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Reviewed, UniProtKB/Swiss-Prot P63458 (FABD_MYCTU)

Last modified November 3, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 [Complete proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

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Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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 on Lys-173 by the prokaryotic ubiquitin-like protein pup, which leads to its degradation by the proteasome. Ref.4

Miscellaneous

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

Sequence similarities

Belongs to the fabD family.

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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-link173Glutamyl lysine isopeptide (Lys-Glu) (interchain with E-Cter in protein pup) Ref.4

Experimental info

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

Secondary structure

1 ................................................... 302
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P63458-1 [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

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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: 9634230] [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: 12218036] [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: 17082771] [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: 18832610] [Abstract]
Cited for: PUPYLATION AT LYS-173, MASS SPECTROMETRY, MUTAGENESIS OF LYS-173.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

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Cross-references

Sequence databases

BX842579 Genomic DNA. Translation: CAA94639.1.
AE000516 Genomic DNA. Translation: AAK46587.1.
PIRG70778.
RefSeqNP_216759.1.
NP_336773.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2QC3X-ray2.30A1-302[»]
2QJ3X-ray3.00A/B1-302[»]
ModBaseSearch...

PTM databases

PhosSiteP63458.

Genome annotation databases

GeneID888769.
924123.
GenomeReviewsGene locus MT2303 in contig AE000516_GR.
Gene locus Rv2243 in contig AL123456_GR.
KEGGmtc:MT2303.
mtu:Rv2243.
TIGRMT2303.

Organism-specific databases

TubercuListRv2243.

Phylogenomic databases

HOGENOMP63458.
OMAAFHTHHM.

Enzyme and pathway databases

BRENDA2.3.1.39. 809.

Family and domain databases

InterProIPR001227. Ac_transferase_reg.
IPR014043. Acyl_transferase.
[Graphical view]
Gene3DG3DSA:3.40.366.10. Ac_transferase_reg. 1 hit.
PfamPF00698. Acyl_transf_1. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFABD_MYCTU
AccessionPrimary (citable) accession number: P63458
Secondary accession number(s): Q10501
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents