Skip Header

Contribute Send feedback
Read comments (?) or add your own

P63458 (FABD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malonyl CoA-acyl carrier protein transacylase

Short name=MCT
EC=2.3.1.39
Gene names
Name:fabD
Ordered Locus Names:Rv2243, MT2303
ORF Names:MTCY427.24
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Pathway

Lipid metabolism; fatty acid biosynthesis.

Post-translational modification

Pupylated at Lys-173 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome. Ref.4 Ref.6

Miscellaneous

Was identified as a natural substrate of the M.tuberculosis proteasome.

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the FabD family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 302302Malonyl CoA-acyl carrier protein transacylase
PRO_0000194218

Regions

Compositional bias206 – 2105Poly-Ala
Compositional bias233 – 2364Poly-Ala

Sites

Active site911 By similarity
Active site1941 By similarity

Amino acid modifications

Cross-link173Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Experimental info

Mutagenesis1731K → A: Nearly abolishes pupylation and dramatically stabilizes this proteasome substrate in wild-type mycobacteria. Ref.4

Secondary structure

................................................... 302
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63458 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: BB7BCD8217FC66C8

FASTA30230,788
        10         20         30         40         50         60 
MIALLAPGQG SQTEGMLSPW LQLPGAADQI AAWSKAADLD LARLGTTAST EEITDTAVAQ 

        70         80         90        100        110        120 
PLIVAATLLA HQELARRCVL AGKDVIVAGH SVGEIAAYAI AGVIAADDAV ALAATRGAEM 

       130        140        150        160        170        180 
AKACATEPTG MSAVLGGDET EVLSRLEQLD LVPANRNAAG QIVAAGRLTA LEKLAEDPPA 

       190        200        210        220        230        240 
KARVRALGVA GAFHTEFMAP ALDGFAAAAA NIATADPTAT LLSNRDGKPV TSAAAAMDTL 

       250        260        270        280        290        300 
VSQLTQPVRW DLCTATLREH TVTAIVEFPP AGTLSGIAKR ELRGVPARAV KSPADLDELA 


NL 

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"Identification of substrates of the Mycobacterium tuberculosis proteasome."
Pearce M.J., Arora P., Festa R.A., Butler-Wu S.M., Gokhale R.S., Darwin K.H.
EMBO J. 25:5423-5432(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEASOME SUBSTRATE.
Strain: ATCC 25618 / H37Rv.
[4]"Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis."
Pearce M.J., Mintseris J., Ferreyra J., Gygi S.P., Darwin K.H.
Science 322:1104-1107(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PUPYLATION AT LYS-173, MASS SPECTROMETRY, MUTAGENESIS OF LYS-173.
Strain: ATCC 25618 / H37Rv.
[5]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[6]"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis."
Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H.
PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PUPYLATION AT LYS-173, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842579 Genomic DNA. Translation: CAA94639.1.
AE000516 Genomic DNA. Translation: AAK46587.1.
AL123456 Genomic DNA. Translation: CCP45023.1.
PIRG70778.
RefSeqNP_216759.1. NC_000962.3.
NP_336773.1. NC_002755.2.
YP_006515666.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QC3X-ray2.30A1-302[»]
2QJ3X-ray3.00A/B1-302[»]
ProteinModelPortalP63458.
SMRP63458. Positions 1-302.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2243.

PTM databases

PhosSiteP0805316.

Proteomic databases

PRIDEP63458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK46587; AAK46587; MT2303.
GeneID13318936.
888769.
924123.
KEGGmtc:MT2303.
mtu:Rv2243.
mtv:RVBD_2243.
PATRIC18126813. VBIMycTub22151_2517.

Organism-specific databases

TubercuListRv2243.

Phylogenomic databases

eggNOGCOG0331.
HOGENOMHOG000036505.
KOK00645.
OMAAFHTRFM.
ProtClustDBCLSK872033.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D3.40.366.10. 2 hits.
InterProIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR016036. Malonyl_transacylase_ACP-bd.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
SUPFAMSSF52151. Acyl_Trfase/lysoPlipase. 1 hit.
SSF55048. Malonyl_transacylase_ACP-bd. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP63458.

Entry information

Entry nameFABD_MYCTU
AccessionPrimary (citable) accession number: P63458
Secondary accession number(s): L0TAL7, Q10501
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families