CEFG_ACRCH
ID CEFG_ACRCH Reviewed; 444 AA.
AC P39058;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acetyl-CoA--deacetylcephalosporin C acetyltransferase;
DE Short=DAC acetyltransferase;
DE Short=DAC-AT;
DE Short=DCPC-ATF;
DE EC=2.3.1.175 {ECO:0000269|PubMed:1569032};
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 Acremonium chrysogenum (Cephalosporium acremonium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreales incertae sedis; Acremonium.
OX NCBI_TaxID=5044;
RN [1]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C10;
RX PubMed=1569032; DOI=10.1128/jb.174.9.3056-3064.1992;
RA Gutierrez S., Velasco J., Fernandez F.J., Martin J.F.;
RT "The cefG gene of Cephalosporium acremonium is linked to the cefEF gene and
RT encodes a deacetylcephalosporin C acetyltransferase closely related to
RT homoserine O-acetyltransferase.";
RL J. Bacteriol. 174:3056-3064(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PF14-1;
RX 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 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 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 AND
RP 319-345.
RC STRAIN=IS-5;
RX 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 expression
RT 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. {ECO:0000269|PubMed:1569032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + deacetylcephalosporin C = cephalosporin C + CoA;
CC Xref=Rhea:RHEA:23860, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57511, ChEBI:CHEBI:58366; EC=2.3.1.175;
CC Evidence={ECO:0000269|PubMed:1569032};
CC -!- PATHWAY: Antibiotic biosynthesis; cephalosporin C biosynthesis.
CC -!- SUBUNIT: Heterodimer of chain I and chain II.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-46 or Met-60 is the
CC initiator. {ECO:0000305}.
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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 AlphaFoldDB; P39058; -.
DR SMR; P39058; -.
DR ESTHER; cepac-cefg; Homoserine_transacetylase.
DR KEGG; ag:AAA32673; -.
DR BioCyc; MetaCyc:MON-13419; -.
DR BRENDA; 2.3.1.175; 114.
DR UniPathway; UPA00172; -.
DR EvolutionaryTrace; P39058; -.
DR GO; GO:0033813; F:deacetylcephalosporin-C acetyltransferase activity; IMP:CACAO.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic biosynthesis;
KW Direct protein sequencing; Transferase.
FT PROPEP 1..71
FT /evidence="ECO:0000269|PubMed:1540196"
FT /id="PRO_0000018678"
FT CHAIN 72..318
FT /note="Acetyl-CoA--deacetylcephalosporin C O-
FT acetyltransferase chain 1"
FT /id="PRO_0000018679"
FT CHAIN 319..444
FT /note="Acetyl-CoA--deacetylcephalosporin C O-
FT acetyltransferase chain 2"
FT /id="PRO_0000018680"
FT DOMAIN 112..425
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 208
FT /evidence="ECO:0000255"
FT ACT_SITE 421
FT /evidence="ECO:0000255"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 90..102
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2VAT"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2VAT"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 182..196
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:2VAT"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 287..293
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:2VAT"
FT TURN 365..369
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:2VAT"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:2VAT"
FT HELIX 428..439
FT /evidence="ECO:0007829|PDB:2VAT"
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
