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P94388 (CAH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cephalosporin-C deacetylase

EC=3.1.1.41
Alternative name(s):
Acetylxylan esterase
EC=3.1.1.72
Gene names
Name:cah
Ordered Locus Names:BSU03180
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

Deacetylation of xylans and xylo-oligosaccharides. Ref.3

Cephalosporin C + H2O = deacetylcephalosporin C + acetate. Ref.3

Subunit structure

Homohexamer. Ref.3 Ref.4

Subcellular location

Cytoplasm Probable Ref.3.

Biotechnological use

Used in the pharmaceutical industry for the chemoenzymatic deacetylation of cephalosporins and the synthesis of novel antibiotics. Ref.3

Sequence similarities

Belongs to the carbohydrate esterase 7 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentCytoplasm
   Molecular functionHydrolase
Serine esterase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionacetylxylan esterase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cephalosporin-C deacetylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Cephalosporin-C deacetylase
PRO_0000360523

Sites

Active site1811Nucleophile
Active site2691Charge relay system
Active site2981Charge relay system
Binding site911Substrate; via amide nitrogen

Experimental info

Mutagenesis1811S → A: Loss of activity.

Secondary structure

........................................................ 318
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P94388 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: BA0D95A34CB503C3

FASTA31835,807
        10         20         30         40         50         60 
MQLFDLPLDQ LQTYKPEKTA PKDFSEFWKL SLEELAKVQA EPDLQPVDYP ADGVKVYRLT 

        70         80         90        100        110        120 
YKSFGNARIT GWYAVPDKEG PHPAIVKYHG YNASYDGEIH EMVNWALHGY ATFGMLVRGQ 

       130        140        150        160        170        180 
QSSEDTSISP HGHALGWMTK GILDKDTYYY RGVYLDAVRA LEVISSFDEV DETRIGVTGG 

       190        200        210        220        230        240 
SQGGGLTIAA AALSDIPKAA VADYPYLSNF ERAIDVALEQ PYLEINSFFR RNGSPETEVQ 

       250        260        270        280        290        300 
AMKTLSYFDI MNLADRVKVP VLMSIGLIDK VTPPSTVFAA YNHLETKKEL KVYRYFGHEY 

       310 
IPAFQTEKLA FFKQHLKG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50453 Genomic DNA. Translation: BAA08952.1.
AL009126 Genomic DNA. Translation: CAB12112.1.
PIRG69596.
RefSeqNP_388200.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L7AX-ray1.50A/B1-318[»]
1ODSX-ray1.90A/B/C/D/E/F/G/H1-318[»]
1ODTX-ray1.70C/H1-318[»]
ProteinModelPortalP94388.
SMRP94388. Positions 1-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU03180.

Protein family/group databases

MEROPSS09.949.

Proteomic databases

PaxDbP94388.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12112; CAB12112; BSU03180.
GeneID938341.
KEGGbsu:BSU03180.
PATRIC18972195. VBIBacSub10457_0326.

Organism-specific databases

GenoListBSU03180. [Micado]

Phylogenomic databases

eggNOGCOG3458.
HOGENOMHOG000250099.
KOK01060.
OMAPYLEINS.
OrthoDBEOG6CZQPN.

Enzyme and pathway databases

BioCycBSUB:BSU03180-MONOMER.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR008391. AXE1.
[Graphical view]
PfamPF05448. AXE1. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP94388.

Entry information

Entry nameCAH_BACSU
AccessionPrimary (citable) accession number: P94388
Secondary accession number(s): Q797Q7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList