ID A4SIR9_AERS4 Unreviewed; 1344 AA.
AC A4SIR9;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Pullulanase {ECO:0000313|EMBL:ABO88791.1};
GN Name=pulA {ECO:0000313|EMBL:ABO88791.1};
GN OrderedLocusNames=ASA_0628 {ECO:0000313|EMBL:ABO88791.1};
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO88791.1, ECO:0000313|Proteomes:UP000000225};
RN [1] {ECO:0000313|Proteomes:UP000000225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061}.
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DR EMBL; CP000644; ABO88791.1; -; Genomic_DNA.
DR RefSeq; WP_005313646.1; NC_009348.1.
DR STRING; 29491.GCA_000820065_01867; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; asa:ASA_0628; -.
DR PATRIC; fig|382245.13.peg.635; -.
DR eggNOG; COG1523; Bacteria.
DR HOGENOM; CLU_004744_5_0_6; -.
DR Proteomes; UP000000225; Chromosome.
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; 1.
DR CDD; cd02860; E_set_Pullulanase; 1.
DR CDD; cd02861; E_set_pullulanase_like; 1.
DR Gene3D; 2.60.40.1110; -; 1.
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; IPR041111; Pullulanase_Ins.
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; PF11852; Pullul_strch_C; 1.
DR Pfam; PF18494; Pullulanase_Ins; 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; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1344
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002673320"
FT DOMAIN 186..294
FT /note="Pullulanase N2"
FT /evidence="ECO:0000259|Pfam:PF17967"
FT DOMAIN 306..390
FT /note="Glycoside hydrolase family 13 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02922"
FT DOMAIN 488..561
FT /note="Pullulanase Ins"
FT /evidence="ECO:0000259|Pfam:PF18494"
FT DOMAIN 911..1078
FT /note="Alpha-1,6-glucosidases pullulanase-type C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11852"
FT REGION 23..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1344 AA; 144399 MW; FEB5709BEEFD5C6C CRC64;
MDMKKTKVAL VTASLLALLS GCNDNSSSPS TPEPTDGPVA RLPDVQPPAE QLVAGPDQAV
IALVDTQTSA ARGIEGPFAS HSLHLWNNDA CNATAESGLN AGWDDKANTP TAVDSFGPSW
VVPLAKLEGC INFIARNGDL ANLTGADMKV VFSDHPDRTV AIVAGKSEVF DSRADAFTAA
FGVAGASAHL IDGNTLIWQG GKDKPHVRLY YTESGTIKAN AEGVFDFPYL SLTATSLTAE
QQAKYPHLKD AAAFALPSGK DLKPLLKGEL VAIGTDADGI LQGATLVQSA GALDALYAEE
ATKLAYGAIV EGGNVTFRLW APTAKSVKLA LFDEQHKALG ERTMTQDDAS GSWSVQGGSE
LVGKFYRYDI QVYHPLSRKL ESYQVTDPYS LSLAMNSEFS QVVDLDDPAL KPEGWDSLKA
PHSQQNPADI TIYEAHVRDL TGNDESTKPE HRGKFLGLTD SDSVPVKHLQ SLAQSGVSHL
HLLPVFDIAT VNEDPAKVAN LQDDFSKLCQ VNAEVKDSKF GGYCGGGQTI EAVLADLQGA
DSKESPQVQE LSGYLRGVDS FNWGYDPYHY TAPEGSYATD AEGSQRILEF REMVKAIKQN
IGMNVVMDVV YNHTNEAGLG PKSVLDKIVP WYYQRLNPET GSVENSTCCS NTAPEHAMFA
KLMDDSLVTW ARDYKIDAFR FDLMGHHPKD QVVQALAAVK QVNPEMYFYG EGWNFGEVQD
DKRFVQATQK HLAGTGIGSF SDRLRDAVRG GSPFDGGDTI RKTQGFGNGA LVDANEMDGV
ELATALHQSD LVRLGMAGNL KEFVLTDKDG MPKKGSDIDY NGQPAGYAQD PTEIQNYVDK
HDNQTLFDNL IYKAPEGADL VRMQGVSLAT AMLGQGIPFT HAGVELLRSK SMERDSYDSG
DWYNRVDYTL ADNNFDKGLP RKDKDGDNYP LIEQVLGKHV KPSGADMATM VGFYQELAEL
RQSSRLLRLG SGAEVIKRVD FRNTGPDQVP GLIVMTVDDG VNAGADLDPA IEGLVVMINA
TNQPQSIGDF RDGKDQPIDL STLQLSPAHH AGSSIADGAL ASGGQLTLGA WSAAVFVKPQ
AGAQGAGLPV SKKIDLSTVP PFGDTDVFVR GFLNEWDPVN KMIFGGNFTY EFTTEVTTDQ
LGTTQVKIAG SEWDGPINYG KCSDTDQLAT GQVSVLCANG GDLPFNADKA GSYKFVFTAM
NKDKPTLSVS FTEPVQSCKV LDTVAGNPLG YNLFVKGELS GWAAQPQYQL SYKGMDGDLA
IYQAAFNYMG TSEFKVANED WSKEYLLNGG GAVTAETGYS LGFSQAGSAN NSITLPQGLW
SVLVKVDPAG TKAGTAVIQE CRAK
//
