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P0C5C2 (CMAS1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 47. Feed History...

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

Names and origin

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

Protein attributes

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

General annotation (Comments)

Function

Catalyzes the conversion of a double bond to a cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence. Ref.3

Catalytic activity

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

Pathway

Lipid metabolism; mycolic acid biosynthesis.

Subunit structure

Homodimer. Ref.4

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the CFA/CMAS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287Cyclopropane mycolic acid synthase 1
PRO_0000089566

Regions

Region33 – 342S-adenosyl-L-methionine binding
Region68 – 769S-adenosyl-L-methionine binding
Region94 – 996S-adenosyl-L-methionine binding
Region123 – 1242S-adenosyl-L-methionine binding

Sites

Active site2691 Probable

Experimental info

Sequence conflict2501A → D in AAK47836. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0C5C2 [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

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]"The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2."
George K.M., Yuan Y., Sherman D.R., Barry C.E. III
J. Biol. Chem. 270:27292-27298(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A CYCLOPROPANE SYNTHASE, NOMENCLATURE.
Strain: ATCC 25618 / H37Rv.
[4]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 18-287 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND SUBSTRATE ANALOG, SUBUNIT.
Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000516 Genomic DNA. Translation: AAK47836.1.
AL123456 Genomic DNA. Translation: CCP46213.1.
PIRG70974.
RefSeqNP_217909.1. NC_000962.3.
NP_338022.1. NC_002755.2.
YP_006516876.1. NC_018143.1.

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[»]
ProteinModelPortalP0C5C2.
SMRP0C5C2. Positions 3-287.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv3392c.

Proteomic databases

PRIDEP0C5C2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47836; AAK47836; MT3499.
GeneID13316994.
887961.
926573.
KEGGmtc:MT3499.
mtu:Rv3392c.
PATRIC18129437. VBIMycTub22151_3814.

Organism-specific databases

TubercuListRv3392c.

Phylogenomic databases

eggNOGCOG2230.
HOGENOMHOG000245191.
KOK00574.
OMAQLANINI.
ProtClustDBCLSK790562.

Enzyme and pathway databases

UniPathwayUPA00915.

Family and domain databases

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

Other

EvolutionaryTraceP0C5C2.

Entry information

Entry nameCMAS1_MYCTU
AccessionPrimary (citable) accession number: P0C5C2
Secondary accession number(s): L0TCE3, Q11195
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 29, 2013
This is version 47 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents