Reviewed, UniProtKB/Swiss-Prot P94388 (CAH_BACSU)

Names and origin

Protein names

Recommended name:
    Cephalosporin C deacetylase
    EC=3.1.1.41
Alternative name(s):
    Acetyl xylan esterase
    EC=3.1.1.72

Gene names

Name:	cah
Ordered Locus Names:	BSU03180

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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.
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
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 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

55 – 63

9

Beta strand

67 – 69

3

Beta strand

73 – 75

3

Beta strand

84 – 87

4

Helix

99 – 107

9

Beta strand

111 – 113

3

Turn

145 – 147

3

Helix

154 – 166

13

Helix

187 – 193

7

Beta strand

200 – 204

5

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 – 265

5

Beta strand

270 – 272

3

Helix

274 – 283

10

Beta strand

286 – 292

7

Helix

302 – 316

15

Sequences

	Sequence		Length	Mass (Da)
	P94388-1 [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: 8969502] [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: 9384377] [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: 12842474] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT ALA-181 IN COMPLEX WITH ACETATE, CATALYTIC ACTIVITY, 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.

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	[»]

ModBase

Search...

Genome annotation databases

GeneID

938341.

GenomeReviews

Gene locus BSU03180 in contig AL009126_GR.

KEGG

bsu:BSU03180.

NMPDR

fig|224308.1.peg.319.

Organism-specific databases

SubtiList

BG11919. cah. [Micado]

CMR

Search...

Phylogenomic databases

HOGENOM

HBG312403.

OMA

DVPFLCH.

Enzyme and pathway databases

BioCyc

SUBTI:BSU03180-MONOMER.

Family and domain databases

InterPro

IPR008391. AXE1.
[Graphical view]

Pfam

PF05448. AXE1. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	January 19, 2010
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)