ID A0A0L7TCB0_9GAMM Unreviewed; 687 AA.
AC A0A0L7TCB0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Alpha-amylase {ECO:0000313|EMBL:KOC93014.1};
GN Name=malS {ECO:0000313|EMBL:KOC93014.1};
GN ORFNames=NG42_13775 {ECO:0000313|EMBL:KOC89171.1}, NG43_12615
GN {ECO:0000313|EMBL:KOC93014.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC93014.1, ECO:0000313|Proteomes:UP000036851};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC89171.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC93014.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR036917-2};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR036917-2};
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:KOC93014.1}.
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DR EMBL; JRXE01000018; KOC89171.1; -; Genomic_DNA.
DR EMBL; JRXF01000018; KOC93014.1; -; Genomic_DNA.
DR RefSeq; WP_052900031.1; NZ_JRXF01000018.1.
DR AlphaFoldDB; A0A0L7TCB0; -.
DR STRING; 1560201.NG42_13775; -.
DR PATRIC; fig|1560201.3.peg.2931; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030980; P:alpha-glucan catabolic process; IEA:InterPro.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR014635; A_amylase_MalS.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 2.
DR PIRSF; PIRSF036917; Alph_amls_MalS; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR036917-2};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR036917-4};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..687
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010427091"
FT DOMAIN 195..647
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 462
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT ACT_SITE 505
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT SITE 567
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT DISULFID 57..75
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
FT DISULFID 123..539
FT /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ SEQUENCE 687 AA; 76894 MW; B1D8AA575B6E68EA CRC64;
MKTLLLSLLM LLSPLAAASW TLESFPAFTA AGDGLFTSSA RLPKGQLPLR LYQDNQCWQP
AGQIRLNQTL SLQPCGDTPA VSWRQFRAGE YQLRIDTRSG TPTLQLSLKN NDQLTRAVVS
QICPRWDGKP VTIDVSSSFA EGETVRDFYA GQTATVTQGK ITLQPAAESG GLLLLESAAT
ANKAPFNWHN ATVYFVLTDR FANGDPTNDH SYGRRSDGQQ EIGTFHGGDL AGLTQKLDYL
QQLGVNALWI SSPLEQIHGW IGGGTKGDFP HYAYHGYYTL DWTRLDANMG NEQDLRALVE
QAHKRGIRLL FDVVVNHVGY ATLTDMQTWQ FGALYLQGAE REEILGKHWG DWRPAAGQNW
HSFNDYINFS DKTGWSQWWG KNWIRTDIGD YDSPGYDDLT MSLAFLPDIK TEAPGASGLP
LFYRHKPDSA AREIPGATPR DYLTHWLSQW VREYGIDGFR VDTAKHVEKA TLAQLKQQAG
VALAQWKAQH PEQAVDNAPF WMTGEAWGHG VMESDYYQHG FDAMINFDFQ DRAAQALNCF
SAIDATYQQM ADKLQRFNVL SYISSHDTRL FFSHDAGQSL SLQQRAADLL LLAPGAVQIY
YGDESGRPFG ATGSDPLQGT RSDMNWDELQ GSKAALLQHW QKLGTFRARH PAIGAGMQQS
QQRTNYYAFS RQHGQDRVMV VWVGDRQ
//
