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Protein

Cyclopropane mycolic acid synthase 2

Gene

cmaA2

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of trans cyclopropanated ketomycolate or methoxymycolate through the conversion of a double bond to a cyclopropane ring at the proximal position of an oxygenated mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. In the absence of MmaA2, CmaA2 has a non-specific cis-cyclopropanating activity and is able to catalyze the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence (By similarity).By similarity

Catalytic activityi

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

Pathway:imycolic 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 sitei290 – 2901By similarity

GO - Molecular functioni

GO - Biological processi

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 2 (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:cmaA2
Ordered Locus Names:ML2426
ORF Names:B2168_F3_130
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
ProteomesiUP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML2426.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Cyclopropane mycolic acid synthase 2PRO_0000089568Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi272631.ML2426.

Structurei

3D structure databases

ProteinModelPortaliQ49807.
SMRiQ49807. Positions 15-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 452S-adenosyl-L-methionine bindingBy similarity
Regioni79 – 879S-adenosyl-L-methionine bindingBy similarity
Regioni105 – 1106S-adenosyl-L-methionine bindingBy similarity
Regioni137 – 1382S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the CFA/CMAS family.Curated

Phylogenomic databases

eggNOGiCOG2230.
HOGENOMiHOG000245191.
KOiK00574.
OMAiCQFTMVK.
OrthoDBiEOG6BGNZP.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR003333. Mycolic_cyclopropane_synthase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10108:SF743. PTHR10108:SF743. 1 hit.
PfamiPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFiPIRSF003085. CMAS. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q49807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPSQSHPAK TPRKQLKPPI EAVQSHYDRS NEFFKLWLDP SMTYSCAYFE
60 70 80 90 100
RPDLTLEEAQ RAKRDLALSK LGLEPGMTLL DIGCGWGSTM LHAIEKYDVN
110 120 130 140 150
VIGLTLSANQ LAHNKLKFAE IDHTRTDRTK DVRLQGWEQF DEPVDRIISL
160 170 180 190 200
GAFEHFADGA GDAGFERYDS FFKMCYDVLP DDGRMLLHTI IVPDAKETKE
210 220 230 240 250
LGLTTPMSLL RFIKFILTEI FPGGRLPKIS QVDHYSSNAG FTVERYHRIG
260 270 280 290 300
SHYVPTLNAW AAALEAHKDE AIALQGRQIY DTYMHYLTGC SDLFRDRYTD

VCQFTLVK
Length:308
Mass (Da):35,132
Last modified:November 1, 1996 - v1
Checksum:i9068380ED6D324AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00018 Genomic DNA. Translation: AAA17222.1.
AL583925 Genomic DNA. Translation: CAC31942.1.
PIRiS72886.
RefSeqiNP_302570.1. NC_002677.1.
WP_010908890.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC31942; CAC31942; CAC31942.
GeneIDi908573.
KEGGimle:ML2426.
PATRICi18059499. VBIMycLep78757_4664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00018 Genomic DNA. Translation: AAA17222.1.
AL583925 Genomic DNA. Translation: CAC31942.1.
PIRiS72886.
RefSeqiNP_302570.1. NC_002677.1.
WP_010908890.1. NC_002677.1.

3D structure databases

ProteinModelPortaliQ49807.
SMRiQ49807. Positions 15-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML2426.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC31942; CAC31942; CAC31942.
GeneIDi908573.
KEGGimle:ML2426.
PATRICi18059499. VBIMycLep78757_4664.

Organism-specific databases

LepromaiML2426.

Phylogenomic databases

eggNOGiCOG2230.
HOGENOMiHOG000245191.
KOiK00574.
OMAiCQFTMVK.
OrthoDBiEOG6BGNZP.

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]
PANTHERiPTHR10108:SF743. PTHR10108:SF743. 1 hit.
PfamiPF02353. CMAS. 1 hit.
[Graphical view]
PIRSFiPIRSF003085. CMAS. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Smith D.R., Robison K.
    Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiCMAS2_MYCLE
AccessioniPrimary (citable) accession number: Q49807
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.