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Protein

Malonyl CoA-acyl carrier protein transacylase

Gene

fabD

Organism
Staphylococcus aureus
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].

Pathway: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891By similarity
Active sitei199 – 1991By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Malonyl CoA-acyl carrier protein transacylase (EC:2.3.1.39)
Short name:
MCT
Gene namesi
Name:fabD
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Malonyl CoA-acyl carrier protein transacylasePRO_0000194220Add
BLAST

Proteomic databases

PRIDEiQ93QD4.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV1230.

Structurei

3D structure databases

ProteinModelPortaliQ93QD4.
SMRiQ93QD4. Positions 2-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiCOG0331.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q93QD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTAIIFPG QGAQKVGMAQ DLFNNNDQAT EILTSAANTL DFDILETMFT
60 70 80 90 100
DEEGKLGETE NTQPALLTHS SALLAALKNL NPDFTMGHSL GEYSSLVAAD
110 120 130 140 150
VLSFEDAVKI VRKRGQLMAQ AFPTGVGSMA AVLGLDFDKV DEICKSLSSD
160 170 180 190 200
DKIIEPANIN CPGQIVVSGH KALIDELVEK GKSLGAKRVM PLAVSGPFHS
210 220 230 240 250
SLMKVIEEDF SSYINQFEWR DAKFPVVQNV NAQGETDKEV IKSNMVKQLY
260 270 280 290 300
SPVQFINSTE WLIDQGVDHF IEIGPGKVLS GLIKKINRDV KLTSIQTLED

VKGWNEND
Length:308
Mass (Da):33,635
Last modified:December 1, 2001 - v1
Checksum:iC28AEC6CC50805C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231F → Y in BAD72836 (Ref. 2) Curated
Sequence conflicti53 – 531E → D in BAD72836 (Ref. 2) Curated
Sequence conflicti220 – 2201R → H in BAD72836 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF275318 Genomic DNA. Translation: AAK69406.1.
AB195288 Genomic DNA. Translation: BAD72836.1.
RefSeqiWP_000047348.1. NZ_KN050644.1.

Genome annotation databases

GeneIDi23197039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF275318 Genomic DNA. Translation: AAK69406.1.
AB195288 Genomic DNA. Translation: BAD72836.1.
RefSeqiWP_000047348.1. NZ_KN050644.1.

3D structure databases

ProteinModelPortaliQ93QD4.
SMRiQ93QD4. Positions 2-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1230.

Chemistry

ChEMBLiCHEMBL1075258.

Proteomic databases

PRIDEiQ93QD4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi23197039.

Phylogenomic databases

eggNOGiCOG0331.

Enzyme and pathway databases

UniPathwayiUPA00094.

Family and domain databases

Gene3Di3.40.366.10. 2 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR024925. Malonyl_CoA-ACP_transAc.
IPR004410. Malonyl_CoA-ACP_transAc_FabD.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and characterization of S.aureus malonyl-CoA:ACP S-malonyl transferase."
    Lin A.H., Choi G.H., McCroskey M., Harris D.W., Murray R.W., Rockenbach S.K., Curry K.A., Marotti K.R.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and expression of Staphylococcus aureus Smith fab genes."
    Morita Y., Ikeno S., Tsuchiya K.S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-303.
    Strain: Smith.

Entry informationi

Entry nameiFABD_STAAU
AccessioniPrimary (citable) accession number: Q93QD4
Secondary accession number(s): Q5TKS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: December 1, 2001
Last modified: June 24, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.