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P94388

- CAH_BACSU

UniProt

P94388 - CAH_BACSU

Protein

Cephalosporin-C deacetylase

Gene

cah

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Esterase that removed acetyl groups from a number of O-acetylated small substrates, such as acetylated xylose, short xylooligosaccharides and cephalosporin C. Has no activity towards polymeric acetylated xylan. Cannot cleave amide linkages.1 Publication

    Catalytic activityi

    Deacetylation of xylans and xylo-oligosaccharides.1 Publication
    Cephalosporin C + H2O = deacetylcephalosporin C + acetate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei91 – 911Substrate; via amide nitrogen
    Active sitei181 – 1811Nucleophile
    Active sitei269 – 2691Charge relay system
    Active sitei298 – 2981Charge relay system

    GO - Molecular functioni

    1. acetylxylan esterase activity Source: UniProtKB-EC
    2. cephalosporin-C deacetylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellulose catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

    Enzyme and pathway databases

    BioCyciBSUB:BSU03180-MONOMER.

    Protein family/group databases

    MEROPSiS09.949.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cephalosporin-C deacetylase (EC:3.1.1.41)
    Alternative name(s):
    Acetylxylan esterase (EC:3.1.1.72)
    Gene namesi
    Name:cah
    Ordered Locus Names:BSU03180
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU03180. [Micado]

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Biotechnological usei

    Used in the pharmaceutical industry for the chemoenzymatic deacetylation of cephalosporins and the synthesis of novel antibiotics.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi181 – 1811S → A: Loss of activity.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 318318Cephalosporin-C deacetylasePRO_0000360523Add
    BLAST

    Proteomic databases

    PaxDbiP94388.

    Interactioni

    Subunit structurei

    Homohexamer.2 Publications

    Protein-protein interaction databases

    STRINGi224308.BSU03180.

    Structurei

    Secondary structure

    1
    318
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 125
    Helixi24 – 3613
    Beta strandi43 – 475
    Beta strandi52 – 6312
    Helixi64 – 663
    Beta strandi67 – 7812
    Beta strandi82 – 887
    Helixi96 – 983
    Helixi99 – 1079
    Beta strandi111 – 1155
    Turni118 – 1203
    Beta strandi121 – 1233
    Beta strandi129 – 1313
    Beta strandi134 – 1374
    Turni138 – 1436
    Turni145 – 1473
    Helixi149 – 16618
    Beta strandi170 – 18011
    Helixi182 – 19312
    Beta strandi198 – 2047
    Helixi210 – 2167
    Turni220 – 2234
    Helixi224 – 2318
    Helixi235 – 24612
    Helixi250 – 2534
    Helixi254 – 2563
    Beta strandi261 – 2666
    Beta strandi270 – 2723
    Helixi274 – 28310
    Beta strandi286 – 2938
    Helixi302 – 31615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L7AX-ray1.50A/B1-318[»]
    1ODSX-ray1.90A/B/C/D/E/F/G/H1-318[»]
    1ODTX-ray1.70C/H1-318[»]
    ProteinModelPortaliP94388.
    SMRiP94388. Positions 1-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP94388.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the carbohydrate esterase 7 family.Curated

    Phylogenomic databases

    eggNOGiCOG3458.
    HOGENOMiHOG000250099.
    KOiK01060.
    OMAiPYLEINS.
    OrthoDBiEOG6CZQPN.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR008391. AXE1.
    [Graphical view]
    PfamiPF05448. AXE1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P94388-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLFDLPLDQ LQTYKPEKTA PKDFSEFWKL SLEELAKVQA EPDLQPVDYP    50
    ADGVKVYRLT YKSFGNARIT GWYAVPDKEG PHPAIVKYHG YNASYDGEIH 100
    EMVNWALHGY ATFGMLVRGQ QSSEDTSISP HGHALGWMTK GILDKDTYYY 150
    RGVYLDAVRA LEVISSFDEV DETRIGVTGG SQGGGLTIAA AALSDIPKAA 200
    VADYPYLSNF ERAIDVALEQ PYLEINSFFR RNGSPETEVQ AMKTLSYFDI 250
    MNLADRVKVP VLMSIGLIDK VTPPSTVFAA YNHLETKKEL KVYRYFGHEY 300
    IPAFQTEKLA FFKQHLKG 318
    Length:318
    Mass (Da):35,807
    Last modified:May 1, 1997 - v1
    Checksum:iBA0D95A34CB503C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50453 Genomic DNA. Translation: BAA08952.1.
    AL009126 Genomic DNA. Translation: CAB12112.1.
    PIRiG69596.
    RefSeqiNP_388200.1. NC_000964.3.
    WP_003246400.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB12112; CAB12112; BSU03180.
    GeneIDi938341.
    KEGGibsu:BSU03180.
    PATRICi18972195. VBIBacSub10457_0326.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50453 Genomic DNA. Translation: BAA08952.1 .
    AL009126 Genomic DNA. Translation: CAB12112.1 .
    PIRi G69596.
    RefSeqi NP_388200.1. NC_000964.3.
    WP_003246400.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L7A X-ray 1.50 A/B 1-318 [» ]
    1ODS X-ray 1.90 A/B/C/D/E/F/G/H 1-318 [» ]
    1ODT X-ray 1.70 C/H 1-318 [» ]
    ProteinModelPortali P94388.
    SMRi P94388. Positions 1-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU03180.

    Protein family/group databases

    MEROPSi S09.949.

    Proteomic databases

    PaxDbi P94388.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12112 ; CAB12112 ; BSU03180 .
    GeneIDi 938341.
    KEGGi bsu:BSU03180.
    PATRICi 18972195. VBIBacSub10457_0326.

    Organism-specific databases

    GenoListi BSU03180. [Micado ]

    Phylogenomic databases

    eggNOGi COG3458.
    HOGENOMi HOG000250099.
    KOi K01060.
    OMAi PYLEINS.
    OrthoDBi EOG6CZQPN.

    Enzyme and pathway databases

    BioCyci BSUB:BSU03180-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P94388.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR008391. AXE1.
    [Graphical view ]
    Pfami PF05448. AXE1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome: determination of the sequence of a 146 kb segment and identification of 113 genes."
      Yamane K., Kumano M., Kurita K.
      Microbiology 142:3047-3056(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    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. "Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed by the hexameric structure of the Bacillus subtilis enzyme at 1.9A resolution."
      Vincent F., Charnock S.J., Verschueren K.H., Turkenburg J.P., Scott D.J., Offen W.A., Roberts S., Pell G., Gilbert H.J., Davies G.J., Brannigan J.A.
      J. Mol. Biol. 330:593-606(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT ALA-181 IN COMPLEX WITH ACETATE, CATALYTIC ACTIVITY, BIOTECHNOLOGY, SUBUNIT, FUNCTION, PROBABLE SUBCELLULAR LOCATION.
    4. "1.5A crystal structure of the cephalosporin C deacetylase."
      Midwest center for structural genomics (MCSG)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiCAH_BACSU
    AccessioniPrimary (citable) accession number: P94388
    Secondary accession number(s): Q797Q7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 20, 2009
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 90 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, Reference proteome

    Documents

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

    External Data

    Dasty 3