(data stored in SCRATCH zone)

SWISSPROT: CAH_BACSU

ID   CAH_BACSU               Reviewed;         318 AA.
AC   P94388; Q797Q7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 110.
DE   RecName: Full=Cephalosporin-C deacetylase;
DE            EC=3.1.1.41;
DE   AltName: Full=Acetylxylan esterase;
DE            EC=3.1.1.72;
GN   Name=cah; OrderedLocusNames=BSU03180;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF MUTANT ALA-181 IN COMPLEX WITH
RP   ACETATE, CATALYTIC ACTIVITY, BIOTECHNOLOGY, SUBUNIT, FUNCTION, AND PROBABLE
RP   SUBCELLULAR LOCATION.
RX   PubMed=12842474; DOI=10.1016/s0022-2836(03)00632-6;
RA   Vincent F., Charnock S.J., Verschueren K.H., Turkenburg J.P., Scott D.J.,
RA   Offen W.A., Roberts S., Pell G., Gilbert H.J., Davies G.J., Brannigan J.A.;
RT   "Multifunctional xylooligosaccharide/cephalosporin C deacetylase revealed
RT   by the hexameric structure of the Bacillus subtilis enzyme at 1.9A
RT   resolution.";
RL   J. Mol. Biol. 330:593-606(2003).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), AND SUBUNIT.
RG   Midwest center for structural genomics (MCSG);
RT   "1.5A crystal structure of the cephalosporin C deacetylase.";
RL   Submitted (AUG-2005) to the PDB data bank.
CC   -!- FUNCTION: Esterase that removed acetyl groups from a number of O-
CC       acetylated small substrates, such as acetylated xylose, short
CC       xylooligosaccharides and cephalosporin C. Has no activity towards
CC       polymeric acetylated xylan. Cannot cleave amide linkages.
CC       {ECO:0000269|PubMed:12842474}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72; Evidence={ECO:0000269|PubMed:12842474};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cephalosporin C + H2O = acetate + deacetylcephalosporin C +
CC         H(+); Xref=Rhea:RHEA:22596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:57511, ChEBI:CHEBI:58366; EC=3.1.1.41;
CC         Evidence={ECO:0000269|PubMed:12842474};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:12842474, ECO:0000269|Ref.4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- BIOTECHNOLOGY: Used in the pharmaceutical industry for the
CC       chemoenzymatic deacetylation of cephalosporins and the synthesis of
CC       novel antibiotics. {ECO:0000269|PubMed:12842474}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 7 family.
CC       {ECO:0000305}.
DR   EMBL; D50453; BAA08952.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12112.1; -; Genomic_DNA.
DR   PIR; G69596; G69596.
DR   RefSeq; NP_388200.1; NC_000964.3.
DR   RefSeq; WP_003246400.1; NZ_JNCM01000030.1.
DR   PDB; 1L7A; X-ray; 1.50 A; A/B=1-318.
DR   PDB; 1ODS; X-ray; 1.90 A; A/B/C/D/E/F/G/H=1-318.
DR   PDB; 1ODT; X-ray; 1.70 A; C/H=1-318.
DR   PDBsum; 1L7A; -.
DR   PDBsum; 1ODS; -.
DR   PDBsum; 1ODT; -.
DR   SMR; P94388; -.
DR   STRING; 224308.BSU03180; -.
DR   ESTHER; bacsu-CAH; Acetyl-esterase_deacetylase.
DR   MEROPS; S09.949; -.
DR   PaxDb; P94388; -.
DR   PRIDE; P94388; -.
DR   EnsemblBacteria; CAB12112; CAB12112; BSU03180.
DR   GeneID; 938341; -.
DR   KEGG; bsu:BSU03180; -.
DR   PATRIC; fig|224308.179.peg.332; -.
DR   eggNOG; ENOG4105I82; Bacteria.
DR   eggNOG; COG3458; LUCA.
DR   HOGENOM; HOG000250099; -.
DR   InParanoid; P94388; -.
DR   KO; K01060; -.
DR   OMA; YDVVNFA; -.
DR   BioCyc; BSUB:BSU03180-MONOMER; -.
DR   BRENDA; 3.1.1.41; 658.
DR   SABIO-RK; P94388; -.
DR   EvolutionaryTrace; P94388; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046555; F:acetylxylan esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047739; F:cephalosporin-C deacetylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005976; P:polysaccharide metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008391; AXE1_dom.
DR   InterPro; IPR039069; CE7.
DR   PANTHER; PTHR40111; PTHR40111; 1.
DR   Pfam; PF05448; AXE1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P94388.
DR   SWISS-2DPAGE; P94388.
KW   3D-structure; Carbohydrate metabolism; Cellulose degradation; Cytoplasm;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Serine esterase.
FT   CHAIN           1..318
FT                   /note="Cephalosporin-C deacetylase"
FT                   /id="PRO_0000360523"
FT   ACT_SITE        181
FT                   /note="Nucleophile"
FT   ACT_SITE        269
FT                   /note="Charge relay system"
FT   ACT_SITE        298
FT                   /note="Charge relay system"
FT   BINDING         91
FT                   /note="Substrate; via amide nitrogen"
FT   MUTAGEN         181
FT                   /note="S->A: Loss of activity."
FT   HELIX           8..12
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           24..36
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          43..47
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          52..63
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           64..66
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          67..78
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          82..88
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           96..98
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           99..107
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          111..115
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   TURN            118..120
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          121..123
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          129..131
FT                   /evidence="ECO:0000244|PDB:1ODT"
FT   STRAND          134..137
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   TURN            138..143
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   TURN            145..147
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           149..166
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          170..180
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           182..193
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          198..204
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           210..216
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   TURN            220..223
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           224..231
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           235..246
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           250..253
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           254..256
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          261..266
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          270..272
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           274..283
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   STRAND          286..293
FT                   /evidence="ECO:0000244|PDB:1L7A"
FT   HELIX           302..316
FT                   /evidence="ECO:0000244|PDB:1L7A"
SQ   SEQUENCE   318 AA;  35807 MW;  BA0D95A34CB503C3 CRC64;
     MQLFDLPLDQ LQTYKPEKTA PKDFSEFWKL SLEELAKVQA EPDLQPVDYP ADGVKVYRLT
     YKSFGNARIT GWYAVPDKEG PHPAIVKYHG YNASYDGEIH EMVNWALHGY ATFGMLVRGQ
     QSSEDTSISP HGHALGWMTK GILDKDTYYY RGVYLDAVRA LEVISSFDEV DETRIGVTGG
     SQGGGLTIAA AALSDIPKAA VADYPYLSNF ERAIDVALEQ PYLEINSFFR RNGSPETEVQ
     AMKTLSYFDI MNLADRVKVP VLMSIGLIDK VTPPSTVFAA YNHLETKKEL KVYRYFGHEY
     IPAFQTEKLA FFKQHLKG
//

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