ID A0A1M4WH09_9GAMM Unreviewed; 577 AA.
AC A0A1M4WH09;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SAMN04487965_0690 {ECO:0000313|EMBL:SHE80516.1};
OS Microbulbifer donghaiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=494016 {ECO:0000313|EMBL:SHE80516.1, ECO:0000313|Proteomes:UP000184170};
RN [1] {ECO:0000313|EMBL:SHE80516.1, ECO:0000313|Proteomes:UP000184170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7063 {ECO:0000313|EMBL:SHE80516.1,
RC ECO:0000313|Proteomes:UP000184170};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQVA01000001; SHE80516.1; -; Genomic_DNA.
DR RefSeq; WP_073271443.1; NZ_FQVA01000001.1.
DR AlphaFoldDB; A0A1M4WH09; -.
DR STRING; 494016.SAMN04487965_0690; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000184170; 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:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR CDD; cd05810; CBM20_alpha_MTH; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR006048; A-amylase/branching_C.
DR InterPro; IPR031319; A-amylase_C.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
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 Pfam; PF00686; CBM_20; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 1.
DR PROSITE; PS51166; CBM20; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..577
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009908104"
FT DOMAIN 476..577
FT /note="CBM20"
FT /evidence="ECO:0000259|PROSITE:PS51166"
FT REGION 553..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 62206 MW; 7C6598CCF519E84D CRC64;
MRHLLAMMST LLLLSAFSAA SNAVPRTAFV HLFEWQWDDI ASECENFLGP KGFAAVQVSP
PQKSVSGSQW WTRYQPVSYA IEGRSGSRAQ FASMVSRCKA AGVDIYVDAV INHMAAWDRS
FPEVPYGPND FHNCTDDINY GDAWSIQNCD LVGLNDLKTE SDYVRGKIAD YMNDLIGLGV
AGFRIDAAKH MPAADINAIK SRLNGNPYIF QEVIGAGGEP IQAADYTWVG DVTEFNFTNT
IGHYFKLRGP LKEISNIGSW SGWLSSDNAI TFVANHDNQR QNTDNTITHK DGSNANNMAH
VFTLGWPYGY PKIMSSYDWS DHDQGPPAQG ASSCGNGWLC EHRSRPIANM VGFRNNTAAY
WGVTDYWDNG NHQMAWGRGG LGFVVLNMEG SNLNRSFQTG MPAGTYCDII HGDFDYSAGT
CSGPTITVDG SGNAAFNVYY RNAAAIHAGA KVGVPCPECG GNAGGETGGG SGGSSGGGSS
AVDVSFTCHN GYTYWGQSVY VVGNTGELGS WDPAQARKLD PAAYPTWSGS VDMPANTDVE
WKCLKREEAN PAAGVEWQSG SNNQFNTSTN SSPTAAF
//
