Database: SPTrEMBLEntry: CEFG_CEPAC
LinkDB: CEFG_CEPAC
Original site: CEFG_CEPAC
ID CEFG_CEPAC Reviewed; 444 AA.
AC P39058;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 15-DEC-2009, entry version 61.
DE RecName: Full=Acetyl-CoA--deacetylcephalosporin C acetyltransferase;
DE Short=DCPC-ATF;
DE Short=DAC acetyltransferase;
DE Short=DAC-AT;
DE EC=2.3.1.175;
DE Contains:
DE RecName: Full=Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 1;
DE Contains:
DE RecName: Full=Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 2;
DE Flags: Precursor;
GN Name=CEFG;
OS Cephalosporium acremonium (Acremonium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC Sordariomycetes; Hypocreomycetidae; Hypocreales;
OC mitosporic Hypocreales; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C10;
RX MEDLINE=92234966; PubMed=1569032;
RA Gutierrez S., Velasco J., Fernandez F.J., Martin J.F.;
RT "The cefG gene of Cephalosporium acremonium is linked to the cefEF
RT gene and encodes a deacetylcephalosporin C acetyltransferase closely
RT related to homoserine O-acetyltransferase.";
RL J. Bacteriol. 174:3056-3064(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PF14-1;
RX MEDLINE=93153828; PubMed=8428381; DOI=10.1007/BF00336747;
RA Mathison L., Soliday C., Stepan T., Aldrich T., Rambosek J.;
RT "Cloning, characterization, and use in strain improvement of the
RT Cephalosporium acremonium gene cefG encoding acetyl transferase.";
RL Curr. Genet. 23:33-41(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 60-444.
RC STRAIN=IS-5;
RX MEDLINE=92337627; PubMed=1632779; DOI=10.1016/S0006-291X(05)80772-7;
RA Matsuda A., Sugiura H., Matsuyama K., Matsumoto H., Ichikawa S.,
RA Komatsu K.;
RT "Cloning and disruption of the cefG gene encoding acetyl coenzyme A:
RT deacetylcephalosporin C o-acetyltransferase from Acremonium
RT chrysogenum.";
RL Biochem. Biophys. Res. Commun. 186:40-46(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-444, AND PROTEIN SEQUENCE OF 72-91
RP AND 319-345.
RC STRAIN=IS-5;
RX MEDLINE=92171978; PubMed=1540196; DOI=10.1016/0006-291X(92)91830-J;
RA Matsuda A., Sugiura H., Matsuyama K., Matsumoto H., Ichikawa S.,
RA Komatsu K.;
RT "Molecular cloning of acetyl coenzyme A: deacetylcephalosporin C o-
RT acetyltransferase cDNA from Acremonium chrysogenum: sequence and
RT expression of catalytic activity in yeast.";
RL Biochem. Biophys. Res. Commun. 182:995-1001(1992).
CC -!- FUNCTION: Catalyzes the conversion of deacetylcephalosporin C to
CC cephalosporin C.
CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + deacetylcephalosporin C = CoA +
CC cephalosporin C.
CC -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC -!- SUBUNIT: Heterodimer of chain I and chain II.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. HTA family.
CC -!- CAUTION: It is uncertain whether Met-1, Met-46 or Met-60 is the
CC initiator.
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DR EMBL; S83551; AAB21471.2; -; mRNA.
DR EMBL; M91649; AAA32673.1; -; Genomic_DNA.
DR EMBL; X65583; CAA46542.1; -; Genomic_DNA.
DR EMBL; S39881; AAB22484.1; -; Genomic_DNA.
DR PIR; B41864; B41864.
DR PDB; 2VAT; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=1-444.
DR PDB; 2VAV; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-444.
DR PDB; 2VAX; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L=1-444.
DR PDBsum; 2VAT; -.
DR PDBsum; 2VAV; -.
DR PDBsum; 2VAX; -.
DR BioCyc; MetaCyc:MONOMER-13419; -.
DR BRENDA; 2.3.1.175; 66776.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0033813; F:deacetylcephalosporin-C acetyltransferase a...; IEA:EC.
DR GO; GO:0004414; F:homoserine O-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; Homoserine_AcTrfase.
DR InterPro; IPR006296; Homoserine_O-AcTrfase.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic biosynthesis;
KW Direct protein sequencing; Transferase.
FT PROPEP 1 71
FT /FTId=PRO_0000018678.
FT CHAIN 72 318 Acetyl-CoA--deacetylcephalosporin C O-
FT acetyltransferase chain 1.
FT /FTId=PRO_0000018679.
FT CHAIN 319 444 Acetyl-CoA--deacetylcephalosporin C O-
FT acetyltransferase chain 2.
FT /FTId=PRO_0000018680.
FT ACT_SITE 208 208 Potential.
FT ACT_SITE 421 421 Potential.
FT HELIX 67 70
FT STRAND 76 84
FT STRAND 90 101
FT STRAND 111 114
FT HELIX 124 126
FT HELIX 129 131
FT TURN 140 142
FT STRAND 144 148
FT TURN 165 167
FT HELIX 182 195
FT STRAND 201 205
FT HELIX 213 217
FT HELIX 241 254
FT TURN 256 258
FT HELIX 274 283
FT HELIX 287 293
FT HELIX 330 332
FT HELIX 333 346
FT HELIX 350 361
FT HELIX 373 377
FT STRAND 384 388
FT HELIX 397 402
FT STRAND 410 414
FT HELIX 423 426
FT HELIX 428 435
SQ SEQUENCE 444 AA; 49161 MW; EFED6FA7FCAFB047 CRC64;
MLPSAQVARL KPDPFPPSLS PIPHGAVTFA ALAPCHNLPI FSSRQMLRDS LTYSHTSPTM
SPQIANRFEA SLDAQDIARI SLFTLESGVI LRDVPVAYKS WGRMNVSRDN CVIVCHTLTS
SAHVTSWWPT LFGQGRAFDT SRYFIICLNY LGSPFGSAGP CSPDPDAEGQ RPYGAKFPRT
TIRDDVRIHR QVLDRLGVRQ IAAVVGASMG GMHTLEWAFF GPEYVRKIVP IATSCRQSGW
CAAWFETQRQ CIYDDPKYLD GEYDVDDQPV RGLETARKIA NLTYKSKPAM DERFHMAPGV
QAGRNISSQD AKKEINGTDS GNSHRAGQPI EAVSSYLRYQ AQKFAASFDA NCYIAMTLKF
DTHDISRGRA GSIPEALAMI TQPALIICAR SDGLYSFDEH VEMGRSIPNS RLCVVDTNEG
HDFFVMEADK VNDAVRGFLD QSLM
//
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