Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P0C5C2 (CFA1_MYCTU)

Last modified February 9, 2010. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Cyclopropane-fatty-acyl-phospholipid synthase 1
      Short name=Cyclopropane fatty acid synthase
      Short name=CFA synthase
    EC=2.1.1.79
Alternative name(s):
    Cyclopropane mycolic acid synthase 1
Gene names
Name: cmaA1
Synonyms: cma1
Ordered Locus Names: Rv3392c, MT3499
ORF Names: MTV004.50
OrganismMycobacterium tuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Hide | Top

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. Mycolic acids, which represent the major constituent of mycobacterial cell wall complex, act as substrates By similarity.

Catalytic activity

S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.

Subcellular location

Cytoplasm By similarity.

Hide | Top

Ontologies

Keywords
   Biological processLipid synthesis
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processlipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncyclopropane-fatty-acyl-phospholipid synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287Cyclopropane-fatty-acyl-phospholipid synthase 1
PRO_0000089566

Regions

Region33 – 342S-adenosyl-L-methionine binding
Region68 – 769S-adenosyl-L-methionine binding
Region94 – 996S-adenosyl-L-methionine binding

Sites

Site2691Essential for catalysis Probable

Experimental info

Sequence conflict2501A → D in AAK47836. Ref.2

Secondary structure

1 .............................................. 287
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P0C5C2-1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 7E254C15DF5FFF97

FASTA28732,461
        10         20         30         40         50         60 
MPDELKPHFA NVQAHYDLSD DFFRLFLDPT QTYSCAYFER DDMTLQEAQI AKIDLALGKL 

        70         80         90        100        110        120 
GLQPGMTLLD VGCGWGATMM RAVEKYDVNV VGLTLSKNQA NHVQQLVANS ENLRSKRVLL 

       130        140        150        160        170        180 
AGWEQFDEPV DRIVSIGAFE HFGHERYDAF FSLAHRLLPA DGVMLLHTIT GLHPKEIHER 

       190        200        210        220        230        240 
GLPMSFTFAR FLKFIVTEIF PGGRLPSIPM VQECASANGF TVTRVQSLQP HYAKTLDLWS 

       250        260        270        280 
AALQANKGQA IALQSEEVYE RYMKYLTGCA EMFRIGYIDV NQFTCQK

« Hide

Hide | Top

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]"Crystal structures of mycolic acid cyclopropane synthases from Mycobacterium tuberculosis."
Huang C.-C., Smith C.V., Glickman M.S., Jacobs W.R. Jr., Sacchettini J.C.
J. Biol. Chem. 277:11559-11569(2002) [PubMed: 11756461] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 18-287.

Hide | Top

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842582 Genomic DNA. Translation: CAA15777.1.
AE000516 Genomic DNA. Translation: AAK47836.1.
PIRG70974.
RefSeqNP_217909.1.
NP_338022.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KP9X-ray2.21A/B1-287[»]
1KPGX-ray2.00A/B/C/D1-287[»]
1KPHX-ray2.00A/B/C/D1-287[»]
ModBaseSearch...

Genome annotation databases

GeneID887961.
926573.
GenomeReviewsGene locus MT3499 in contig AE000516_GR.
KEGGmtc:MT3499.
mtu:Rv3392c.
TIGRMT3499.

Organism-specific databases

TubercuListRv3392c.

Phylogenomic databases

HOGENOMHBG687502.
OMAVLAEAYM.

Enzyme and pathway databases

BRENDA2.1.1.79. 809.

Family and domain databases

InterProIPR003333. CMAS.
[Graphical view]
PfamPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFPIRSF003085. CMAS. 1 hit.
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCFA1_MYCTU
AccessionPrimary (citable) accession number: P0C5C2
Secondary accession number(s): Q11195
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: February 9, 2010
This is version 20 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)

Hide | Top

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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