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Database: UniProt/TrEMBL
Entry: Q663W5_YERPS
LinkDB: Q663W5_YERPS
Original site: Q663W5_YERPS 
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
//
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