ID A0A143HP38_9GAMM Unreviewed; 568 AA.
AC A0A143HP38;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=A3224_13645 {ECO:0000313|EMBL:AMX03479.1}, SAMN05660479_03257
GN {ECO:0000313|EMBL:SFD13936.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX03479.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMX03479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|EMBL:AMX03479.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SFD13936.1, ECO:0000313|Proteomes:UP000181967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19189 {ECO:0000313|EMBL:SFD13936.1,
RC ECO:0000313|Proteomes:UP000181967};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000548,
CC ECO:0000256|RuleBase:RU361134};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; CP014864; AMX03479.1; -; Genomic_DNA.
DR EMBL; FOKT01000013; SFD13936.1; -; Genomic_DNA.
DR RefSeq; WP_067155736.1; NZ_JAPHQD010000009.1.
DR AlphaFoldDB; A0A143HP38; -.
DR STRING; 252514.A3224_13645; -.
DR GeneID; 76609078; -.
DR KEGG; mthd:A3224_13645; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000076077; Chromosome.
DR Proteomes; UP000181967; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR Gene3D; 2.60.40.3620; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
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 Pfam; PF02806; Alpha-amylase_C; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..568
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013476380"
FT DOMAIN 30..369
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 378..460
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 568 AA; 61742 MW; 38C57D06EDC6F68E CRC64;
MKKPQGFRCW LSGVGLALGA LSAGNASAGT AFVHLFEWRW NDIASECENF LGPKGFDAVQ
ISPPQEHISL DTWWARYQPV TYTNLTSRSG TEAELASMIQ RCHAAGVKVY ADMVINHTAA
WNQGGTGWGG TPWSVTNHPE FSPQDYHSDC TVSNYGDAYN VWNCRLSGLP DLNTGSGYVQ
DRLAAYFNKL KGMGVDGFRV DAVKHMAPGD LQAILNKAGN PWVFSEVIGA AGEAAEIQPG
NYTYLGHVTE FKYGTDLASN FNGQIKYLAS IGESWGLLPS YKAVNFVDNH DRERGHGGGG
NLTYKDGAKY NLANVFMLAH PYGYPKVMSG YRFTNTDIGP PATGPQGCTN SAWVCQHRWG
NIANMVGFRN FVDGTAMTNW WDNGNNQIAF GRGNKGFVVI NNESGQLNQT LYTGLPAGEY
CNVLAGDDAC SGHMITVDGK GYATFNIAAN SAAAIHGGAV AAPCRECAAQ NFPQLYFRGT
ANGWGVDTMA LVADHTWQIS VSFDGQADQR FKFDVYGDWR QNYGDSGADG TLDRTGADIY
TPVVGDYLVE VNDRTMTYSL HCLECGEY
//
