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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)DescriptionActionsGraphical viewLength
Active sitei208Sequence analysis1
Active sitei421Sequence analysis1

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)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000186781 – 711 PublicationAdd BLAST71
ChainiPRO_000001867972 – 318Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 1Add BLAST247
ChainiPRO_0000018680319 – 444Acetyl-CoA--deacetylcephalosporin C O-acetyltransferase chain 2Add BLAST126

Proteomic databases

PRIDEiP39058.

Interactioni

Subunit structurei

Heterodimer of chain I and chain II.

Structurei

Secondary structure

1444
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi67 – 70Combined sources4
Beta strandi76 – 84Combined sources9
Beta strandi90 – 102Combined sources13
Beta strandi111 – 115Combined sources5
Helixi124 – 126Combined sources3
Helixi129 – 131Combined sources3
Beta strandi136 – 138Combined sources3
Turni140 – 142Combined sources3
Beta strandi144 – 148Combined sources5
Beta strandi154 – 159Combined sources6
Turni165 – 167Combined sources3
Helixi174 – 176Combined sources3
Helixi182 – 196Combined sources15
Beta strandi201 – 207Combined sources7
Helixi209 – 217Combined sources9
Helixi218 – 220Combined sources3
Turni222 – 224Combined sources3
Beta strandi228 – 232Combined sources5
Helixi239 – 254Combined sources16
Helixi259 – 261Combined sources3
Helixi270 – 283Combined sources14
Helixi287 – 293Combined sources7
Helixi330 – 332Combined sources3
Helixi333 – 346Combined sources14
Helixi350 – 361Combined sources12
Turni365 – 369Combined sources5
Helixi373 – 377Combined sources5
Beta strandi384 – 388Combined sources5
Beta strandi393 – 395Combined sources3
Helixi397 – 406Combined sources10
Beta strandi410 – 414Combined sources5
Helixi420 – 422Combined sources3
Helixi423 – 426Combined sources4
Helixi428 – 439Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP39058.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39058.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini112 – 425AB hydrolase-1Sequence analysisAdd BLAST314

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
PDB 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.
SMRiP39058.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERicepac-cefg. Homoserine_transacetylase.

Proteomic databases

PRIDEiP39058.

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: November 2, 2016
This is version 89 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.