ID   Q8E0M2_STRA5            Unreviewed;       488 AA.
AC   Q8E0M2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=Alpha amylase family protein {ECO:0000313|EMBL:AAM99595.1};
GN   OrderedLocusNames=SAG0708 {ECO:0000313|EMBL:AAM99595.1};
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435 {ECO:0000313|EMBL:AAM99595.1, ECO:0000313|Proteomes:UP000000821};
RN   [1] {ECO:0000313|EMBL:AAM99595.1, ECO:0000313|Proteomes:UP000000821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R {ECO:0000313|Proteomes:UP000000821};
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin S., Kolonay J.F., Umayam L.A., Madupu R., Lewis M.R.,
RA   Radune D., Fedorova N.B., Scanlan D., Khouri H., Mulligan S., Carty H.A.,
RA   Cline R.T., Gill J., Scarselli M., Mora M., Iacobini E.T., Brettoni C.,
RA   Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., Rappuoli R.,
RA   Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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; AE009948; AAM99595.1; -; Genomic_DNA.
DR   RefSeq; NP_687723.1; NC_004116.1.
DR   RefSeq; WP_000180590.1; NC_004116.1.
DR   AlphaFoldDB; Q8E0M2; -.
DR   STRING; 208435.SAG0708; -.
DR   KEGG; sag:SAG0708; -.
DR   PATRIC; fig|208435.3.peg.714; -.
DR   HOGENOM; CLU_024572_2_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000000821; Chromosome.
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; cd11318; AmyAc_bac_fung_AmyA; 1.
DR   Gene3D; 2.40.30.140; -; 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; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001021-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000821}.
FT   DOMAIN          4..392
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        234
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   ACT_SITE        264
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-1"
FT   BINDING         103
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         197
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
FT   BINDING         238
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001021-2"
SQ   SEQUENCE   488 AA;  56555 MW;  57249E354B2F053E CRC64;
     MTNELIMQAF EWYLPSDGNH WKKLEESISD LKKLGISKIW LPPAFKGTSS DDVGYGVYDL
     FDLGEFDQNG TIRTKYGRKE EYLKLIKSLK ANGIKPFADI VLNHKANGDH KEKFQVIKVN
     PENRQEALSE PYEIEGWTGF DFPGRQGEYN DFKWHWYHFT GLDYDAKNNE TDIFMIVGDN
     KGWADDDLID DENGNFDYLM YNDIDFKHPE VIKNLQDWAK WFIETTGIEG FRLDAVKHID
     SYFIQTFIND IRTKIKPDLE VFGEYWKSDQ TSMKDYLEAT QFQFSLVDVT LHMNFFDASH
     QNRDFDMRTI FDDSLVIDNP EYAVTFVENH DTQSGQALES RVEDWFKPLA YGLILLRQQG
     TPCLFYGDYY GIQGEFGQPS FKEVIDKMAE LRQNYVFGKQ VDYFTHSNCI GWTCLGDEEH
     NSCLAVVLTN GDQGWKHMEV GEIYAGKTFV DYLGNCEQEV VIGDDGWGDF LVESASISAW
     VPKIEEAN
//