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Protein

Cyclopropane mycolic acid synthase 1

Gene

cmaA1

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

Functioni

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.1 Publication

Catalytic activityi

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

Pathwayi: mycolic acid biosynthesis

This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway mycolic acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei269 – 2691Curated

GO - Molecular functioni

  • cyclopropane-fatty-acyl-phospholipid synthase activity Source: MTBBASE

GO - Biological processi

  • mycolic acid biosynthetic process Source: MTBBASE
  • S-adenosylmethionine metabolic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00915.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclopropane mycolic acid synthase 1 (EC:2.1.1.79)
Short name:
CMAS
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 namesi
Name:cmaA1
Synonyms:cma1, CMAS-1
Ordered Locus Names:Rv3392c
ORF Names:MTV004.50
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3392c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287Cyclopropane mycolic acid synthase 1PRO_0000089566Add
BLAST

Proteomic databases

PaxDbiP9WPB7.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi83332.Rv3392c.

Structurei

Secondary structure

1
287
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 168Combined sources
Helixi20 – 234Combined sources
Turni24 – 263Combined sources
Helixi45 – 5713Combined sources
Turni58 – 614Combined sources
Beta strandi67 – 726Combined sources
Helixi77 – 8610Combined sources
Beta strandi89 – 957Combined sources
Helixi97 – 10812Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi116 – 1216Combined sources
Helixi123 – 1253Combined sources
Beta strandi131 – 1377Combined sources
Helixi139 – 1413Combined sources
Turni144 – 1463Combined sources
Helixi147 – 15711Combined sources
Beta strandi163 – 1719Combined sources
Helixi174 – 1774Combined sources
Turni178 – 1814Combined sources
Helixi185 – 19814Combined sources
Helixi208 – 2169Combined sources
Turni217 – 2193Combined sources
Beta strandi221 – 2277Combined sources
Helixi229 – 24517Combined sources
Helixi247 – 2537Combined sources
Helixi256 – 27419Combined sources
Beta strandi277 – 28610Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KP9X-ray2.21A/B1-287[»]
1KPGX-ray2.00A/B/C/D2-287[»]
1KPHX-ray2.00A/B/C/D1-287[»]
ProteinModelPortaliP9WPB7.
SMRiP9WPB7. Positions 3-287.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 342S-adenosyl-L-methionine binding
Regioni68 – 769S-adenosyl-L-methionine binding
Regioni94 – 996S-adenosyl-L-methionine binding
Regioni123 – 1242S-adenosyl-L-methionine binding

Sequence similaritiesi

Belongs to the CFA/CMAS family.Curated

Phylogenomic databases

eggNOGiENOG4108NUI. Bacteria.
COG2230. LUCA.
KOiK00574.
OMAiRYDAFFT.
PhylomeDBiP9WPB7.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR003333. Mycolic_cyclopropane_synthase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFiPIRSF003085. CMAS. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WPB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDELKPHFA NVQAHYDLSD DFFRLFLDPT QTYSCAYFER DDMTLQEAQI
60 70 80 90 100
AKIDLALGKL GLQPGMTLLD VGCGWGATMM RAVEKYDVNV VGLTLSKNQA
110 120 130 140 150
NHVQQLVANS ENLRSKRVLL AGWEQFDEPV DRIVSIGAFE HFGHERYDAF
160 170 180 190 200
FSLAHRLLPA DGVMLLHTIT GLHPKEIHER GLPMSFTFAR FLKFIVTEIF
210 220 230 240 250
PGGRLPSIPM VQECASANGF TVTRVQSLQP HYAKTLDLWS AALQANKGQA
260 270 280
IALQSEEVYE RYMKYLTGCA EMFRIGYIDV NQFTCQK
Length:287
Mass (Da):32,461
Last modified:April 16, 2014 - v1
Checksum:i7E254C15DF5FFF97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46213.1.
PIRiG70974.
RefSeqiNP_217909.1. NC_000962.3.
WP_003900041.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP46213; CCP46213; Rv3392c.
GeneIDi887961.
KEGGimtu:Rv3392c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46213.1.
PIRiG70974.
RefSeqiNP_217909.1. NC_000962.3.
WP_003900041.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KP9X-ray2.21A/B1-287[»]
1KPGX-ray2.00A/B/C/D2-287[»]
1KPHX-ray2.00A/B/C/D1-287[»]
ProteinModelPortaliP9WPB7.
SMRiP9WPB7. Positions 3-287.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv3392c.

Proteomic databases

PaxDbiP9WPB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46213; CCP46213; Rv3392c.
GeneIDi887961.
KEGGimtu:Rv3392c.

Organism-specific databases

TubercuListiRv3392c.

Phylogenomic databases

eggNOGiENOG4108NUI. Bacteria.
COG2230. LUCA.
KOiK00574.
OMAiRYDAFFT.
PhylomeDBiP9WPB7.

Enzyme and pathway databases

UniPathwayiUPA00915.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR003333. Mycolic_cyclopropane_synthase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFiPIRSF003085. CMAS. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCMAS1_MYCTU
AccessioniPrimary (citable) accession number: P9WPB7
Secondary accession number(s): L0TCE3, P0C5C2, Q11195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: September 7, 2016
This is version 17 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.