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P39058 (CEFG_CEPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA--deacetylcephalosporin C acetyltransferase

Short name=DAC acetyltransferase
Short name=DAC-AT
Short name=DCPC-ATF
EC=2.3.1.175
Gene names
Name:CEFG
OrganismCephalosporium acremonium (Acremonium chrysogenum)
Taxonomic identifier5044 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesmitosporic HypocrealesAcremonium

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C.

Catalytic activity

Acetyl-CoA + deacetylcephalosporin C = CoA + cephalosporin C.

Pathway

Antibiotic biosynthesis; cephalosporin C biosynthesis.

Subunit structure

Heterodimer of chain I and chain II.

Sequence similarities

Belongs to the AB hydrolase superfamily. HTA family.

Caution

It is uncertain whether Met-1, Met-46 or Met-60 is the initiator.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 7171
PRO_0000018678
Chain72 – 318247Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 1
PRO_0000018679
Chain319 – 444126Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 2
PRO_0000018680

Sites

Active site2081 Potential
Active site4211 Potential

Secondary structure

.................................................. 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39058 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: EFED6FA7FCAFB047

FASTA44449,161
        10         20         30         40         50         60 
MLPSAQVARL KPDPFPPSLS PIPHGAVTFA ALAPCHNLPI FSSRQMLRDS LTYSHTSPTM 

        70         80         90        100        110        120 
SPQIANRFEA SLDAQDIARI SLFTLESGVI LRDVPVAYKS WGRMNVSRDN CVIVCHTLTS 

       130        140        150        160        170        180 
SAHVTSWWPT LFGQGRAFDT SRYFIICLNY LGSPFGSAGP CSPDPDAEGQ RPYGAKFPRT 

       190        200        210        220        230        240 
TIRDDVRIHR QVLDRLGVRQ IAAVVGASMG GMHTLEWAFF GPEYVRKIVP IATSCRQSGW 

       250        260        270        280        290        300 
CAAWFETQRQ CIYDDPKYLD GEYDVDDQPV RGLETARKIA NLTYKSKPAM DERFHMAPGV 

       310        320        330        340        350        360 
QAGRNISSQD AKKEINGTDS GNSHRAGQPI EAVSSYLRYQ AQKFAASFDA NCYIAMTLKF 

       370        380        390        400        410        420 
DTHDISRGRA GSIPEALAMI TQPALIICAR SDGLYSFDEH VEMGRSIPNS RLCVVDTNEG 

       430        440 
HDFFVMEADK VNDAVRGFLD QSLM 

« Hide

References

[1]"The cefG gene of Cephalosporium acremonium is linked to the cefEF gene and encodes a deacetylcephalosporin C acetyltransferase closely related to homoserine O-acetyltransferase."
Gutierrez S., Velasco J., Fernandez F.J., Martin J.F.
J. Bacteriol. 174:3056-3064(1992) [PubMed: 1569032] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: C10.
[2]"Cloning, characterization, and use in strain improvement of the Cephalosporium acremonium gene cefG encoding acetyl transferase."
Mathison L., Soliday C., Stepan T., Aldrich T., Rambosek J.
Curr. Genet. 23:33-41(1993) [PubMed: 8428381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: PF14-1.
[3]"Cloning and disruption of the cefG gene encoding acetyl coenzyme A: deacetylcephalosporin C o-acetyltransferase from Acremonium chrysogenum."
Matsuda A., Sugiura H., Matsuyama K., Matsumoto H., Ichikawa S., Komatsu K.
Biochem. Biophys. Res. Commun. 186:40-46(1992) [PubMed: 1632779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 60-444.
Strain: IS-5.
[4]"Molecular cloning of acetyl coenzyme A: deacetylcephalosporin C o-acetyltransferase cDNA from Acremonium chrysogenum: sequence and expression of catalytic activity in yeast."
Matsuda A., Sugiura H., Matsuyama K., Matsumoto H., Ichikawa S., Komatsu K.
Biochem. Biophys. Res. Commun. 182:995-1001(1992) [PubMed: 1540196] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-444, PROTEIN SEQUENCE OF 72-91 AND 319-345.
Strain: IS-5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S83551 mRNA. Translation: AAB21471.2.
M91649 Genomic DNA. Translation: AAA32673.1.
X65583 Genomic DNA. Translation: CAA46542.1.
S39881 Genomic DNA. Translation: AAB22484.1.
PIRB41864.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VATX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-444[»]
2VAVX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-444[»]
2VAXX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L1-444[»]
ProteinModelPortalP39058.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13419.

Family and domain databases

InterProIPR000073. AB_hydrolase_1.
IPR008220. Homoserine_AcTrfase.
[Graphical view]
PANTHERPTHR10992:SF262. PTHR10992:SF262. 1 hit.
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFPIRSF000443. Homoser_Ac_trans. 1 hit.
TIGRFAMsTIGR01392. HomoserO_Ac_trn. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCEFG_CEPAC
AccessionPrimary (citable) accession number: P39058
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 19, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families