ID   Q6LKA3_PHOPR            Unreviewed;       474 AA.
AC   Q6LKA3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=VV20400 {ECO:0000313|EMBL:CAG22277.1};
GN   OrderedLocusNames=PBPRB0404 {ECO:0000313|EMBL:CAG22277.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG22277.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378676; CAG22277.1; -; Genomic_DNA.
DR   RefSeq; WP_011220488.1; NC_006371.1.
DR   AlphaFoldDB; Q6LKA3; -.
DR   STRING; 298386.PBPRB0404; -.
DR   KEGG; ppr:PBPRB0404; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_029247_2_0_6; -.
DR   Proteomes; UP000000593; Chromosome 2.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
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:UP000000593}.
FT   DOMAIN          21..385
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   474 AA;  53598 MW;  70615C9B6EAAF22A CRC64;
     MTSLFNTEYA STLSAPSVAT NVILHAFDWP YSKVTESAKA IADSGYKAIL VSPPLKSFHS
     KDGTQWWQRY QPQDYRVIDN QLGNTNDFRK MAETLNLHDI DIYADIVFNH MANESHERND
     LNYPNSNIIS QYKDKREYFD SIKLFGDLSQ PLFTKDDFLS AFPIKDWKDP WQVQHGRISS
     GGSDPGLPTL KNNKNVVKKQ KLYLKALKKI GVKGFRIDAA KHMTLDHIQE LCDEDITEGM
     HIFGEIITDG GATKEEYELF LQPYLEKTTL GAYDFPLFHT VLDVFNKNAS MASLINPYSL
     GSALENQRAI TFAITHDIPN NDVFLDQVMS EENERLAYCY ILGRDGGVPL VYTDLDTSGI
     KSSRDKPRWC DAWNDPILAN MIHFHNIMHC QPMAIIEQTQ DLLVFSRGEH GVVAINKGKK
     AVSYELPIKY SQQNRTEINE IINMEGVKLL PPSLGSETGA ILQLPAQSCA MLVS
//