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Protein

Pullulanase

Gene

amyX

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.

Kineticsi

    1. Vmax=27.6 µmol/min/mg enzyme (at pH 5.4)1 Publication

    pH dependencei

    Optimum pH is 6.0.1 Publication

    Temperature dependencei

    Optimum temperature is 40 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei406 – 4061NucleophileBy similarity
    Active sitei435 – 4351Proton donorBy similarity
    Sitei525 – 5251Transition state stabilizerBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciBSUB:BSU29930-MONOMER.

    Protein family/group databases

    CAZyiCBM48. Carbohydrate-Binding Module Family 48.
    GH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pullulanase (EC:3.2.1.41)
    Alternative name(s):
    Alpha-dextrin endo-1,6-alpha-glucosidase
    Pullulan 6-glucanohydrolase
    Gene namesi
    Name:amyX
    Ordered Locus Names:BSU29930
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    Proteomesi
    • UP000001570 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 718718PullulanasePRO_0000381992Add
    BLAST

    Proteomic databases

    PaxDbiC0SPA0.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100016321.

    Structurei

    Secondary structure

    1
    718
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 148Combined sources
    Beta strandi17 – 237Combined sources
    Helixi24 – 263Combined sources
    Turni27 – 293Combined sources
    Beta strandi34 – 385Combined sources
    Beta strandi41 – 5212Combined sources
    Beta strandi54 – 629Combined sources
    Beta strandi74 – 763Combined sources
    Beta strandi82 – 843Combined sources
    Helixi89 – 924Combined sources
    Helixi94 – 1007Combined sources
    Beta strandi107 – 1104Combined sources
    Beta strandi112 – 1209Combined sources
    Beta strandi125 – 1328Combined sources
    Beta strandi139 – 1424Combined sources
    Helixi147 – 1493Combined sources
    Beta strandi150 – 1578Combined sources
    Beta strandi163 – 1708Combined sources
    Beta strandi173 – 1775Combined sources
    Beta strandi183 – 1853Combined sources
    Helixi187 – 1893Combined sources
    Beta strandi191 – 1933Combined sources
    Helixi212 – 2143Combined sources
    Beta strandi217 – 2204Combined sources
    Helixi222 – 2276Combined sources
    Helixi239 – 2435Combined sources
    Helixi256 – 2638Combined sources
    Beta strandi266 – 2716Combined sources
    Beta strandi274 – 2796Combined sources
    Helixi284 – 2863Combined sources
    Beta strandi293 – 3008Combined sources
    Beta strandi308 – 3103Combined sources
    Helixi311 – 32717Combined sources
    Beta strandi331 – 3366Combined sources
    Helixi344 – 3463Combined sources
    Helixi348 – 3525Combined sources
    Turni354 – 3563Combined sources
    Beta strandi364 – 3663Combined sources
    Beta strandi371 – 3733Combined sources
    Helixi381 – 39818Combined sources
    Beta strandi402 – 4054Combined sources
    Helixi408 – 4103Combined sources
    Helixi413 – 42614Combined sources
    Beta strandi431 – 4344Combined sources
    Helixi445 – 4473Combined sources
    Helixi451 – 4566Combined sources
    Beta strandi461 – 4633Combined sources
    Helixi465 – 4728Combined sources
    Beta strandi475 – 4773Combined sources
    Helixi483 – 4853Combined sources
    Helixi488 – 4903Combined sources
    Helixi491 – 4988Combined sources
    Beta strandi510 – 5134Combined sources
    Helixi514 – 5163Combined sources
    Beta strandi517 – 5193Combined sources
    Beta strandi524 – 5274Combined sources
    Helixi529 – 5368Combined sources
    Helixi542 – 55716Combined sources
    Beta strandi559 – 5668Combined sources
    Helixi569 – 5713Combined sources
    Helixi586 – 5894Combined sources
    Helixi593 – 5986Combined sources
    Helixi600 – 61516Combined sources
    Helixi617 – 6204Combined sources
    Helixi624 – 6307Combined sources
    Beta strandi631 – 6366Combined sources
    Beta strandi638 – 6458Combined sources
    Turni649 – 6513Combined sources
    Beta strandi653 – 66210Combined sources
    Beta strandi664 – 6718Combined sources
    Beta strandi673 – 6764Combined sources
    Beta strandi678 – 6836Combined sources
    Beta strandi686 – 6949Combined sources
    Beta strandi696 – 71015Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E8YX-ray2.11A/B1-718[»]
    2E8ZX-ray2.20A/B1-718[»]
    2E9BX-ray2.30A/B1-718[»]
    ProteinModelPortaliC0SPA0.
    SMRiC0SPA0. Positions 1-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiC0SPA0.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Phylogenomic databases

