ID K4KI64_SIMAS Unreviewed; 663 AA.
AC K4KI64;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN OrderedLocusNames=M5M_08225 {ECO:0000313|EMBL:AFU98834.1};
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:AFU98834.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU98834.1, 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|ARBA:ARBA00000548};
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; CP003746; AFU98834.1; -; Genomic_DNA.
DR RefSeq; WP_015046999.1; NZ_ATUQ01000002.1.
DR AlphaFoldDB; K4KI64; -.
DR STRING; 1117647.M5M_08225; -.
DR KEGG; saga:M5M_08225; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_369072_0_0_6; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000000466; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 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; 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 InterPro; IPR014756; Ig_E-set.
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; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000466};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..663
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003878327"
FT DOMAIN 26..363
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 373..455
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
SQ SEQUENCE 663 AA; 72163 MW; 8CF893F202219831 CRC64;
MKTSIPLIGA LAFAASSFSS VASAGTAFVH LFEWKWDDIA TECESFLGPK GFDAVQVSPP
HEHTAGPYWW TRYQPVSYNN LTSRSGNETQ FKNMVNRCNA AGVKIYVDVV MNNWASYQGH
GNVASGGSSW TPRNYPELSG QDFHSDCTIS NYGDANNVWD CGLYGMPDLN TGASYPQDYV
ANYMKRLTSW GVAGFRIDAA KHIRPSELDT VMAKAQRPWA FLEVIGAAGE AVQPGQYTYI
GPVTEFKYGT DLAANFNGQI KNLKTLGPSW GLQASDKAVV FVDNHDRERG HGGGGNLTYK
EGTKYNLANV FMLAYPYGYP KVMSGYKFTD TDAGPPAGAT NCSNSEWVCQ HRWGNIANMV
EFRNFTVGAW SVNNWWDNGA NQIAFSRGDK GFVVINNESY ALSQTLYTGL PAGNYCNVLA
GADKCSGDVI SVAANGYATF NVPANAAAAI HGGALAGGGC VTDCPPVSNV PSLNVRGTFN
GWGNLPMTLV ADNTWQATFT LNGQANQRFK VDVYGDWSLN YGDNGADGVL DQTGADIYTT
ASGEFRLTVN DQTMRYTLEQ VGQCNACFAG NFSQMYFRGT ANNWSATPMA LVANNVWELV
VNFDGQSNQR FKFDVNADWS HNYGDNGANG SLERTGADIF TNLVGQYRVR MNDQAMTYSI
QPL
//
