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Database: UniProt
Entry: C9QD61_VIBOR
LinkDB: C9QD61_VIBOR
Original site: C9QD61_VIBOR 
ID   C9QD61_VIBOR            Unreviewed;       694 AA.
AC   C9QD61;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:EGU50501.1};
GN   Name=malS {ECO:0000313|EMBL:EGU50501.1};
GN   ORFNames=VIOR3934_05859 {ECO:0000313|EMBL:EGU50501.1};
OS   Vibrio orientalis CIP 102891 = ATCC 33934.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=675816 {ECO:0000313|EMBL:EGU50501.1, ECO:0000313|Proteomes:UP000002817};
RN   [1] {ECO:0000313|EMBL:EGU50501.1, ECO:0000313|Proteomes:UP000002817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102891 / ATCC 33934 {ECO:0000313|Proteomes:UP000002817};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EGU50501.1}.
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DR   EMBL; AFWH01000023; EGU50501.1; -; Genomic_DNA.
DR   RefSeq; WP_004411047.1; NZ_AFWH01000023.1.
DR   AlphaFoldDB; C9QD61; -.
DR   STRING; 675816.VIA_000652; -.
DR   PATRIC; fig|675816.5.peg.2018; -.
DR   eggNOG; COG0366; Bacteria.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000002817; 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; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}.
FT   DOMAIN          202..655
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        467
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        510
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         323
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   BINDING         471
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            576
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT   DISULFID        130..545
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   694 AA;  78535 MW;  1DDADF7DD74E9849 CRC64;
     MKKSILALSA SLLAACSQTP NNVLTLTIGE TQATFEQQNG LLVAEQTLTK GSYSLSIADH
     QQSCGSRYAL QDAARIKFNK ALKLDNCSDS AAIPMRVFSA NTYQFVLNPE SNELTVTIKP
     KENAIARYQC PVASDHPTTI DVSATFANGS TIRDALTGQQ ATVSNGKVRL QAGAMSQGVM
     LLEQVESPQI AAFSWDNATV YFVMTDRFYN GNPNNDHSYG RSNDDDKEIA TFHGGDLAGL
     TEKLDYLEQL GVNALWITSP LEQIHGWVGG GSNGDFKHYG YHGYYHQDWT ELDANMGTEQ
     ELKTLIDTAH SKGIRIIWDV VLNHTGYATL ADMQEFDFGQ LYLDAQEAQD ILGEQWTDWT
     PKQGQNWHSF NDYINYRDGE AWQKWWGKDW LRTDIGDYDQ PGYNDRTMSL AHLPDIKTES
     ERATGLPNFY RNKSTNAQDV SQTPQQHLIT WLSDWVREYG IDGFRVDTAK HVEFETWQQL
     KLESTAALAE WKQNNPDKAL DDLPFWMTGE VWAHGVVKSP YFDHGFDSII NFEFQGDVAP
     KALSCFADLD RDYQRYAERI NQDSSFNVLS YLSSHDTSLF WGSRAKTIEQ QVRAANALML
     APGAIQIYYG DEIARDFGPT GSDPHQGTRS DMPWDQITGE RQQLLEHWQK LGQFRQRHPA
     IAQGEHITRH QQGYYAFERR YQDDKVLVVY TGSQ
//
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