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Protein

Cyclopropane mycolic acid synthase MmaA2

Gene

mmaA2

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 cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.2 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited by S-adenosyl-N-decyl-aminoethyl (SADAE) and thiacetazone (TAC).2 Publications

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)DescriptionActionsGraphical viewLength
Binding sitei136S-adenosyl-L-methionine; via carbonyl oxygen1
Active sitei269By similarity1

GO - Molecular functioni

  • cyclopropane-fatty-acyl-phospholipid synthase activity Source: UniProtKB
  • methyltransferase activity Source: UniProtKB

GO - Biological processi

  • mycolic acid biosynthetic 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

BioCyciMetaCyc:G185E-4787-MONOMER.
MTBH37RV:G185E-4787-MONOMER.
UniPathwayiUPA00915.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclopropane mycolic acid synthase MmaA2 (EC:2.1.1.79)
Short name:
CMAS
Alternative name(s):
Cyclopropane-fatty-acyl-phospholipid synthase
Short name:
CFA synthase
Mycolic acid methyltransferase
Short name:
MA-MT
S-adenosylmethionine-dependent methyltransferase
Short name:
AdoMet-MT
Short name:
SAM-MT
Gene namesi
Name:mmaA2
Synonyms:mma2
Ordered Locus Names:Rv0644c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0644c.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Disruption phenotypei

Disruption of this gene suppresses a cyclopropane group at the distal position of alpha mycolic acid and cause a mild impairment in methoxymycolate, but not in ketomycolate. A 2-fold reduction in the relative abundance of cis-cyclopropanated methoxymycolate is observed. Cells lacking both cmA2 and mmaA2 genes cannot cis cyclopropanate methoxymycolates or ketomycolates.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00003983592 – 287Cyclopropane mycolic acid synthase MmaA2Add BLAST286

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylvalineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ79FX6.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv0644c.

Structurei

Secondary structure

1287
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 16Combined sources8
Helixi20 – 24Combined sources5
Helixi45 – 57Combined sources13
Turni58 – 61Combined sources4
Beta strandi67 – 72Combined sources6
Helixi77 – 86Combined sources10
Beta strandi89 – 95Combined sources7
Helixi97 – 108Combined sources12
Beta strandi116 – 121Combined sources6
Helixi123 – 125Combined sources3
Beta strandi131 – 137Combined sources7
Helixi139 – 142Combined sources4
Helixi144 – 146Combined sources3
Helixi147 – 157Combined sources11
Beta strandi163 – 171Combined sources9
Helixi174 – 179Combined sources6
Helixi186 – 198Combined sources13
Helixi208 – 218Combined sources11
Beta strandi221 – 227Combined sources7
Helixi229 – 245Combined sources17
Helixi247 – 253Combined sources7
Helixi256 – 275Combined sources20
Beta strandi277 – 286Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TPYX-ray2.20A1-287[»]
ProteinModelPortaliQ79FX6.
SMRiQ79FX6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ79FX6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni33 – 34S-adenosyl-L-methionine binding2
Regioni72 – 74S-adenosyl-L-methionine binding3
Regioni94 – 99S-adenosyl-L-methionine binding6
Regioni123 – 124S-adenosyl-L-methionine binding2

Sequence similaritiesi

Belongs to the CFA/CMAS family.Curated

Phylogenomic databases

eggNOGiENOG4108NUI. Bacteria.
COG2230. LUCA.
HOGENOMiHOG000245191.
InParanoidiQ79FX6.
KOiK00574.
OMAiSESYFVM.
PhylomeDBiQ79FX6.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q79FX6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI
60 70 80 90 100
AKIDLALGKL GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA
110 120 130 140 150
AHVQKSFDEM DTPRDRRVLL AGWEQFNEPV DRIVSIGAFE HFGHDRHADF
160 170 180 190 200
FARAHKILPP DGVLLLHTIT GLTRQQMVDH GLPLTLWLAR FLKFIATEIF
210 220 230 240 250
PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA EALQEHKSEA
260 270 280
IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK
Length:287
Mass (Da):32,724
Last modified:July 5, 2004 - v1
Checksum:i669C3224C6B178C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43387.1.
RefSeqiNP_215158.1. NC_000962.3.
WP_003900985.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43387; CCP43387; Rv0644c.
GeneIDi888061.
KEGGimtu:Rv0644c.
PATRICi18149942. VBIMycTub87468_0719.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43387.1.
RefSeqiNP_215158.1. NC_000962.3.
WP_003900985.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TPYX-ray2.20A1-287[»]
ProteinModelPortaliQ79FX6.
SMRiQ79FX6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0644c.

Proteomic databases

PaxDbiQ79FX6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43387; CCP43387; Rv0644c.
GeneIDi888061.
KEGGimtu:Rv0644c.
PATRICi18149942. VBIMycTub87468_0719.

Organism-specific databases

TubercuListiRv0644c.

Phylogenomic databases

eggNOGiENOG4108NUI. Bacteria.
COG2230. LUCA.
HOGENOMiHOG000245191.
InParanoidiQ79FX6.
KOiK00574.
OMAiSESYFVM.
PhylomeDBiQ79FX6.

Enzyme and pathway databases

UniPathwayiUPA00915.
BioCyciMetaCyc:G185E-4787-MONOMER.
MTBH37RV:G185E-4787-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ79FX6.

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 nameiMMAA2_MYCTU
AccessioniPrimary (citable) accession number: Q79FX6
Secondary accession number(s): L0T7B6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 5, 2004
Last modified: November 2, 2016
This is version 90 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.