ID Q82AS4_STRAW Unreviewed; 1806 AA.
AC Q82AS4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 133.
DE RecName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000256|ARBA:ARBA00030238};
GN Name=amyX {ECO:0000313|EMBL:BAC73694.1};
GN ORFNames=SAVERM_5982 {ECO:0000313|EMBL:BAC73694.1};
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=227882 {ECO:0000313|EMBL:BAC73694.1, ECO:0000313|Proteomes:UP000000428};
RN [1] {ECO:0000313|EMBL:BAC73694.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [2] {ECO:0000313|EMBL:BAC73694.1, ECO:0000313|Proteomes:UP000000428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC NRRL 8165 / MA-4680 {ECO:0000313|Proteomes:UP000000428};
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
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};
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DR EMBL; BA000030; BAC73694.1; -; Genomic_DNA.
DR SMR; Q82AS4; -.
DR KEGG; sma:SAVERM_5982; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_000910_0_0_11; -.
DR OMA; TREQFYF; -.
DR Proteomes; UP000000428; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF209; PERIPLASMIC ALPHA-AMYLASE; 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; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000428};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..1806
FT /note="1,4-alpha-D-glucan glucanohydrolase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004298684"
FT DOMAIN 70..530
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1806 AA; 194325 MW; 58AF920DCB9F63BA CRC64;
MDLIPRGSAP RTRRTHRHSR TAAAVAAAAL AVSLAQPLEA RAATPPAPPS DAKLAAEPAR
HDATREQFYF VMPDRFANGD TSNDKGGLTG SRLSTGYDPT DKGFYQGGDL KGLTRKLDYI
KGLGTTSIWL APIFKNQPVQ GTGKDASAGY HGYWITDFTK VDPHFGTNKD LETLISKAHA
KGMKVFFDVI TNHTADVVDY EEKSYGYLSK GAFPYLTKDG RPFDDAGYTD GPRKFPAVDG
DSFPRTPAVA ARKKNAKVPS WLNDPTMYHN RGDSTFAGES STHGDFSGLD DLWTERPEVV
RGMEKIYEKW VRDFGIDGFR IDTVKHVNTE FWTQWATALD AYAKKRGKDD FFMFGEVYSA
DTSVTSPYVT QGRLDSTLDF PFQDAARSYA SQGGSAKKLA SVFGDDYKYT TDKANAYEQV
TFLGNHDMGR IGYFLNQDNP KATDAELLRK DRLANELMFL SRGNPVVYYG DEQGFTGSGG
DKDARQTMFA SKVADYLDDD EIGTDRGHAS DAYDTSAPLY KEIAALSKLR KDNPALADGI
QTERYAADGA GVYAFSRTDA RTGTEYVVAV NNADKASAAT FATGSADTAF KGIHGTDDVL
KSDADKKITV TVPAGAAVVL KAAGRPGTPA AKPSLTLKAP DAGATGTVEL SADVDGGRLN
RVVFAAQVGN AKWRTLGSAD HAPYRVTQTI GKDVPAGTAL RYKAVVIDAA GRTASATAAS
TTGTPPAAET PTASSRDYAI VHYKRPDGDY TDWRLYAWGD LADGESTTWP AGHDFVGRDA
YGAFAYVKLK PGASTVNFLV IDKDGDKDVS ADRTIDVTKA GEVWVEQGKE TVRTERPDYP
AQDKTKAVIH YHRADGDLTG WGLHVWTGAA TPTDWSKPLE PVRTDAYGAV FEVPLTDGAT
SLSYIIHKGD EKDLSADRSL DLTADGHEVW LLNGQENHLL PQPAGSAAAL DLTTSKAVWI
DRNTVAWNGS DAAASTQLLS SRDGSIAVKD GSLTSDDERW LRLSKTSLTD AQKAAFPHLK
SYTAWSVDPR DRDRVREALA GQVVASQRAA NGAVLAATGV QLAGVLDDLY DATKADLGPT
FRGGHPTLAV WAPTAQSVSL ELDGAHVRMK RNNATGVWSV TGPASWKGKP YRYVVKVWAP
TVRKVVTNKV TDPYSVALTT DSERSLVVDL DDRSLAPSGW SSLKKPKAVP LRDAEIQELH
IRDFSVADRT VPAKDRGTYL AFTDKNSDGS RHLRQLAESG TSYVHLLPAF DIATIAEKKS
GQQATDCDLA SYAADSEKQQ ECLTAVAAKD AYNWGYDPYH YTVPEGSYAT DANGTRRTVE
FRRMVKSLNQ DGLRVVMDVV YNHTAAAGQA GTSVLDRIVP GYYQRLLADG SVATSTCCAN
TATENAMMGK LVVDSLVTWA KEYKVDGFRF DLMGHQPKAN ILAVRKALDA LTVAKDGVDG
KKIILYGEGW NFGEVADDAR FVQATQKNMA GTGIATFSDR ARDAVRGGGP FDADPGVQGF
GSGLYTDPNS SDANGTPAEQ KARLLHYQDL IKVGLSGNLA KYRFTDSSGK EVTGSEVDYN
GTGAGYADAP GDALAYADAH DNESLYDALT YKLPKGTPAG DRARMQVLAM ATAALAQGPS
LSQAGSDLLR SKSLDRNSYD SGDWFNAIHW NCQDGNGFGR GLPMAADNKS KWPYATPLLT
SVKVGCDQIE GTSAGYQDLL RIRTTEPDFS LSTAGQVQSK LTFPLSGKDE TPGVITMKLG
DLVVVFNATP DQQEQTVAAL AGKDYALHPV QAAGADPIVK SASYTAKSGM FAVPGRTVAI
FSQVAR
//