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Protein

Acetyl-CoA--deacetylcephalosporin C acetyltransferase

Gene

CEFG

Organism
Acremonium chrysogenum (Cephalosporium acremonium)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C.

Catalytic activityi

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

Pathwayi: cephalosporin C biosynthesis

This protein is involved in the pathway cephalosporin C biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway cephalosporin C biosynthesis and in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei208 – 2081Sequence analysis
Active sitei421 – 4211Sequence analysis

GO - Molecular functioni

  • deacetylcephalosporin-C acetyltransferase activity Source: CACAO
  • homoserine O-acetyltransferase activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13419.
BRENDAi2.3.1.175. 114.
UniPathwayiUPA00172.

Protein family/group databases

ESTHERicepac-cefg. Homoserine_transacetylase.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA--deacetylcephalosporin C acetyltransferase (EC:2.3.1.175)
Short name:
DAC acetyltransferase
Short name:
DAC-AT
Short name:
DCPC-ATF
Cleaved into the following 2 chains:
Gene namesi
Name:CEFG
OrganismiAcremonium chrysogenum (Cephalosporium acremonium)
Taxonomic identifieri5044 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreales incertae sedisAcremonium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 71711 PublicationPRO_0000018678Add
BLAST
Chaini72 – 318247Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 1PRO_0000018679Add
BLAST
Chaini319 – 444126Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 2PRO_0000018680Add
BLAST

Interactioni

Subunit structurei

Heterodimer of chain I and chain II.

Structurei

Secondary structure

1
444
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi67 – 704Combined sources
Beta strandi76 – 849Combined sources
Beta strandi90 – 10213Combined sources
Beta strandi111 – 1155Combined sources
Helixi124 – 1263Combined sources
Helixi129 – 1313Combined sources
Beta strandi136 – 1383Combined sources
Turni140 – 1423Combined sources
Beta strandi144 – 1485Combined sources
Beta strandi154 – 1596Combined sources
Turni165 – 1673Combined sources
Helixi174 – 1763Combined sources
Helixi182 – 19615Combined sources
Beta strandi201 – 2077Combined sources
Helixi209 – 2179Combined sources
Helixi218 – 2203Combined sources
Turni222 – 2243Combined sources
Beta strandi228 – 2325Combined sources
Helixi239 – 25416Combined sources
Helixi259 – 2613Combined sources
Helixi270 – 28314Combined sources
Helixi287 – 2937Combined sources
Helixi330 – 3323Combined sources
Helixi333 – 34614Combined sources
Helixi350 – 36112Combined sources
Turni365 – 3695Combined sources
Helixi373 – 3775Combined sources
Beta strandi384 – 3885Combined sources
Beta strandi393 – 3953Combined sources
Helixi397 – 40610Combined sources
Beta strandi410 – 4145Combined sources
Helixi420 – 4223Combined sources
Helixi423 – 4264Combined sources
Helixi428 – 43912Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP39058.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39058.

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily. HTA family.Curated

Family and domain databases

Gene3Di3.40.50.1820. 3 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR008220. Homoserine_AcTrfase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000443. Homoser_Ac_trans. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01392. homoserO_Ac_trn. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39058-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPSAQVARL KPDPFPPSLS PIPHGAVTFA ALAPCHNLPI FSSRQMLRDS
60 70 80 90 100
LTYSHTSPTM SPQIANRFEA SLDAQDIARI SLFTLESGVI LRDVPVAYKS
110 120 130 140 150
WGRMNVSRDN CVIVCHTLTS SAHVTSWWPT LFGQGRAFDT SRYFIICLNY
160 170 180 190 200
LGSPFGSAGP CSPDPDAEGQ RPYGAKFPRT TIRDDVRIHR QVLDRLGVRQ
210 220 230 240 250
IAAVVGASMG GMHTLEWAFF GPEYVRKIVP IATSCRQSGW CAAWFETQRQ
260 270 280 290 300
CIYDDPKYLD GEYDVDDQPV RGLETARKIA NLTYKSKPAM DERFHMAPGV
310 320 330 340 350
QAGRNISSQD AKKEINGTDS GNSHRAGQPI EAVSSYLRYQ AQKFAASFDA
360 370 380 390 400
NCYIAMTLKF DTHDISRGRA GSIPEALAMI TQPALIICAR SDGLYSFDEH
410 420 430 440
VEMGRSIPNS RLCVVDTNEG HDFFVMEADK VNDAVRGFLD QSLM
Length:444
Mass (Da):49,161
Last modified:February 1, 1995 - v1
Checksum:iEFED6FA7FCAFB047
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83551 mRNA. Translation: AAB21471.2.
M91649 Genomic DNA. Translation: AAA32673.1.
X65583 Genomic DNA. Translation: CAA46542.1.
S39881 Genomic DNA. Translation: AAB22484.1.
PIRiB41864.

Genome annotation databases

KEGGiag:AAA32673.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S83551 mRNA. Translation: AAB21471.2.
M91649 Genomic DNA. Translation: AAA32673.1.
X65583 Genomic DNA. Translation: CAA46542.1.
S39881 Genomic DNA. Translation: AAB22484.1.
PIRiB41864.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP39058.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERicepac-cefg. Homoserine_transacetylase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA32673.

Enzyme and pathway databases

UniPathwayiUPA00172.
BioCyciMetaCyc:MONOMER-13419.
BRENDAi2.3.1.175. 114.

Miscellaneous databases

EvolutionaryTraceiP39058.

Family and domain databases

Gene3Di3.40.50.1820. 3 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR008220. Homoserine_AcTrfase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000443. Homoser_Ac_trans. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01392. homoserO_Ac_trn. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCEFG_ACRCH
AccessioniPrimary (citable) accession number: P39058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.