ID A0A2A9E2L8_9MICO Unreviewed; 627 AA.
AC A0A2A9E2L8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=ATL42_0278 {ECO:0000313|EMBL:PFG32439.1};
OS Sanguibacter antarcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC Sanguibacter.
OX NCBI_TaxID=372484 {ECO:0000313|EMBL:PFG32439.1, ECO:0000313|Proteomes:UP000225548};
RN [1] {ECO:0000313|EMBL:PFG32439.1, ECO:0000313|Proteomes:UP000225548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18966 {ECO:0000313|EMBL:PFG32439.1,
RC ECO:0000313|Proteomes:UP000225548};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFG32439.1}.
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DR EMBL; PDJG01000001; PFG32439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9E2L8; -.
DR Proteomes; UP000225548; 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 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; IPR005085; CBM25.
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; PF03423; CBM_25; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM00632; Aamy_C; 1.
DR SMART; SM01066; CBM_25; 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:UP000225548}.
FT DOMAIN 86..431
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 440..520
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT DOMAIN 533..611
FT /note="Carbohydrate binding module family 25"
FT /evidence="ECO:0000259|SMART:SM01066"
SQ SEQUENCE 627 AA; 65896 MW; 5B14DA55FD458FBE CRC64;
MTRQLMAAPR SRGRSNHWSV RRWSTQSTAL LTAGALAASA LLGGALTPLA PASAAPMATV
QPAVASPVLT SPVLVSAAPT VPGRGNTAVN MFQWTWNAIA SECTSTLGPA GYAYVQTSPP
QEHIRGTAWW TSYQPVSYKL ESKLGTRTEF KAMVDTCDAA GVKIIADTVI NHMTGADGGS
GTGFAGTPYG IESFPGPDGG YGPNDFNDCK TNISNYSDRY QVQNCRLVSL QDLKTGSDYV
RSEIAAYLND MINLGVVGFR IDAAKHIPAG DLAAIKGKLT NPNVFWVHEV IGAAGEPIQP
SEYLGSGDSH EFNYARTLKS RFDGRIADLR SISNGLLASD RAGVFVDNHD TERNGETMNY
KWGAKYKLAN VFMLAYPYGW PTVYTGYTFS DKDAGAPQQG DGQVIDASCS NTATWTCAHR
WPEIKNMVGF RTAVGTEAVT SWWDNGNNQI AFGRGSKGYV AINNEASAVT RTFQSSLPAG
TYCDVVAGDG CTKTVSVNGS GQLTATIPAY GALALHVGAL SGGTGGPGDP DPATKLAVYY
STNKGWSAYN VHYKVGSGAW TTVPGKAMSA ACTGWVSTTI ATSGATVTAA FNNGSGTWDN
NGSKDYTLTG ATAAVKDGTV TTTDPCA
//
