PULA_BACSU
ID PULA_BACSU Reviewed; 718 AA.
AC C0SPA0; O34587; Q795S6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
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;
GN Name=amyX; OrderedLocusNames=BSU29930;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP PROTEIN SEQUENCE OF 1-10, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=168;
RX PubMed=16582490; DOI=10.1107/s1744309106007901;
RA Malle D., Itoh T., Hashimoto W., Murata K., Utsumi S., Mikami B.;
RT "Overexpression, purification and preliminary X-ray analysis of pullulanase
RT from Bacillus subtilis strain 168.";
RL Acta Crystallogr. F 62:381-384(2006).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=27.6 umol/min/mg enzyme (at pH 5.4)
CC {ECO:0000269|PubMed:16582490};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:16582490};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:16582490};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AF008220; AAC00283.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14971.2; -; Genomic_DNA.
DR PIR; G69585; G69585.
DR RefSeq; NP_390871.2; NC_000964.3.
DR RefSeq; WP_003229246.1; NZ_JNCM01000036.1.
DR PDB; 2E8Y; X-ray; 2.11 A; A/B=1-718.
DR PDB; 2E8Z; X-ray; 2.20 A; A/B=1-718.
DR PDB; 2E9B; X-ray; 2.30 A; A/B=1-718.
DR PDBsum; 2E8Y; -.
DR PDBsum; 2E8Z; -.
DR PDBsum; 2E9B; -.
DR AlphaFoldDB; C0SPA0; -.
DR SMR; C0SPA0; -.
DR STRING; 224308.BSU29930; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; CBM68; Carbohydrate-Binding Module Family 68.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; C0SPA0; -.
DR PRIDE; C0SPA0; -.
DR EnsemblBacteria; CAB14971; CAB14971; BSU_29930.
DR GeneID; 937292; -.
DR KEGG; bsu:BSU29930; -.
DR PATRIC; fig|224308.179.peg.3251; -.
DR eggNOG; COG1523; Bacteria.
DR InParanoid; C0SPA0; -.
DR OMA; YNRIVEC; -.
DR PhylomeDB; C0SPA0; -.
DR BioCyc; BSUB:BSU29930-MON; -.
DR EvolutionaryTrace; C0SPA0; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0051060; F:pullulanase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 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; IPR040697; PulA_N1.
DR InterPro; IPR011840; PulA_typeI.
DR InterPro; IPR045041; Pullulanase_PULA-like.
DR PANTHER; PTHR43631; PTHR43631; 2.
DR Pfam; PF00128; Alpha-amylase; 2.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF17999; PulA_N1; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02104; pulA_typeI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..718
FT /note="Pullulanase"
FT /id="PRO_0000381992"
FT ACT_SITE 406
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 525
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 553
FT /note="A -> V (in Ref. 1; AAC00283)"
FT /evidence="ECO:0000305"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:2E8Y"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 311..327
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:2E8Y"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 413..426
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 465..472
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 491..498
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 559..566
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 586..589
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 593..598
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 600..615
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:2E8Y"
FT HELIX 624..630
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 631..636
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:2E8Y"
FT TURN 649..651
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 653..662
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 664..671
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:2E9B"
FT STRAND 678..683
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 686..694
FT /evidence="ECO:0007829|PDB:2E8Y"
FT STRAND 696..710
FT /evidence="ECO:0007829|PDB:2E8Y"
SQ SEQUENCE 718 AA; 81077 MW; 2D23D065C50007E9 CRC64;
MVSIRRSFEA YVDDMNIITV LIPAEQKEIM TPPFRLETEI TDFPLAVREE YSLEAKYKYV
CVSDHPVTFG KIHCVRASSG HKTDLQIGAV IRTAAFDDEF YYDGELGAVY TADHTVFKVW
APAATSAAVK LSHPNKSGRT FQMTRLEKGV YAVTVTGDLH GYEYLFCICN NSEWMETVDQ
YAKAVTVNGE KGVVLRPDQM KWTAPLKPFS HPVDAVIYET HLRDFSIHEN SGMINKGKYL
ALTETDTQTA NGSSSGLAYV KELGVTHVEL LPVNDFAGVD EEKPLDAYNW GYNPLHFFAP
EGSYASNPHD PQTRKTELKQ MINTLHQHGL RVILDVVFNH VYKRENSPFE KTVPGYFFRH
DECGMPSNGT GVGNDIASER RMARKFIADC VVYWLEEYNV DGFRFDLLGI LDIDTVLYMK
EKATKAKPGI LLFGEGWDLA TPLPHEQKAA LANAPRMPGI GFFNDMFRDA VKGNTFHLKA
TGFALGNGES AQAVMHGIAG SSGWKALAPI VPEPSQSINY VESHDNHTFW DKMSFALPQE
NDSRKRSRQR LAAAIILLAQ GVPFIHSGQE FFRTKQGVEN SYQSSDSINQ LDWDRRETFK
EDVHYIRRLI SLRKAHPAFR LRSAADIQRH LECLTLKEHL IAYRLYDLDE VDEWKDIIVI
HHASPDSVEW RLPNDIPYRL LCDPSGFQED PTEIKKTVAV NGIGTVILYL ASDLKSFA
