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P94388

- CAH_BACSU

UniProt

P94388 - CAH_BACSU

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Protein
Cephalosporin-C deacetylase
Gene
cah, BSU03180
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 Inferred 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

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 deacetylase
PRO_0000360523Add
BLAST

Proteomic databases

PaxDbiP94388.

Interactioni

Subunit structurei

Homohexamer.2 Publications

Protein-protein interaction databases

STRINGi224308.BSU03180.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP94388.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 89 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

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