINNSSLP
AKRTITTHWK NKTLIDYSGN SHLFFVTDSD GNVTIQVPAN SYTVWSIGK
//
