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Database: UniProt
Entry: A0A151JE03_9VIBR
LinkDB: A0A151JE03_9VIBR
Original site: A0A151JE03_9VIBR 
ID   A0A151JE03_9VIBR        Unreviewed;       687 AA.
AC   A0A151JE03;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:KYN23857.1};
GN   ORFNames=AUQ44_18500 {ECO:0000313|EMBL:KYN23857.1};
OS   Vibrio cidicii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1763883 {ECO:0000313|EMBL:KYN23857.1, ECO:0000313|Proteomes:UP000075349};
RN   [1] {ECO:0000313|Proteomes:UP000075349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2756-81 {ECO:0000313|Proteomes:UP000075349};
RA   Tarr C.L., Gladney L.M.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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};
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:KYN23857.1}.
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DR   EMBL; LOMK01000002; KYN23857.1; -; Genomic_DNA.
DR   RefSeq; WP_065820088.1; NZ_CP046803.1.
DR   AlphaFoldDB; A0A151JE03; -.
DR   Proteomes; UP000075349; Unassembled WGS sequence.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
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:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR036917-2};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..687
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007582616"
FT   DOMAIN          203..646
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        464
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        504
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   BINDING         468
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            569
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT   DISULFID        130..538
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   687 AA;  76472 MW;  9D3939211842C91C CRC64;
     MKLNAITLTL LLSSAAAVAE PNLTISTTTN SRDFPLSAEQ PLVVPLVKDT YTLKVTGLEG
     NCQAQDDQRI KFNQPISLNC GKATELPLKI LFSGDYSFAF DASANTLTFK REPKKVAKSE
     FKRPVPQVEC EVYAGGEVSV NLGDTFADGT ELRDAYSGQT VTVKNGAVSL TPAAGSGGLL
     LLEPVTPAKS DTGFDYRNAN IYFVMVDRFH NADPSNDNSY GRKKDGKEEV GTFHGGDLKG
     VIAKLDYIQS LGTDAIWLSP IVEQVHGFVG GGDSGSFPFY AYHGYWTRDF TKIDQNFGND
     ADLKTLVDEA HKRGIKVLLD AVINHSGYST LADLQFDGLN VIKPEGQLPP KWADWQPQAG
     QNWHSYHQAI DYQSQNWRQW WGPDWVRTGL PGYQAPGSSD ITMSLAGLPD FITESTQAVT
     PPAWLLNNPG TRVVARENYS VADYLIEWQS DWVKRFGIDG YRVDTVKHVE GEVWQRLKKA
     GSERLEEWRK ANGKTGEPFW MMGEVWGHSA YRSPYFDDGF DALINFDMQK KLDKGAACFS
     QMADTYQDYA NTIVKEKDFN PVSYMSSHDT ELFFSRFKDY AMQRNAANAL LLSPGAVQVY
     YGDEIGRNIG PYADDFHQGT RSDMVWTLND DQQGLLKHWQ TVAKFRQAHP AIGAGVHQVI
     EQEGAYVFSR TQGDDKVVVA FVGRTEK
//
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