Q7U1J9 (MMAA2_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cyclopropane mycolic acid synthase MmaA2
Short name=CMAS
EC=2.1.1.79

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 names

Name:	cmaC
Synonyms:	mmaA2, mmas-2
Ordered Locus Names:	Mb0663c

Organism

Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]

Taxonomic identifier

233413 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis

Protein attributes

Sequence length	287 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 By similarity. Ref.1
Catalytic activity	S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.
Pathway	Lipid metabolism; mycolic acid biosynthesis.
Sequence similarities	Belongs to the CFA/CMAS family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	mycolic acid biosynthetic process Inferred from mutant phenotype Ref.1. Source: UniProtKB
Molecular_function	cyclopropane-fatty-acyl-phospholipid synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 287	287	Cyclopropane mycolic acid synthase MmaA2		PRO_0000398360
Regions
	Region	33 – 34	2	S-adenosyl-L-methionine binding By similarity
	Region	72 – 74	3	S-adenosyl-L-methionine binding By similarity
	Region	94 – 99	6	S-adenosyl-L-methionine binding By similarity
	Region	123 – 124	2	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	269	1	By similarity
	Binding site	136	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	208	1	I → S in AAC44874. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q7U1J9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 4894FF920B090129	FASTA	287	32,681
	10 20 30 40 50 60 MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI AKIDLALGKL 70 80 90 100 110 120 GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA AHVQKSFDEM DTPLDRRVLL 130 140 150 160 170 180 AGWEQFNEPV DRIVSIGAFE HFGHDRHADF FARAHKILPP DGVLLLHTIT GLTRQQMVDH 190 200 210 220 230 240 GLPLTLWLAR FLKFIATEIF PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA 250 260 270 280 EALQEHKSEA IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mycobacterium bovis BCG genes involved in the biosynthesis of cyclopropyl keto- and hydroxy-mycolic acids." Dubnau E., Laneelle M.-A., Soares S., Benichou A., Vaz T., Prome D., Prome J.-C., Daffe M., Quemard A. Mol. Microbiol. 23:313-322(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN OXYGEN-CONTAINING MYCOLATES BIOSYNTHESIS, NOMENCLATURE. Strain: BCG / Pasteur.
[2]	"The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G. Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U77466 Genomic DNA. Translation: AAC44874.1. BX248336 Genomic DNA. Translation: CAD93525.1.
RefSeq	NP_854321.1. NC_002945.3.
3D structure databases
HSSP	HSSP built from PDB template 1KPH based on UniProtKB Q11195.
ProteinModelPortal	Q7U1J9.
SMR	Q7U1J9. Positions 3-287.
ModBase	Search...
Protein-protein interaction databases
STRING	233413.Mb0663c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD93525; CAD93525; Mb0663c.
GeneID	1091773.
KEGG	mbo:Mb0663c.
PATRIC	18003118. VBIMycBov88188_0723.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG2230.
HOGENOM	HOG000245191.
KO	K00574.
OMA	PAKFSLI.
ProtClustDB	CLSK790562.
Enzyme and pathway databases
UniPathway	UPA00915.
Family and domain databases
InterPro	IPR003333. Mycolic_cyclopropane_synthase. [Graphical view]
Pfam	PF02353. CMAS. 1 hit. [Graphical view]
PIRSF	PIRSF003085. CMAS. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MMAA2_MYCBO

Accession

Primary (citable) accession number: Q7U1J9
Secondary accession number(s): P94923

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program