ID K4KJZ3_SIMAS Unreviewed; 469 AA.
AC K4KJZ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN OrderedLocusNames=M5M_06775 {ECO:0000313|EMBL:AFU98550.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU98550.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU98550.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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|RuleBase:RU361134};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; CP003746; AFU98550.1; -; Genomic_DNA.
DR AlphaFoldDB; K4KJZ3; -.
DR STRING; 1117647.M5M_06775; -.
DR KEGG; saga:M5M_06775; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_029247_2_0_6; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000000466; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11315; AmyAc_bac1_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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 PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..469
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003878367"
FT DOMAIN 31..385
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 469 AA; 52621 MW; FE034F2ECB1D433E CRC64;
MNKKVLSGWR NALKSTAVAA SLCIPSLACA DVILHAFNWS YTDVKNKASE ISSIGYKAVL
VAPPLKSAKN GCEWWQRYQP QDWRVIDHCL GNKESFKAMI DALQAKGVVV YADIVLNHMA
NERNGATDFP GNSTLVDYAN NRTYWNKQKL FGNLDNGLLS PWDFHEAKCI SNYNDVWQVQ
NWRICGAYPD KGLPDLNPNS YVVDQQRAYL QALKNLGVKG FRVDAAKHMT NWHMNQIFTS
SIKSGMHVFG EVITGGGTSS SDYQQFLGPY LSGTDHDAYD FPLLNAMRNA LQPNGWMSSL
DNPVAGGNAL PGDRAVTMPI THDIPTNAGF RYLIMNTTDE HLAYAYVLGR KDGAPMVFSD
QTGTDGGRWV NDYKQSDIKA MVKFHNRVKG QGQEGIWADQ CVLAFRRGKE GVVGINKCGE
EKWIKLNTNE KYYWYRNYTD VFSGETFSID ASVKWIRIPP RAARMWTAS
//
