PULA_KLEAE
ID PULA_KLEAE Reviewed; 1096 AA.
AC P07811;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Pullulanase;
DE EC=3.2.1.41;
DE AltName: Full=Alpha-dextrin endo-1,6-alpha-glucosidase;
DE AltName: Full=Pullulan 6-glucanohydrolase;
DE Flags: Precursor;
GN Name=pulA;
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DIACYLGLYCEROL AT CYS-20, AND
RP PALMITOYLATION AT CYS-20.
RC STRAIN=W70;
RX PubMed=3155373; DOI=10.1128/jb.169.5.2301-2306.1987;
RA Katsuragi N., Takizawa N., Murooka Y.;
RT "Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes
RT W70.";
RL J. Bacteriol. 169:2301-2306(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74, SUBUNIT, DIACYLGLYCEROL AT
RP CYS-20, AND PALMITOYLATION AT CYS-20.
RC STRAIN=FG9;
RX PubMed=2846288; DOI=10.1002/j.1460-2075.1988.tb03148.x;
RA Charalambous B.M., Keen J.N., McPherson M.J.;
RT "Collagen-like sequences stabilize homotrimers of a bacterial hydrolase.";
RL EMBO J. 7:2903-2909(1988).
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 -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:2846288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M16187; AAA25124.1; ALT_SEQ; Genomic_DNA.
DR PIR; A26879; A26879.
DR PDB; 2FGZ; X-ray; 1.75 A; A=20-1090.
DR PDB; 2FH6; X-ray; 1.80 A; A=20-1090.
DR PDB; 2FH8; X-ray; 1.90 A; A=20-1087.
DR PDB; 2FHB; X-ray; 1.80 A; A=20-1090.
DR PDB; 2FHC; X-ray; 1.85 A; A=20-1090.
DR PDB; 2FHF; X-ray; 1.65 A; A=20-1090.
DR PDBsum; 2FGZ; -.
DR PDBsum; 2FH6; -.
DR PDBsum; 2FH8; -.
DR PDBsum; 2FHB; -.
DR PDBsum; 2FHC; -.
DR PDBsum; 2FHF; -.
DR AlphaFoldDB; P07811; -.
DR SMR; P07811; -.
DR CAZy; CBM41; Carbohydrate-Binding Module Family 41.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P07811; -.
DR KEGG; ag:AAA25124; -.
DR SABIO-RK; P07811; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10315; CBM41_pullulanase; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
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; IPR041111; Pullulanase_Ins.
DR InterPro; IPR040671; Pullulanase_N2.
DR InterPro; IPR045041; Pullulanase_PULA-like.
DR PANTHER; PTHR43631; PTHR43631; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF11852; DUF3372; 1.
DR Pfam; PF03714; PUD; 1.
DR Pfam; PF18494; Pullulanase_Ins; 1.
DR Pfam; PF17967; Pullulanase_N2; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 2.
DR TIGRFAMs; TIGR02103; pullul_strch; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane;
KW Palmitate; Signal.
FT SIGNAL 1..19
FT CHAIN 20..1096
FT /note="Pullulanase"
FT /id="PRO_0000001426"
FT REGION 24..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 694
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 723
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 851
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:2846288,
FT ECO:0000305|PubMed:3155373"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305|PubMed:2846288,
FT ECO:0000305|PubMed:3155373"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 271..274
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 323..328
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 332..340
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 373..382
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 387..393
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 435..439
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 442..446
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 448..452
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 466..470
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 475..485
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 524..527
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 541..548
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 558..569
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 578..584
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 596..610
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 637..640
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 642..644
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 650..652
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 658..664
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 669..684
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 701..714
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 719..722
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 730..732
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 738..743
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 747..749
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 752..758
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 768..771
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 775..777
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 778..781
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 791..805
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 824..826
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 827..829
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 832..834
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 840..842
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 850..852
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 855..862
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 869..884
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 886..893
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 896..898
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 912..916
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 928..930
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 934..937
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 941..947
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 956..973
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 977..980
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 984..990
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 991..995
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1004..1010
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 1013..1015
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1018..1026
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1028..1030
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1032..1034
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 1038..1041
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 1048..1051
FT /evidence="ECO:0007829|PDB:2FH8"
FT HELIX 1056..1058
FT /evidence="ECO:0007829|PDB:2FH8"
FT TURN 1060..1063
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1069..1071
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1073..1075
FT /evidence="ECO:0007829|PDB:2FH8"
FT STRAND 1079..1086
FT /evidence="ECO:0007829|PDB:2FH8"
SQ SEQUENCE 1096 AA; 119336 MW; FE7D9167CDACFD79 CRC64;
MLRYTCHALF LGSLVLLSGC DNSSSSSTSG SPGSPGNPGN PGTPGTPDPQ DVVVRLPDVA
VPGEAVQASA RQAVIHLVDI AGITSSTPAD YATKNLYLWN NETCDALSAP VADWNDVSTT
PTGSDKYGPY WVIPLTKESG SINVIVRDGT NKLIDSGRVS FSDFTDRTVS VIAGNSAVYD
SRADAFRAAF GVALADAHWV DKTTLLWPGG ENKPIVRLYY SHSSKVAADS NGEFSDKYVK
LTPTTVNQQV SMRFPHLASY PAFKLPDDVN VDELLQGDDG GIAESDGILS LSHPGADRRR
AGRYLCRRAE ALSYGAQLTD SGVTFRVWAP TAQQVELVIY SADKKVIASH PMTRDSASGA
WSWQGGSDLK GAFYRYAMTV YHPQSRKVEQ YEVTDPYAHS LSTNSEYSQV VDLNDSALKP
EGWDGLTMPH AQKTKADLAK MTIHESHIRD LSAWDQTVPA ELRGKYLALT AQESNMVQHL
KQLSASGVTH IELLPVFDLA TVNEFSDKVA DIQQPFSRLC EVNSAVKSSE FAGYCDSGST
VEEVLTQLKQ NDSKDNPQVQ ALNTLVAQTD SYNWGYDPFH YTVPEGSYAT DPEGTARIKE
FRTMIQAIKQ DLGMNVIMDV VYNHTNAAGP TDRTSVLDKI VPWYYQRLNE TTGSVESATC
CSDSAPEHRM FAKLIADSLA VWTTDYKIDG FRFDLMGYHP KAQILSAWER IKALNPDIYF
FGEGWDSNQS DRFEIASQIN LKGTGIGTFS DRLRDAVRGG GPFDSGDALR QNQGVGSGAG
VLPNELTTLS DDQARHLADL TRLGMAGNLA DFVLIDKDGA VKRGSEIDYN GAPGGYAADP
TEVVNYVSKH DNQTLWDMIS YKAAQEADLD TRVRMQAVSL ATVMLGQGIA FDQQGSELLR
SKSFTRDSYD SGDWFNRVDY SLQDNNYNVG MPRSSDDGSN YDIIARVKDA VATPGETELK
QMTAFYQELT ALRKSSPLFT LGDGATVMKR VDFRNTGADQ QTGLLVMTID DGMQAGRQSG
QPCRRHRGGD QRRAGKPDAA GLRRHIAPAE RYSAGGGRPV AGERVQVAAD GSVTLPAWSV
AVLELPQASR RALACR
