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Protein

Malonyl CoA-acyl carrier protein transacylase

Gene

fabD

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Miscellaneous

Was identified as a natural substrate of the M.tuberculosis proteasome.
Was identified as a high-confidence drug target.

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 sitei91By similarity1
Active sitei194By similarity1

GO - Molecular functioni

  • [acyl-carrier-protein] S-malonyltransferase activity Source: MTBBASE

GO - Biological processi

  • fatty acid biosynthetic process Source: MTBBASE

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Chemistry databases

SwissLipidsiSLP:000000965.

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:Rv2243
ORF Names:MTCY427.24
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv2243.

Subcellular locationi

GO - Cellular componenti

  • fatty acid synthase complex Source: MTBBASE

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi173K → A: Nearly abolishes pupylation and dramatically stabilizes this proteasome substrate in wild-type mycobacteria. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001942181 – 302Malonyl CoA-acyl carrier protein transacylaseAdd BLAST302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki173Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)2 Publications

Post-translational modificationi

Pupylated at Lys-173 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome.2 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP9WNG5.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv2243.

Structurei

Secondary structure

1302
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 6Combined sources6
Turni14 – 22Combined sources9
Helixi26 – 36Combined sources11
Helixi41 – 46Combined sources6
Helixi50 – 53Combined sources4
Helixi56 – 76Combined sources21
Turni77 – 82Combined sources6
Beta strandi85 – 89Combined sources5
Helixi93 – 100Combined sources8
Helixi106 – 124Combined sources19
Beta strandi129 – 137Combined sources9
Helixi139 – 148Combined sources10
Beta strandi152 – 158Combined sources7
Beta strandi161 – 167Combined sources7
Helixi168 – 176Combined sources9
Beta strandi183 – 186Combined sources4
Helixi196 – 201Combined sources6
Helixi202 – 210Combined sources9
Beta strandi218 – 222Combined sources5
Turni224 – 226Combined sources3
Helixi233 – 242Combined sources10
Helixi243 – 245Combined sources3
Helixi250 – 259Combined sources10
Beta strandi262 – 267Combined sources6
Helixi274 – 281Combined sources8
Beta strandi287 – 289Combined sources3
Helixi293 – 295Combined sources3
Turni296 – 300Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QC3X-ray2.30A1-302[»]
2QJ3X-ray3.00A/B1-302[»]
ProteinModelPortaliP9WNG5.
SMRiP9WNG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi206 – 210Poly-Ala5
Compositional biasi233 – 236Poly-Ala4

Sequence similaritiesi

Belongs to the FabD family.Curated

Phylogenomic databases

eggNOGiENOG4105CJF. Bacteria.
COG0331. LUCA.
KOiK00645.
OMAiAANYNCP.
PhylomeDBiP9WNG5.

Family and domain databases

InterProiView protein in InterPro
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR020801. PKS_acyl_transferase.
PfamiView protein in Pfam
PF00698. Acyl_transf_1. 1 hit.
SMARTiView protein in SMART
SM00827. PKS_AT. 1 hit.
SUPFAMiSSF52151. SSF52151. 2 hits.
SSF55048. SSF55048. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WNG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIALLAPGQG SQTEGMLSPW LQLPGAADQI AAWSKAADLD LARLGTTAST
60 70 80 90 100
EEITDTAVAQ PLIVAATLLA HQELARRCVL AGKDVIVAGH SVGEIAAYAI
110 120 130 140 150
AGVIAADDAV ALAATRGAEM AKACATEPTG MSAVLGGDET EVLSRLEQLD
160 170 180 190 200
LVPANRNAAG QIVAAGRLTA LEKLAEDPPA KARVRALGVA GAFHTEFMAP
210 220 230 240 250
ALDGFAAAAA NIATADPTAT LLSNRDGKPV TSAAAAMDTL VSQLTQPVRW
260 270 280 290 300
DLCTATLREH TVTAIVEFPP AGTLSGIAKR ELRGVPARAV KSPADLDELA

NL
Length:302
Mass (Da):30,788
Last modified:April 16, 2014 - v1
Checksum:iBB7BCD8217FC66C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP45023.1.
PIRiG70778.
RefSeqiNP_216759.1. NC_000962.3.
WP_003411559.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP45023; CCP45023; Rv2243.
GeneIDi888769.
KEGGimtu:Rv2243.

Similar proteinsi

Entry informationi

Entry nameiFABD_MYCTU
AccessioniPrimary (citable) accession number: P9WNG5
Secondary accession number(s): L0TAL7, P63458, Q10501
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: June 7, 2017
This is version 21 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families