ID Q663W5_YERPS Unreviewed; 687 AA.
AC Q663W5;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=Alpha-amylase protein {ECO:0000313|EMBL:CAH23147.1};
DE EC=3.2.1.1 {ECO:0000313|EMBL:CAH23147.1};
DE Flags: Precursor;
GN Name=malS {ECO:0000313|EMBL:CAH23147.1};
GN OrderedLocusNames=YPTB3909 {ECO:0000313|EMBL:CAH23147.1};
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH23147.1, ECO:0000313|Proteomes:UP000001011};
RN [1] {ECO:0000313|EMBL:CAH23147.1, ECO:0000313|Proteomes:UP000001011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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};
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DR EMBL; BX936398; CAH23147.1; -; Genomic_DNA.
DR RefSeq; WP_011193333.1; NZ_CP009712.1.
DR AlphaFoldDB; Q663W5; -.
DR GeneID; 66843672; -.
DR KEGG; ypo:BZ17_2672; -.
DR KEGG; yps:YPTB3909; -.
DR PATRIC; fig|273123.14.peg.2801; -.
DR OMA; DKVMVVW; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
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; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF209; PERIPLASMIC ALPHA-AMYLASE; 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 Glycosidase {ECO:0000313|EMBL:CAH23147.1};
KW Hydrolase {ECO:0000313|EMBL:CAH23147.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
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_5004268388"
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; 77131 MW; 939D0D95C1646FE7 CRC64;
MKRLTLPLLL VLSPAAMANW SLQHFPAFTE QDSGIFLSSS SLTKGEYPLK FYQDKQCWQP
TGPVKLNQML SLQPCQENIA IPWRLFRDGQ YQARIDTRSG TPTLTLSVTA PVAEAIQVVT
HSCQRWDGNP VTVDVSKTFA EGEIVRDFYS GQTATVSLGK ITLRPAPESG GLLLLESAQT
QQAAPFSWQN ATVYFALTDR FNNGNPANDH SYGRHGDGMQ EIGTFHGGDL AGLTEKLDYL
QQLGVNALWI SSPLEQIHGW VGGGTKGDFP HYAYHGYYGL DWTRLDANMG TEQDLRTLVE
QAHKRGIRIL FDVVMNHVGY ATLADMQNDQ FGALYLQGDQ QEKTLGKRWN DWTPGSGQTW
HSFNDYINFS DKTAWDNWWG KKWIRTDIGD YDTPGYDDLT MSLAFLPDIK TESTQPSGLP
VFYRNKPDTA AQEIAGATPR DYMTHWLSQW VRDYGIDGFR VDTAKHVEKP AWQQLKQQSI
AALAEWKAAH PEQALDNLPF WMTGEAWGHG VMKSDYYQNG FDAMINFDFQ DQANQALACF
SSIESTYNQM AEKLQNFNVL SYLSSHDTRL FFKDDAQQSL AKQQRAGSLL LLAPGAVQIF
YGDESGRKFG PTGSDPLQGT RSDMNWSELS GEKGALLAHW QKVSQFRARH PAIGAGVQQS
QQTANYYAFS RQHQGDKVLV VWVGDKN
//