Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Malonyl CoA-acyl carrier protein transacylase

Gene

fabD

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei89By similarity1
Active sitei199By similarity1

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

BRENDAi2.3.1.39. 3352.
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
Ordered Locus Names:SAV1230
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000002481 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001942241 – 308Malonyl CoA-acyl carrier protein transacylaseAdd BLAST308

Proteomic databases

PaxDbiQ99UN8.

2D gel databases

World-2DPAGE0002:Q99UN8.

Interactioni

Protein-protein interaction databases

STRINGi158878.SAV1230.

Structurei

Secondary structure

1308
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni16 – 25Combined sources10
Helixi27 – 39Combined sources13
Helixi44 – 49Combined sources6
Helixi59 – 76Combined sources18
Beta strandi83 – 88Combined sources6
Helixi91 – 98Combined sources8
Helixi104 – 120Combined sources17
Beta strandi126 – 134Combined sources9
Helixi137 – 147Combined sources11
Beta strandi154 – 161Combined sources8
Beta strandi164 – 170Combined sources7
Helixi171 – 180Combined sources10
Turni181 – 185Combined sources5
Beta strandi187 – 191Combined sources5
Helixi201 – 206Combined sources6
Helixi207 – 214Combined sources8
Turni229 – 231Combined sources3
Beta strandi233 – 235Combined sources3
Helixi238 – 248Combined sources11
Helixi255 – 264Combined sources10
Beta strandi267 – 276Combined sources10
Helixi278 – 286Combined sources9
Beta strandi288 – 295Combined sources8
Helixi298 – 304Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IM9X-ray1.46A5-308[»]
ProteinModelPortaliQ99UN8.
SMRiQ99UN8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99UN8.

Family & Domainsi

Sequence similaritiesi

Belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiENOG4105CJF. Bacteria.
COG0331. LUCA.
HOGENOMiHOG000036504.
KOiK00645.
OMAiFHCALMQ.
PhylomeDBiQ99UN8.

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.
IPR020801. PKS_acyl_transferase.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SMARTiSM00827. PKS_AT. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99UN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTAIIFPG QGAQKVGMAQ DLFNNNDQAT EILTSAAKTL 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):33,649
Last modified:June 1, 2001 - v1
Checksum:iB2FAEF8A200804C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57392.1.
RefSeqiWP_000047343.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57392; BAB57392; SAV1230.
KEGGisav:SAV1230.
PATRICi19563173. VBIStaAur52173_1264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000017 Genomic DNA. Translation: BAB57392.1.
RefSeqiWP_000047343.1. NC_002758.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IM9X-ray1.46A5-308[»]
ProteinModelPortaliQ99UN8.
SMRiQ99UN8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi158878.SAV1230.

2D gel databases

World-2DPAGE0002:Q99UN8.

Proteomic databases

PaxDbiQ99UN8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB57392; BAB57392; SAV1230.
KEGGisav:SAV1230.
PATRICi19563173. VBIStaAur52173_1264.

Phylogenomic databases

eggNOGiENOG4105CJF. Bacteria.
COG0331. LUCA.
HOGENOMiHOG000036504.
KOiK00645.
OMAiFHCALMQ.
PhylomeDBiQ99UN8.

Enzyme and pathway databases

UniPathwayiUPA00094.
BRENDAi2.3.1.39. 3352.

Miscellaneous databases

EvolutionaryTraceiQ99UN8.

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.
IPR020801. PKS_acyl_transferase.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000446. Mct. 1 hit.
SMARTiSM00827. PKS_AT. 1 hit.
[Graphical view]
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.
TIGRFAMsiTIGR00128. fabD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFABD_STAAM
AccessioniPrimary (citable) accession number: Q99UN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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.