ID   Q7CLU8_XANCP            Unreviewed;       475 AA.
AC   Q7CLU8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amy {ECO:0000313|EMBL:AAM40063.1};
GN   OrderedLocusNames=XCC0748 {ECO:0000313|EMBL:AAM40063.1};
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM40063.1, ECO:0000313|Proteomes:UP000001010};
RN   [1] {ECO:0000313|EMBL:AAM40063.1, ECO:0000313|Proteomes:UP000001010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC   {ECO:0000313|Proteomes:UP000001010};
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC         polysaccharides containing three or more (1->4)-alpha-linked D-
CC         glucose units.; EC=3.2.1.1; Evidence={ECO:0000256|RuleBase:RU361134};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; AE008922; AAM40063.1; -; Genomic_DNA.
DR   RefSeq; NP_636139.1; NC_003902.1.
DR   AlphaFoldDB; Q7CLU8; -.
DR   STRING; 190485.XCC0748; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; AAM40063; AAM40063; XCC0748.
DR   KEGG; xcc:XCC0748; -.
DR   PATRIC; fig|190485.4.peg.813; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_029247_2_0_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11315; AmyAc_bac1_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001010};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..475
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004288060"
FT   DOMAIN          36..384
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   475 AA;  51839 MW;  981AC0D90777488C CRC64;
     MHATSRPCPR TFWQRAHQLL LIALTLLLTT ASAQADVILH AFNWPYATVE ARAKQIADAG
     YRKVLVAPAY RSEGSAWWAR YQPQDIRLID NPLGDTTAFA RMVQALANNG VETYADVVFN
     HMANEAATRS DLNYPGSAVL AQYAANPGRY DALRLFGTVQ SNFLSASDFG PAQCISNYND
     AFQVRNYRIC GGGSDPGLPD LLGNDWVVQQ QRAYLQALKG LGVTGFRVDA AKHMTFDHLN
     RVFDAGIRSG VYVFGEVITG GGSGNGDYDQ FLAPYLQSTP HAAYDFPLFN AVRNAFGVGA
     SMQQLVDPAS TGQALPGNRA VTFAVTHDIP NNAGFRYAIL DPVDETLAYA YLLGRNGGVP
     MVYTDNNESG DNRWVNAYLR DDLRRMIGFH NGVQGSDMQV LSSSACHILF RRGSLGIVGI
     NKCGNPVNTT VAMNGSVLFW NADYVDALGS GTVVRISSGS YTFTLPARQA RMWRR
//