P94388 (CAH_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Cellular component	Cytoplasm
Molecular function	Hydrolase Serine esterase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetylxylan esterase activity Inferred from electronic annotation. Source: EC carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW cephalosporin-C deacetylase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 318

318

Cephalosporin-C deacetylase

PRO_0000360523

Sites

Active site

181

1

Nucleophile

Active site

269

1

Charge relay system

Active site

298

1

Charge relay system

Binding site

91

1

Substrate; via amide nitrogen

Experimental info

Mutagenesis

181

1

S → A: Loss of activity.

Secondary structure

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318

Helix Strand Turn

Details...

Helix

8 – 12

5

Helix

24 – 36

13

Beta strand

43 – 47

5

Beta strand

52 – 63

12

Helix

64 – 66

3

Beta strand

67 – 78

12

Beta strand

82 – 88

7

Helix

96 – 98

3

Helix

99 – 107

9

Beta strand

111 – 115

5

Turn

118 – 120

3

Beta strand

121 – 123

3

Beta strand

129 – 131

3

Beta strand

134 – 137

4

Turn

138 – 143

6

Turn

145 – 147

3

Helix

149 – 166

18

Beta strand

170 – 180

11

Helix

182 – 193

12

Beta strand

198 – 204

7

Helix

210 – 216

7

Turn

220 – 223

4

Helix

224 – 231

8

Helix

235 – 246

12

Helix

250 – 253

4

Helix

254 – 256

3

Beta strand

261 – 266

6

Beta strand

270 – 272

3

Helix

274 – 283

10

Beta strand

286 – 293

8

Helix

302 – 316

15

Sequences

	Sequence		Length	Mass (Da)
	P94388 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: BA0D95A34CB503C3	FASTA	318	35,807
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

PIR

G69596.

RefSeq

NP_388200.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P94388.

SMR

P94388. Positions 1-318.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU03180.

Protein family/group databases

MEROPS

S09.949.

Proteomic databases

PaxDb

P94388.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB12112; CAB12112; BSU03180.

GeneID

938341.

KEGG

bsu:BSU03180.

PATRIC

18972195. VBIBacSub10457_0326.

Organism-specific databases

GenoList

BSU03180. [Micado]

Phylogenomic databases

eggNOG

COG3458.

HOGENOM

HOG000250099.

KO

K01060.

OMA

PYLEINS.

ProtClustDB

CLSK886663.

Enzyme and pathway databases

BioCyc

BSUB:BSU03180-MONOMER.

Family and domain databases

InterPro

IPR008391. AXE1.
[Graphical view]

Pfam

PF05448. AXE1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P94388.

Entry information

Entry name

CAH_BACSU

Accession

Primary (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:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program