ID A0A117S2V8_9ACTN Unreviewed; 1794 AA.
AC A0A117S2V8;
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=AQJ91_00595 {ECO:0000313|EMBL:KUO23105.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO23105.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO23105.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO23105.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
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:KUO23105.1}.
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DR EMBL; LMXB01000007; KUO23105.1; -; Genomic_DNA.
DR RefSeq; WP_067014538.1; NZ_KQ949075.1.
DR STRING; 909626.AQJ91_00595; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000053260; 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; 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:KUO23105.1};
KW Nucleotide-binding {ECO:0000313|EMBL:KUO23105.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..1794
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007156001"
FT DOMAIN 67..523
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1794 AA; 193577 MW; 0B995C7207E7B795 CRC64;
MIPRWPAPSR RRTTHAGRVA AVTVTALAAA LVQPLAAQAD TPPPPPSDAR LAAEPARHDA
TREQFYFVLP DRFANGDTGN DRGGLTGSRL ATGYDPTDKG FYQGGDLKGL TKRLDYIKGL
GTTSIWMAPI FKNRPVQGEG TNASAGYHGY WITDFTQVDP HFGTNKDLQT LISKAHAKGM
KVYFDVITNH TADVVDYEEK SYDYLAKGAF PYLTKDGEPF DDADYAGTAD FPEVDADSFP
RTPKVTSNPK VPSWLNDPTM YHNRGDSTYA GESTTYGDFS GLDDLWTERP EVVKGMGRIY
QRWVRDFDID GFRIDTVKHV NMEFWTQWAT ALDAYAAKKG RDDFFMFGEV YSADTNITSP
YVTQGRLDAT LDFPFQEAAR QYASQGGSAR KLASVFGDDY KYTTDKANAY EQVTFLGNHD
MGRIGYFLGQ DNPKATDAEL VKKAELANEL MFLSRGNPVV YYGDEQGFTG AGGDKDARQT
LFASRTADYL DDDQLGTDRT HASDAYDTSA PLYEQIAALA ELRKANPALT DGLQTERYAA
EGAGVYAFSR TGTDKTEYVV AFNNAGEAKS ATFATGSADM TFRGIHGTDA TLKSDADKRI
TVTVPAGTAV VLKAAGKLAK PATRPTVTLK APDTGATGTV ELTAHVDGGQ LNRVVFAAQV
GNGKWRTLGS GDHAPYKVTQ TIGTDVPAGT ALRYKAVVID SAGRTASALA ASTTGTPPAP
ETPTASSRDH AIVHYKRTDG DYGDWGLYAW GDLADGESTE WPDSHPFTGR DAYGAFAYVK
LKPGASNVGF LVIDKDGNKD VSADRAIDVT QTGEVWIEQG KADVRTERPE YPAQDKTKAV
LHYHRADGNY DGWGLHVWTG AANPTEWSNP LKPVKTDTYG AVFEVPLTEG ATSLSYIIHK
GDEKDLAADQ SLDLKATGHE VWLLNGQEKY LLPQPAGAAA ALDLTTSKAV WVDRNTVAWN
GSEAAASTQL LYSRDGSIAV EDGALTGDAK WLRLSRTTLT DAQKAKFPHL GDYAAWTVDP
RDRDRVREAL SGQVVASQRA ANGAVQAATG VQIAGVLDDL YDAASAKLGP TFRDGRPTLA
VWAPTAQSVK LEVGDSTVAM KRNDTTGVWS VTGPRSWKNK PYRYVVKVWA PSVRKVVTNK
VTDPYSVALT ADSERSLVVD LNDRSLAPSG WSGLGKPKAV PLKDAQIQEL HIRDFSVEDR
TAANPGTYLA FADKDSDGSK HLRELAASGT SYVHLLPAFD IATIPEKPSD QATVDCDLAA
YPADSDQQQE CVAKIAAKDA YNWGYDPYHY TVPEGSYATD PDGTRRTVEF RKMVKALNED
GLRVVMDVVY NHTAAGGQAE TSVLDRIVPG YYQRLLADGS VANSTCCANT ATENAMMGKL
VVDSVVTWAR EYKVDGFRFD LMGHHPKANI LAVRKALDAL TLAKDGVDGK KIILYGEGWN
FGEVADDARF VQATQKNMAG TGIATFSDRA RDAVRGGGPF DEDPGIQGFA SGLYTDPNSS
TSNGTSEEQR ARLLHYQDLI KVGLSGNLAK YRFTDTGGKE VTGAEVDYNG APAGYADAPG
DALAYADAHD NESLFDALAF KLPKGTSAAD RARMQVLAMA TATLSQGPAL SQAGTDLLRS
KSLDRNSYDS GDWFNAIHWT CADGNGFGRG LPMAADNASK WPYAKPLLGT VKVGCEQIEG
TSAAYQDLLR LRTTESVFSL DTAGQVQSKL SFPLSGKEET PGVITMELGD LVVVFNATPE
TQEQRIVSLA GRNYRLHPVQ ASGADPIVKG SAYQEESGTF AVPGRTVAVF SRAV
//
