ID A0A0M9YV95_9ACTN Unreviewed; 1784 AA.
AC A0A0M9YV95;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-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=ADK55_04520 {ECO:0000313|EMBL:KOU67115.1};
OS Streptomyces sp. WM4235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415551 {ECO:0000313|EMBL:KOU67115.1, ECO:0000313|Proteomes:UP000037699};
RN [1] {ECO:0000313|EMBL:KOU67115.1, ECO:0000313|Proteomes:UP000037699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM4235 {ECO:0000313|EMBL:KOU67115.1,
RC ECO:0000313|Proteomes:UP000037699};
RA Noorani M.;
RL Submitted (JUL-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:KOU67115.1}.
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DR EMBL; LGDE01000024; KOU67115.1; -; Genomic_DNA.
DR RefSeq; WP_053676127.1; NZ_LGDE01000024.1.
DR PATRIC; fig|1415551.3.peg.984; -.
DR Proteomes; UP000037699; 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; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:KOU67115.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KOU67115.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037699};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1784
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005841921"
FT DOMAIN 54..514
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1784 AA; 191666 MW; 12B7485813DED31D CRC64;
MIRPAAGVIA ASLAVTLLPA LPASAASRPP APPSDAALAA EPARHDLTRE QFYFVLPDRF
ANGDPRNDRG GLTGSRLETG LDPTDKGFYQ GGDLKGLTDR LDYIKGLGTT AIWMAPIFKS
QPVQGAGADV SAGYHGYWIT DFTQVDPHFG TNADLERLID KAHRKGMKVF FDVITNHTAD
VIDHREASRG YLSKGAFPYL TKDGVPFDDS DHADGKRKFP ATDADSFPLT PVVPAAKKNV
KVPSWLNDPS MYHNRGDSTF AGESSEQGDF SGLDDLWTER PEVVDGMEKI YEKWVRDFDI
DGFRIDTVKH VNTGFWTQWA TALDAYAAKR GREDFFMFGE VYSADTAVTS PYVTRGRLDA
TLDFPLQDAI RAYASQGAGA SRLGSVLADD HRYTTDKANA YEQVTFLGNH DMGRFGTFLK
QDRPQAGERE LLDRYRLANE LMFLSRGNPV IYSGDEQGFT GAGGDKDARQ PLFASRTADY
LDDDQLGTAR THASDAYDPQ HPLYRQISAL AKLTRDHPAL RDGVQSARLD TDSVHAVART
DARTRTEYLV ASNNATGPRT VELDAPAGAG YRTLYGGTSP YAGTIRASAA GKLTVTVPAL
GSVVLRATAP LAPPATRPSL TLKAPAAGAT GTVELSAEVT GGSLNRVVFA AQAGAGKWQV
LGSADHAPYR VTQHVTAALG TPLRYKAVVV DSAGRTASAL AGSVAGQAPP APAPGATQRE
YAVVHYNRPD GDYADRRLYA WGDIAEGEAR PWPEGHAFSG RDAYGAFAYV RLKPGASSVN
YLVIDKDGNK DVAADRTVDV TRTGEIWLEQ GKEAARTERP AQPPQDTTKA VLHHQRPDGA
YDGWGLHVWA GAANPTDWSK PLRPTRIDSF GAVYEVPLAE GAQSLSYILH KGDEKDLPTD
QSLDLKATGH EVWMLGGKER YLLPQPAGSA AALDLTKAEA VWIDRDTVAW KAPEAAASLQ
LLASREGRIT VDDGALKEEG AAWLRLNRSE LTAAQKKKFP HLASYAAFTV DARDRDRVRE
ALRGQLVASA RAANGAVLAA TGVQLAGVLD DLYATTAALG PVFKDGRPTL SVWAPTARKV
SLELDGRTVA MRRDDATGVW SVRGERSWTG KPYRYDVTVW APSTRRMVRN LVTDPYSTAL
TTDSARSLAV DLADPKLAPA GWRNLKKPAP VPFTSAQIQE LHVRDFSVAD RTTTHPGQYL
AFTDTGSAGM RHLRDLAAAG TSYVHLLPAF DIGTIPEKPA DRTEPACDLK AYAPDSDQQQ
ACVSAAAAKD AYNWGYDPQH YTVPEGSYAS DPNGTARTVE FRRMVQSLNG AGLRTVMDVV
YNHTVAAGQS DKSVLDRIVP GYYQRLLPDG AVATSTCCAN TAPENTMMGR LVVDSIVTWA
KEYKVDGFRF DLMGHHPKDN ILAVRKALDG LTLAKDGVDG KRIVLYGEGW NFGEVADDAR
FVQATQKNMA GTGIATFSDR SRDAVRGGGP FDEDPGVQGF ASGLFTAPNS SPANGTPEQQ
RARLLHAQDL IKVGLTGNLA SYAFTDTTGR RIKGSELDYN GAPAGYAAAP GDALAYADAH
DNESLYDALT FKLPKGTPEA DKARMQVLAM ATATLSQGPA LSQAGTDLLR SKSLDRNSFD
SGDWFNAIHW DCRDGNGFGR GLPPAADNQP KWPYAKPLLT GPAPGCPEIT GTSAAHRDLL
RIRTTEPAFA LTTADAVQRT IGFPLSGTEE TPGVITMTAG DLVVVFNATP GVRSQRVADL
AGRGYALHPI QAAGSDATVK GSTYDTGTGQ FTVPARTVAV FKRG
//
