ID   Q65QT2_MANSM            Unreviewed;       685 AA.
AC   Q65QT2;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   SubName: Full=AmyA protein {ECO:0000313|EMBL:AAU38678.1};
GN   Name=amyA {ECO:0000313|EMBL:AAU38678.1};
GN   OrderedLocusNames=MS2071 {ECO:0000313|EMBL:AAU38678.1};
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38678.1, ECO:0000313|Proteomes:UP000000607};
RN   [1] {ECO:0000313|EMBL:AAU38678.1, ECO:0000313|Proteomes:UP000000607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38678.1,
RC   ECO:0000313|Proteomes:UP000000607};
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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};
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DR   EMBL; AE016827; AAU38678.1; -; Genomic_DNA.
DR   RefSeq; WP_011201226.1; NC_006300.1.
DR   AlphaFoldDB; Q65QT2; -.
DR   STRING; 221988.MS2071; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; msu:MS2071; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000000607; Chromosome.
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; 1.
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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..685
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004268308"
FT   DOMAIN          195..647
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   ACT_SITE        461
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   ACT_SITE        503
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-1"
FT   BINDING         316
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   BINDING         465
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-2"
FT   SITE            565
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-3"
FT   DISULFID        59..77
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
FT   DISULFID        123..537
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036917-4"
SQ   SEQUENCE   685 AA;  78192 MW;  0E6F28791227DB88 CRC64;
     MKKSLLYLCL FTSSAAFAQG WQHTHFQHFN DNAESNLFQS QTPLGKGNYP LTFTLDNQCY
     QPQSAVKLNQ TVSLIPCSGE APQLRLFRQG NYIAQIDMRS GTPTLRISVE QRAENDNNTV
     KSCPVWNKQP IEIDVSSTFT EGESVRDFYS GQTAKVKNGK VTMMPAENAG GLILLEKSAD
     KKTEVFDWKN ATVYFVLTDR FHNGNPANDN SYGRHKDGMQ EIGTFHGGDL QGLTAKLDYL
     QQLGVNVLWI SSPLEQMHGW VGGGNKGDFP HYGYHGYYHL DWTKLDANMG TEADLKNLMR
     QAHRRGIRVL FDVVMNHTGY ATLADMQEFN FGDFYLKPEE MAATLGKKWT TWQPQKGQNW
     HSFNDFIKFG DSKAWQNWWG KDWVRADIGD YDSPKFDDLK MSLSALPDLK TESESAVKLP
     RFFQHKNTNA KELANAKVRD YLITWLTDWV RRYGVDGFRV DTAKHVEKPT WLALKQASQQ
     ALKEWQQKNP QESFGDDFWM TGEAWGHGVF KSDYYQNGFD AMINFDFQDQ AKNALDCFAR
     IDPVYQDMSN KLKDFNVLSY LSSHDTRLFF HSDSERNAVK QKTAANLLLL SSGAVQIYYG
     DESGREFGAT GSDPVQGTRS DMNWKELQND QSKQALHQHW QKLAQFRQRH RAVGAGVHQT
     LKSEGYFAFS RTLGEDKVMV VWAGN
//