ID   J1YD98_9ALTE            Unreviewed;       641 AA.
AC   J1YD98;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Alpha amylase catalytic subunit {ECO:0000313|EMBL:EJI85850.1};
GN   ORFNames=AEST_12520 {ECO:0000313|EMBL:EJI85850.1};
OS   Alishewanella aestuarii B11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alishewanella.
OX   NCBI_TaxID=1197174 {ECO:0000313|EMBL:EJI85850.1, ECO:0000313|Proteomes:UP000012043};
RN   [1] {ECO:0000313|EMBL:EJI85850.1, ECO:0000313|Proteomes:UP000012043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B11 {ECO:0000313|EMBL:EJI85850.1,
RC   ECO:0000313|Proteomes:UP000012043};
RX   PubMed=22965096; DOI=10.1128/JB.01255-12;
RA   Jung J., Choi S., Chun J., Park W.;
RT   "Genome Sequence of Pectin-Degrading Alishewanella aestuarii Strain B11T,
RT   Isolated from Tidal Flat Sediment.";
RL   J. Bacteriol. 194:5476-5476(2012).
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:EJI85850.1}.
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DR   EMBL; ALAB01000011; EJI85850.1; -; Genomic_DNA.
DR   RefSeq; WP_008607797.1; NZ_ALAB01000011.1.
DR   AlphaFoldDB; J1YD98; -.
DR   PATRIC; fig|1197174.4.peg.1223; -.
DR   Proteomes; UP000012043; Unassembled WGS sequence.
DR   GO; GO:0047669; F:amylosucrase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11324; AmyAc_Amylosucrase; 1.
DR   Gene3D; 1.10.1740.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR044077; Amylosucrase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   PANTHER; PTHR10357:SF213; ALPHA AMYLASE CATALYTIC REGION; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
FT   DOMAIN          109..532
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   641 AA;  73138 MW;  14BAAA13B03D7C27 CRC64;
     MPQYLTRSMT ADPAQLAHFS DILLKRYSSS LKTLAKGRWP LLAERLRQQL PALLALYLPL
     YGARFDAYYH LEQLLKILAK AIAQRPDYLL AEDAAPQDWH QSQQALGSAC YVDLFAGDFQ
     RLKQRIPYLQ QTGINYLHLM PLFKAPEPNS DGGYAVSDYR ATMPKLGTMT ELADLMQSLH
     QHGIRPVLDF VFNHTSDEHR WAQKAKAGDT EYQDYYFFFD EAERDRYAPY LREIFPEIRR
     GCFTREANSG RWVWTTFNSF QWDLNYANPA VFNAMAEEML FLANQGAAVL RLDALAFVWK
     EAGTNCENLP LAHTLIRAFN QVARLAAPAL QFKSEAIVHP DEVVKYIAPE ECQLSYNPLL
     MALLWNSLAT RKTRLLTESL QRRFAIDPHC SWVNYIRCHD DIGWTFDDNV AWQLGINPEH
     HRQFLNQFYT GQFAGSFASG VPFQQNPQTG DCRVAGMLAS LTGVEQALKT GNTAHLQHAL
     ARIYLLNSVI LSIGGLPLLY MGDELGLLND YSYQQDAAKK DDSRWVNRVA VNEQQLESAT
     DSTKLSGKIY QQLQQLLGVR RRLPLLGQGK TEILASANPH LFSYRRYQDQ QSLLCVVNFS
     EHSQTLAMPA CSQWRDELSG NLYQGARLEL QPYQVLWLTA L
//