ID A0A124H886_9ACTN Unreviewed; 1803 AA.
AC A0A124H886;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN ORFNames=AQI70_02675 {ECO:0000313|EMBL:KUM82230.1};
OS Streptomyces curacoi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM82230.1, ECO:0000313|Proteomes:UP000054024};
RN [1] {ECO:0000313|EMBL:KUM82230.1, ECO:0000313|Proteomes:UP000054024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM82230.1,
RC ECO:0000313|Proteomes:UP000054024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT the species Streptomyces curacoi.";
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:KUM82230.1}.
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DR EMBL; LMWJ01000001; KUM82230.1; -; Genomic_DNA.
DR RefSeq; WP_062143504.1; NZ_KQ947984.1.
DR STRING; 146536.AQI70_02675; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000054024; 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:0043169; F:cation 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; IPR006048; A-amylase/branching_C.
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; PF02806; Alpha-amylase_C; 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:KUM82230.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KUM82230.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1803
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038400991"
FT DOMAIN 67..527
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1803 AA; 194477 MW; CA940C262BD16410 CRC64;
MIPRWPVPSR RRTAYAGRVA AVTVTALAAA LVQPLAARAE TPPAPPSDAK LAAEPARHDS
TREQFYFVLP DRFANGDTGN DKGGLTGSRL ATGYDPTDKG FYQGGDLKGL TRKLDYIKGL
GTTSIWMAPI FKNQPVQGTG SNASAGYHGY WITDFTQVDP HFGSNKDLQT LISKAHAKGM
KVYFDVITNH TADVVDYQEK SYDYLSKGAF PYLTKDGRPF DDADYADGTR KFPAVDADSF
PRTPAAPAAK KDLKVPSWLN DPTMYHNRGD STFAGESSAH GDFSGLDDLW TERPEVVSGM
EKIYQRWVRD FDIDGFRIDT VKHVNMEFWT QWATALDSYA AKKGRDDFFM FGEVYSADTN
VTAPYVTQGR LDATLDFPFQ EAARQYASQG GSARKLAGVF GDDYKYTTDK ANAYEQVTFL
GNHDMGRIGY FLNQDNPKAT DAELLKKDRL ANELMFLSRG NPVVYYGDEQ GFTGAGGDKD
ARQTLFASKT ADYLDDDQLG TDRTHASDAY DPSAPLYRQI SALSKLRKAH PALADGVQTE
RYAADGAGVY AFSRTDARKG IEYVVAFNNA DEAKTATFAT GSAGMAFKGI YGTDDSVRSD
ADKKLTVTVP AGSAIVLKAA GRLAEPAAEP TLTLRAPATG ATGTVEIGAD VDGGQLNRVV
FAAQVGNGKW KTLGSADHAP YKVTQTIGKD VPAGTALRYK AVVIDSAGRT ASATAASTTG
TPPAPETPTA SSRDHAIVHY KRTDGDYANW GLYAWGDLAD GESTNWPDSH PFIGRDAYGA
FAYVKLKPGA SSVGFLVIDK DGNKDVSADR TIDVTRTGEI WIEQGKEAVR TERPAADYPA
PDKTKAVLHY HRADGDYDGW GLHVWTGAAN PTDWSNSLKP VKTDPYGAVF EVPLTDGATS
LSYIIHKGDE KDLPADQSLD LTANGHEVWL VSGQEKYLLP QPAGSAAALD LTTSKAVWID
RNTLAWNGSE GAASTQLLYS RTGSIEVKDG ALTGDDARWL RLSRTSLTDA QQAKFPHLKD
YAAWSVDPRD RDRVREAVRG QLVASQRAAN GAVLAATGVQ IAGVLDDLYS GATKSDLGPT
FAKGRPTLAV WAPTAQSVEL EIGDSTVAMK RDGTTGVWSV TGPRSWKNKP YRYVVEVWAP
GVRKVVTNKV TDPYAVALTA NSRRSLVVDL DDRSLAPSGW SSYTKPKAVP LKDAQIQELH
IRDFSVADRT AKHPGTYLAF TDKASDGSRH LRELAKAGTS YVHLLPAFDI ATIPEKKSEQ
ATVDCDLASF PADSDRQQEC VSKIAAKDAF NWGYDPYHYT VPEGSYATDP DGTARTVEFR
KMVKALNDDG LRVVMDVVYN HTAASGQADT SVLDRIVPGY YQRLLADGSV ANSTCCANTA
TENAMMGKLV VDSVVTWAKE YKVDGFRFDL MGHHPKANIL AVRKALDALT VEKDGVDGKK
IILYGEGWNF GEVADDARFV QATQKNMAGT GIATFSDRAR DAVRGGGPFD EDPGIQGFAS
GLYTEPNSST NNGTPAEQKA RLLHYQDLIK VGLSGNLAGY RFTDTSGKEV KGSEVDYNGA
PAGYADAPGD ALAYADAHDN ESLFDALAYK LPASTSAADR ARMQVLAMAT ATLSQGPALS
QAGTDLLRSK SLDRNSYDSG DWFNAIHWNC ADGNGFGRGL PMAADNAAKW PYAKPLLSTV
KVGCEQIEGA SAAYRDLLRI RATESAFSLD TAGQVQSKLS FPLSGKDETP GVITMRLGDL
VVVFNATPEK QEQRIVSLAD EGYRLHPVQA SGADSIVKSS SFEGKTGTFA VPGRTVAVFS
RAL
//
