ID A0A0W8IHH0_9MICO Unreviewed; 1907 AA.
AC A0A0W8IHH0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=pullulanase {ECO:0000256|ARBA:ARBA00024062};
DE EC=3.2.1.41 {ECO:0000256|ARBA:ARBA00024062};
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase {ECO:0000256|ARBA:ARBA00029618};
DE AltName: Full=Pullulan 6-glucanohydrolase {ECO:0000256|ARBA:ARBA00031076};
GN ORFNames=AVL62_07285 {ECO:0000313|EMBL:KUG59460.1};
OS Serinicoccus chungangensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG59460.1, ECO:0000313|Proteomes:UP000054837};
RN [1] {ECO:0000313|EMBL:KUG59460.1, ECO:0000313|Proteomes:UP000054837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG59460.1,
RC ECO:0000313|Proteomes:UP000054837};
RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., Mayilraj S.,
RA Bhadada S.K.;
RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and
RT assembly.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan,
CC amylopectin and glycogen, and in the alpha- and beta-limit dextrins
CC of amylopectin and glycogen.; EC=3.2.1.41;
CC Evidence={ECO:0000256|ARBA:ARBA00023965};
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:KUG59460.1}.
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DR EMBL; LQBL01000002; KUG59460.1; -; Genomic_DNA.
DR RefSeq; WP_058889934.1; NZ_LQBL01000002.1.
DR STRING; 767452.AVL62_07285; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000054837; Unassembled WGS sequence.
DR GO; GO:0051060; F:pullulanase activity; IEA:InterPro.
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; cd02860; E_set_Pullulanase; 1.
DR CDD; cd12962; X25_BaPul_like; 3.
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; 4.
DR Gene3D; 2.60.40.1130; Rab geranylgeranyltransferase alpha-subunit, insert domain; 1.
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; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR PANTHER; PTHR43002:SF11; PULLULANASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054837};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1907
FT /note="pullulanase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038444438"
FT DOMAIN 160..613
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 1907 AA; 206229 MW; 3C0FAF2E7F2A96C3 CRC64;
MTRPLLAAAL SATLLATTGA ATLASQAVAP SMAAAAPART VTLVGDLQSE LGCAQDWAAA
CEATVLSPVE GSPDLYRSSF EVPAGRWEYK VALDGAWDES YPQANLAFEL QGPATVEFSF
DDVEDEVGLV PLLGEQTTEQ DAALATDSLR APVTREQFYF VMADRFANGD PTNDTAGIAG
DRLQHGFDPT DKGFFHGGDL AGIQDRLDYI EGLGTTAIWL TPSFKNRPVQ GEGADASAGY
HGYWVTDFTQ IDPHLGTNEE MKALIDEAHD RGMKVYFDII TNHTADVIDY AEGEYGYVDK
ETEPYRDAAG NAFDDRDYVN KPFPLLDPET SFPYTPVFRT EEDAEVKVPG WLNDRTLYHN
RGDSTFAGES SLYGDFVGLD DLFTENPEVV DGMVDIYSTW ADLGIDGFRI DTVKHVNLEF
WQEFSPRVLE AAREGNEDFF MFGEVYDSNP EYLSTFPTEG ELQAVIDFGF QARSVAFARG
AATTDLRTFY AQDDYYTDTD SNAYQLPTFT GNHDMGRAAM MLAGDHSGED LQRRVELTNA
LMFLTRGQPV VYYGDEQGFI GAGGDKDARQ DMFATQVQQY ADEPVIGAPS GARDRYDTGH
PLYRQIAALS DLVEANPALA DGAQIHRYAS NEAGIYAFSR IDAEEQVEYL VVANNSDEPQ
QASLSTYGSR TMFRAIYGER GRFITGSEGR LTVDVDPLSV EVYRAEKDLR GRREAPSVAM
TSPAAGGVVG GRAEIGAAVP ENVFAQVTFA YRPVGVQEWS VLGTDDNAPY RVFHDVTGLP
DGTLLEYRAI LQGHSGNVSA SSSYGIVGEA GSGGGGGGGV DPIGPVEQPD AVSVPGSHNP
AMGCSGDWQP DCDQAQLTLD AKDTVWKGTY DAGTIPAGDY EYKAAIDRSW DESYGAGGAP
GGANIGYTAD GGPVSFYYEH ARHYVTSDAE GPIITAPGSM QSELGCPGDW DPSCMAPWLI
DPDGDGTYTY ATTAIPAGTY ELKVAHGLSW DENYGEGGER DGANIGFSVP SDGVRTTLSY
DLQTHVLSVT TSEAGVAPDL GSQRAYWVRD DLVAWPAEGV GDAVLRDWRL HWSADGGLGI
DAEAVTGGDS SPLTLDPDGL PEEVLEDFPH LEGYLALRLD RRSARAAGDI LTGQVAVAMY
DDLGRLADAT GVQVPGVLDD LYAERAADTA LGVSWRGPNP TLRLWAPTAQ DVRLLTWPEG
GQGDPQESSL RRLKDGSWEI KGKRSWTGRE YLFEVDVFVP ETGAVETNRV TDPYSVALTL
DSERSVLVDL DDRQWQPRVW QRAEAPALED EVDQTIYELH VRDFSMADPD VPAELRGSYL
AFAEDGYGRR HLEALAEAGM NTVHLLPTFD IASIPETTAD AEAVPQPDCD LDSLPPDSAE
QQECVMAQAD ADAFNWGYDP WHFMAPEGSY ASTTQAAQGG ARVAEFRTMV GGLHESGLRV
VLDKVFNHTA QSGQGSKSVL DKVVPGYYHR LNAVGDVETS TCCENIATEH AMAEKLMVDA
VVVWARDYKV DGFRFDLMGH HSRDNMQAVR AALDELTVRR DGVDGSQVTL YGEGWNFGEV
ADNARFYQAT QGQLDGTSIG TFNDRLRDGV RGGGPFDEDP GAEKGFATGG TSGNDTDLVQ
VGLAGNLRGF ELRSQETGEV VTGEQVDYNG SAAGYAEDPD EVVNYVDAHD NETIFDALTF
KLPQDLPMAD RVRMNTLALS TTTLSQSISF WHGGADLLRS KSLDRNSYNS GDWFNLLDFT
MTENGFGRGL PPAADNEDKW DLMRPLLADP SLAPEPADIE QASEMAADLL RLRFSSDLFR
LADPELVQEK VSFPVSGTAD GDAQVVVMRV DDTVGADVDP GLDGLVVVFN ASGEQVDQVV
PGLEGEQLEL SPVQAEGADE VVREATWEAA TGTATVPART VAVFVQP
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