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 03-AUG-2022, entry version 118.
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}.
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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 AlphaFoldDB; P94388; -.
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; BSU_03180.
DR GeneID; 938341; -.
DR KEGG; bsu:BSU03180; -.
DR PATRIC; fig|224308.179.peg.332; -.
DR eggNOG; COG3458; Bacteria.
DR InParanoid; P94388; -.
DR OMA; VHFAARG; -.
DR BioCyc; BSUB:BSU03180-MON; -.
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:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
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;
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 /ligand="substrate"
FT MUTAGEN 181
FT /note="S->A: Loss of activity."
FT HELIX 8..12
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 52..63
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1L7A"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1ODT"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:1L7A"
FT TURN 138..143
FT /evidence="ECO:0007829|PDB:1L7A"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 149..166
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:1L7A"
FT TURN 220..223
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 235..246
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1L7A"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:1L7A"
FT HELIX 302..316
FT /evidence="ECO:0007829|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