    eggNOGiENOG4108IUM. Bacteria.
    COG1523. LUCA.
    HOGENOMiHOG000059883.
    InParanoidiC0SPA0.
    KOiK01200.
    OMAiYNRIVEC.
    OrthoDBiEOG66TG1T.
    PhylomeDBiC0SPA0.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR004193. Glyco_hydro_13_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR011840. PulA_typeI.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 2 hits.
    PfamiPF00128. Alpha-amylase. 2 hits.
    PF02922. CBM_48. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsiTIGR02104. pulA_typeI. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    C0SPA0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVSIRRSFEA YVDDMNIITV LIPAEQKEIM TPPFRLETEI TDFPLAVREE
    60 70 80 90 100
    YSLEAKYKYV CVSDHPVTFG KIHCVRASSG HKTDLQIGAV IRTAAFDDEF
    110 120 130 140 150
    YYDGELGAVY TADHTVFKVW APAATSAAVK LSHPNKSGRT FQMTRLEKGV
    160 170 180 190 200
    YAVTVTGDLH GYEYLFCICN NSEWMETVDQ YAKAVTVNGE KGVVLRPDQM
    210 220 230 240 250
    KWTAPLKPFS HPVDAVIYET HLRDFSIHEN SGMINKGKYL ALTETDTQTA
    260 270 280 290 300
    NGSSSGLAYV KELGVTHVEL LPVNDFAGVD EEKPLDAYNW GYNPLHFFAP
    310 320 330 340 350
    EGSYASNPHD PQTRKTELKQ MINTLHQHGL RVILDVVFNH VYKRENSPFE
    360 370 380 390 400
    KTVPGYFFRH DECGMPSNGT GVGNDIASER RMARKFIADC VVYWLEEYNV
    410 420 430 440 450
    DGFRFDLLGI LDIDTVLYMK EKATKAKPGI LLFGEGWDLA TPLPHEQKAA
    460 470 480 490 500
    LANAPRMPGI GFFNDMFRDA VKGNTFHLKA TGFALGNGES AQAVMHGIAG
    510 520 530 540 550
    SSGWKALAPI VPEPSQSINY VESHDNHTFW DKMSFALPQE NDSRKRSRQR
    560 570 580 590 600
    LAAAIILLAQ GVPFIHSGQE FFRTKQGVEN SYQSSDSINQ LDWDRRETFK
    610 620 630 640 650
    EDVHYIRRLI SLRKAHPAFR LRSAADIQRH LECLTLKEHL IAYRLYDLDE
    660 670 680 690 700
    VDEWKDIIVI HHASPDSVEW RLPNDIPYRL LCDPSGFQED PTEIKKTVAV
    710
    NGIGTVILYL ASDLKSFA
    Length:718
    Mass (Da):81,077
    Last modified:May 5, 2009 - v1
    Checksum:i2D23D065C50007E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti553 – 5531A → V in AAC00283 (PubMed:9387221).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF008220 Genomic DNA. Translation: AAC00283.1.
    AL009126 Genomic DNA. Translation: CAB14971.2.
    PIRiG69585.
    RefSeqiNP_390871.2. NC_000964.3.
    WP_003229246.1. NZ_JNCM01000036.1.

    Genome annotation databases

    EnsemblBacteriaiCAB14971; CAB14971; BSU29930.
    GeneIDi937292.
    KEGGibsu:BSU29930.
    PATRICi18977892. VBIBacSub10457_3134.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF008220 Genomic DNA. Translation: AAC00283.1.
    AL009126 Genomic DNA. Translation: CAB14971.2.
    PIRiG69585.
    RefSeqiNP_390871.2. NC_000964.3.
    WP_003229246.1. NZ_JNCM01000036.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E8YX-ray2.11A/B1-718[»]
    2E8ZX-ray2.20A/B1-718[»]
    2E9BX-ray2.30A/B1-718[»]
    ProteinModelPortaliC0SPA0.
    SMRiC0SPA0. Positions 1-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.Bsubs1_010100016321.

    Protein family/group databases

    CAZyiCBM48. Carbohydrate-Binding Module Family 48.
    GH13. Glycoside Hydrolase Family 13.

    Proteomic databases

    PaxDbiC0SPA0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB14971; CAB14971; BSU29930.
    GeneIDi937292.
    KEGGibsu:BSU29930.
    PATRICi18977892. VBIBacSub10457_3134.

    Phylogenomic databases

    eggNOGiENOG4108IUM. Bacteria.
    COG1523. LUCA.
    HOGENOMiHOG000059883.
    InParanoidiC0SPA0.
    KOiK01200.
    OMAiYNRIVEC.
    OrthoDBiEOG66TG1T.
    PhylomeDBiC0SPA0.

    Enzyme and pathway databases

    BioCyciBSUB:BSU29930-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiC0SPA0.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR015902. Glyco_hydro_13.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR004193. Glyco_hydro_13_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR011840. PulA_typeI.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 2 hits.
    PfamiPF00128. Alpha-amylase. 2 hits.
    PF02922. CBM_48. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF81296. SSF81296. 1 hit.
    TIGRFAMsiTIGR02104. pulA_typeI. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
      Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
      Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
      Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
      Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168."
      Malle D., Itoh T., Hashimoto W., Murata K., Utsumi S., Mikami B.
      Acta Crystallogr. F 62:381-384(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-10, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: 168.

    Entry informationi

    Entry nameiPULA_BACSU
    AccessioniPrimary (citable) accession number: C0SPA0
    Secondary accession number(s): O34587, Q795S6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 1, 2009
    Last sequence update: May 5, 2009
    Last modified: June 8, 2016
    This is version 55 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.