GenomeNet

Database: UniProt
Entry: Q82AS4_STRAW
LinkDB: Q82AS4_STRAW
Original site: Q82AS4_STRAW 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system