ID D9VT87_9ACTN Unreviewed; 1332 AA.
AC D9VT87;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
DE Flags: Fragment;
GN ORFNames=SSNG_02073 {ECO:0000313|EMBL:EFL14821.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL14821.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL14821.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL14821.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; GG657750; EFL14821.1; -; Genomic_DNA.
DR STRING; 253839.SSNG_02073; -.
DR eggNOG; COG0366; Bacteria.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_5_0_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0051060; F:pullulanase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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; 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; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 2.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF49452; Starch-binding domain-like; 2.
PE 3: Inferred from homology;
FT DOMAIN 269..361
FT /note="Pullulanase carbohydrate-binding module 41"
FT /evidence="ECO:0000259|Pfam:PF03714"
FT DOMAIN 378..469
FT /note="Pullulanase carbohydrate-binding module 41"
FT /evidence="ECO:0000259|Pfam:PF03714"
FT DOMAIN 485..599
FT /note="Pullulanase N2"
FT /evidence="ECO:0000259|Pfam:PF17967"
FT DOMAIN 606..685
FT /note="Glycoside hydrolase family 13 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02922"
FT DOMAIN 1183..1329
FT /note="Alpha-1,6-glucosidases pullulanase-type C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11852"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..125
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFL14821.1"
SQ SEQUENCE 1332 AA; 143470 MW; 9208910700076D63 CRC64;
QGRPPAAVRH PRRRLPGRRP ARNGAHTRER CIRSGAPALH PDQCSLEADQ GPPGPARRHP
ERAPRRRLRV RLRPHRPQDP YRVPGRRQQQ RHRPYRRGRR PARRLLPAPV RRHRPRRHPL
RGPRPRHSLP GRQAHPEPAR PRHPGPPGHR PPARPRRAAL CSPLRPPPPA PLCTVELSAD
VTPGAGPGAL TRVVFAAQTG TGKWQVLGSA DHAPYKVTQT TDPATAAGTP LRYKAVAVDS
AGRTASALAA STTGQTPPPA PPTATQRDYA VVHYNRPDGD YANWRLYAWG DLADGEATPW
PEGHPFTGRD AYGAFAYVRL KPGASSIGYL VIDKDGNKDV AADRTLDLTK TGEIWLEQGR
EPARTDRPAY PPQDQAKAVL HYQRPDGAHD GWGLHVWTGA ATPTDWSKPL LPTRTDSYGA
VYEVPLAPGA TSLSYILHKG DQKDLPTDQS LDLKATGHEV WLLAGREKHL LPQPAGSSAA
LDLTKAEAVW IDRDTLAWNA PQTAASLQLL ASRDGRITTD GGVLHGAGAP WLRLNRSALT
PAQKQKFPHL AAYTAYTVDP RDRDRVREAL RGQLVASARA ANGAVLAATG VQLAGVLDDL
YANNSPLGPV FKDGRPTLSV WAPTAQQVAL ELDGRTVPMR RDDTTGVWSV RGDRSWTGKP
YRYAVTVWAP STRQIVRNLV TDPYSTALTT DSTHSLAVDL ADPKLAPPGW KELRKPAPVP
FTSAQIQELH IRDFSIADAT AKHPGQYLAF TDTGSDGMRH LRELAAAGTS YVHLLPAFDF
GTVPEDPKAR TEPACDLKAH APDSEQQQAC VAAAAAKDGF NWGYDPLHYT VPEGSYASDP
NGTARTVEFR RMVQSLNGAG LRTVMDVVYN HTVASGQSDK SVLDRIVPGY YQRLLADGSV
ATSTCCSNTA PENAMMGRLV VDSVVTWARQ YKVDGFFFDL MGHHPKANVL AVRKALDELT
VAKDGVDGKK IVLYGEGWNF GEVADDARFV QATQKNMAGT GIATFSDRAR DAVRGGGPFD
EDPRVQGFAS GLFTDPNGSP ANGTPAEQRA RLLHAQDLLK VGLSGNLASY AFTDSAGRRT
TGSGVDYNGA PAGYAAAPGD ALAYADAHDN ESLYDALAYK LPAGTPTADR ARMQVLAMAT
AALSQGPALS QAGTDLLRSK SLDRNSFDSG DWFNALHWDC RDGNGFGRGL PPAADNRAKW
PWAKPLLTGP APGCAEITAA SGAYRDLLRI RTTEPAFALT TAEAVQQRLS FPLSGPEETP
GVLTMALGDL VVVFNATPAD QRQRVPALAG TGYALHPVQA AGSDPAVKRS AYDPATGEFT
APARTVAVFK RG
//
