ID A0A101NR32_9ACTN Unreviewed; 1790 AA.
AC A0A101NR32;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=AQI88_06185 {ECO:0000313|EMBL:KUM97809.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM97809.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM97809.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM97809.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-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:KUM97809.1}.
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DR EMBL; LMWL01000008; KUM97809.1; -; Genomic_DNA.
DR RefSeq; WP_066993078.1; NZ_KQ948016.1.
DR STRING; 67285.AQI88_06185; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000054241; 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: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:KUM97809.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KUM97809.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1790
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007101845"
FT DOMAIN 56..513
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 698..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1790 AA; 192504 MW; 69DC966625AC9D19 CRC64;
MIPRARRAAA VTAVALAAAL IQPLAAHAAT PPAPPSDAAL AAQPARHDDT RDQFYFVMPD
RFANGDRSND RGGLTGSRLS TGYDPTDKGF YQGGDLKGLT KRLDYIKDLG TTAIWMAPIF
KNRPVQGTGS NASAGYHGYW ITDFTQVDPH FGTNKDLQTL ISKAHAKGMK VFFDVITNHT
ADVVDYEEKS SDYLSKGAFP YLTKDGRPFD DADYADGTRK FPAVSGASFP YTPEVTSNSK
VPAWLNDPTM YHNRGDSTYA GESTTYGDFS GLDDLWTERP EVVRGMEKIY ERWVRDFGVD
GFRIDTVKHV DLDFWTQWAT ALDKYAAAQG RKNFFMFGEV YSADTNITSP YVTQGRLDAT
LDFPFQDAAR AYASQGGSAQ KLASVFGDDY KYTTDKANAY EQVTFLGNHD MGRIGYFLKQ
DNPKATDAEI LRKDRLANEL MFLSRGNPVV YYGDEQGFTG SGGDKDARQT MFASKVADYL
DDDEIGTDRT HASDSYDTSA PLYKDIAALS RLRRADPALT DGVQTERYAA DGAGIYAFTR
TDAKTGAEYV VALNNAGEAK SATFATGSAG MSYQGIYGTD ATTKTDADRK LTVTVPAGSA
VVLKATGALA EPAAKPALTL KAPATGATGT VDVTAGVDGG QLNRVVFAAQ VGNGRWKTLG
SADHAPYKVT QAIGKDVPAG TALRYKAVVT DSAGHTASAL ASSTTGTPPA PEAPTASSRD
YAVVHYKRTD GDYGNWGLYA WGDLADGEST TWPNSHPFVG RDAYGAFAYV KLKPGASHVG
FLVIDKDGNK DVSADRSIDV TRTGEVWIEQ GKTDVLTEKP GSPAQDKTKA VIHYHRADGN
YDGWGLHVWT GAENPTDWSN PLKPVKTDAY GAVFEVPLTA GATSLSYIIH KGDDKDLPTD
QSLDLKSNGY EVWLLNGQEK YLLPQPAGSA AALDLTTSKA VWIDRNTVAW NGVDGAASTQ
LLYSHDGSIA VKDGALTSDD ERWLRLTKTT LSDAQKARFP HLKDYTAWSV DPRDRDRVRA
ALGGQLVASQ RAANGAVLAA TGVQIAGVLD DLYSGATKSE LGPVFHDGRP TLSVWAPTAQ
SVHLDLDGTA VKMRRNATTG VWSVTGPASW KGKPYRYVVK VWAPSVRKVV TNKVTDPYSV
ALTANSERSL VVDLNDRSLA PSGWSGLRKP KAVPLKDAQI QELHIRDFSV ADKTVPAKDQ
GTYLAFTDKN SDGSQHLRQL AKAGTSYVHL LPAFDIATIP EKKADQARTD CDLASYAADS
DKQQECVAKI AAKDAYNWGY DPYHYTVPEG SYATDPDGTA RTVQFRRMVQ ALNGDGLRVV
MDVVYNHTAA SGQADTSVLD RIVPGYYQRL LADGSVADST CCSNTAPENA MMGKLVVDSI
VTWAKEYKVD GFRFDLMGHH PKANILAVRK ALDALTPDKD GVDGKKIILY GEGWNFGEVA
NDARFVQATQ ANMAGTGIAT FSDRARDAVR GGGPFDSDPG VQGFASGLYT DPNTSTANGT
AAEQKARLLH YQDLIKVGLT GSLKSFTFTD SDGKEVKGSE VDYNGAPAGY ADAPGDALAY
VDAHDNESLF DALTYKLPKD TSASDRARMQ VLAMATAALS QGPALSQAGT DLLRSKSLDR
NSFDSGDWFN AIHWDCADGN GFGRGLPMAA DNQSKWSYAK PLLGTVKVGC PQITGASAAY
QDLLRVRTTE KAFSLGTAAQ VQDRLAFPLS GKEETPGVIT MQLGDLVVVF NATPERQDQR
ISALAGDHYR LHPVQESGAD PVVKTSSYAA GSGTFTVPAR TVAVFTRAAK
//
