ID A0A0J7AIU7_9ACTN Unreviewed; 1783 AA.
AC A0A0J7AIU7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=ACS04_15180 {ECO:0000313|EMBL:KMO97016.1};
OS Streptomyces roseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO97016.1, ECO:0000313|Proteomes:UP000035932};
RN [1] {ECO:0000313|EMBL:KMO97016.1, ECO:0000313|Proteomes:UP000035932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO97016.1,
RC ECO:0000313|Proteomes:UP000035932};
RA Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA Barona-Gomez F.;
RT "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT hidden chemical diversity on bacterial genomes.";
RL Submitted (JUN-2015) 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 -!- 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}.
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:KMO97016.1}.
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DR EMBL; LFML01000056; KMO97016.1; -; Genomic_DNA.
DR RefSeq; WP_048477119.1; NZ_LFML01000056.1.
DR STRING; 66430.ACS04_15180; -.
DR PATRIC; fig|66430.4.peg.5704; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000035932; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11339; AmyAc_bac_CMD_like_2; 1.
DR CDD; cd11341; AmyAc_Pullulanase_LD-like; 1.
DR CDD; cd10315; CBM41_pullulanase; 2.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR Gene3D; 2.60.40.1110; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR005323; CBM41_pullulanase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
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 InterPro; IPR011839; Pullul_strch.
DR InterPro; IPR024561; Pullul_strch_C.
DR InterPro; IPR040671; Pullulanase_N2.
DR NCBIfam; TIGR02103; pullul_strch; 1.
DR PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF03714; PUD; 2.
DR Pfam; PF11852; Pullul_strch_C; 1.
DR Pfam; PF17967; Pullulanase_N2; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:KMO97016.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KMO97016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035932};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1783
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005285854"
FT DOMAIN 53..514
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1783 AA; 190494 MW; EBE4F49D54197E6E CRC64;
MIRPAAGAIA AALAVTLLPA LPAAAAAPPA PPSDAKLAAE PARHDLTRDQ FYFVLPDRFA
NGDPRNDTGG LTGSRLETGL DPTDKGFYQG GDLKGLTDRL DYIKGLGTTA IWMAPIFKNQ
PVQGKGAGEV SAGYHGYWIT DFTQVDPHFG TNADLERLID KAHAKGMKVF FDVITNHTAD
VVDYREQSYS YLSKGAFPYL TKDGVPFEDS DYADGKRTFP RVDTGSFPRT PFVPDAKKNL
KAPAWLNDPT MYHNRGDSTF AGESSDQGDF FGLDDLWTER PEVVSGMEKI YEKWVKDFSI
DGFRIDTVKH VNTGFWTQWA TALDKYAAQR GRKNFFMFGE VYSADTAVTS PYVTQGRLDA
TLDFPLQDAI RAYASQGAGA PRLGSVLADD YRYTTDKANA YEQVTFLGNH DMGRFGTFLK
QDRPGAGEQE LLDRYRLANE LMFFSRGNPV IYSGDEQGFT GAGGDKDARQ PLFATKIADY
LDDDQLGTVR THASDAYDPG HPLYQQISAL SKLTKEHPAL RDGVQSERLA DGSVYAFART
DTRSRTEYLV AANNAAEART VELDAPAGAQ YRTLYGGTAL LRASSAGKLT VTVPALGSVV
LQGAAPLAAP AAKPALTLKA PAAGAAGTVE LSAEVTGGGL NRVVFAAQTG TGTWQVLGSA
DHAPYKVTQH IDATTPAGPA LRYKAVVVDA SGRTASALAE SVSGLTPPSP VPTATQRDYA
VVHYRRADGD YTNWRLYAWG DLADGEATPW PAGHDFTGRD AYGAFAYVRL KPGASSVGYL
VIDKDGNKDV TADRTLDVTK SGEVWLEQGK VAATTDRPAY PPQDQAKAVL HYQRPDGAYD
GWGLHVWTGA ANPTDWSKPL MPARTDSYGA VYEVPLAAGA TSLGYILHKG DEKDLPTDQS
LDLKATGHEV WMLGGRAPYL LPQPAGSSAA LDLTKSEAVW IDRDTVAWNA PAAAASTELL
ASREGTVTAA DGVLHADGAQ WLRLARAELT AAQKQKFPHL ATYAAFTVDP RDRGRVREAL
RGQLVASART ANGAVLAATG VQLAGVLDDL YANNAPLGPV FKDGRPTLSV WAPTARQVAL
ELDGRTVPMR RDDATGVWSV RGERGWSGKP YRYAVTVWAP STGRMVHNRV TDPYSTALTT
DSTYSLAVDL ADPKLAPPGW RGLRKPAPVP FTSAQIQELH IRDFSVADPT STHPGQYLAF
TDTASAGMRH LRELAASGTS YVHLLPAFDI GTIPEKASDR TEPACDLSVY APDSPEQQAC
VAAAAAKDAY NWGYDPLHYT VPEGSYASDP NGTARTVEFR RMVQSLNGAG LRTVMDVVYN
HTVAAGQSDK SVLDRIVPGY YQRLLADGSV ATSTCCANTA PENAMMGRLV VDSIVTWAKE
YKVDGFRFDL MGHHPKANIL AVRQALDALT VAKDGVDGKK IILYGEGWNF GEVADDARFV
QATQKNMAGT GIATFSDRSR DAVRGGGPFD EDPRVQGFAS GLFTAPNASP ANGTADQQRA
RLLHAQDLIK VGLSGNLASY AFTDSAGKPT KGSEVDYNGS PAGYAAAPGD ALAYADAHDN
ETLADALAYK LAPGTSAPDR ARMQVLAMAV GTLSQGPSLS QAGTDLLRSK SLDRNSYDSG
DWFNAIHWDC RQGNGFGRGL PPAADNGSKW VYAKPLLAAG KAPGCAEITG ASAAYRDLLR
IRTTEPAFAL TTPAAVQAAL AFPLSGKDET PGVITMTLGD LVVVFNATPA AQSQRVPALA
GTAYTLHPAQ AAGSDAAVRQ AAYDVRTGEF TTPPRTVAVF KRP
//
