P0C5C2 (CMAS1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

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 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.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	S-adenosylmethionine metabolic process Inferred from direct assay Ref.4. Source: MTBBASE mycolic acid biosynthetic process Inferred from direct assay. Source: MTBBASE
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	cyclopropane-fatty-acyl-phospholipid synthase activity Inferred from direct assay Ref.3. Source: MTBBASE
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 1

PRO_0000089566

Regions

Region

33 – 34

2

S-adenosyl-L-methionine binding

Region

68 – 76

9

S-adenosyl-L-methionine binding

Region

94 – 99

6

S-adenosyl-L-methionine binding

Region

123 – 124

2

S-adenosyl-L-methionine binding

Sites

Active site

269

1

Probable

Experimental info

Sequence conflict

250

1

A → D in AAK47836. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

287

Helix Strand Turn

Details...

Helix

9 – 16

8

Helix

20 – 24

5

Helix

45 – 57

13

Beta strand

67 – 72

6

Helix

77 – 86

10

Beta strand

89 – 93

5

Helix

97 – 107

11

Beta strand

112 – 114

3

Beta strand

116 – 119

4

Helix

123 – 125

3

Beta strand

131 – 136

6

Helix

147 – 155

9

Beta strand

163 – 171

9

Turn

174 – 176

3

Beta strand

179 – 182

4

Helix

186 – 198

13

Helix

208 – 215

8

Turn

216 – 219

4

Beta strand

221 – 227

7

Helix

229 – 245

17

Helix

247 – 253

7

Helix

256 – 274

19

Beta strand

277 – 286

10

Sequences

	Sequence		Length	Mass (Da)
	P0C5C2 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 7E254C15DF5FFF97	FASTA	287	32,461
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9634230] [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. , 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: 12218036] [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: 7592990] [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: 11756461] [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

BX842582 Genomic DNA. Translation: CAA15777.1.
AE000516 Genomic DNA. Translation: AAK47836.1.

PIR

G70974.

RefSeq

NP_217909.1. NC_000962.2.
NP_338022.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KP9	X-ray	2.21	A/B	1-287	[»]
1KPG	X-ray	2.00	A/B/C/D	1-287	[»]
1KPH	X-ray	2.00	A/B/C/D	1-287	[»]

ProteinModelPortal

P0C5C2.

SMR

P0C5C2. Positions 3-287.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000003412; EBMYCP00000003412; EBMYCG00000003410.
EBMYCT00000070708; EBMYCP00000068767; EBMYCG00000070703.

GeneID

887961.
926573.

GenomeReviews

Gene locus MT3499 in contig AE000516_GR.
Gene locus Rv3392c in contig AL123456_GR.

KEGG

mtc:MT3499.
mtu:Rv3392c.

PATRIC

18129437. VBIMycTub22151_3814.

TIGR

MT3499.

Organism-specific databases

TubercuList

Rv3392c.

Phylogenomic databases

GeneTree

EBGT00050000016600.

HOGENOM

HBG687502.

OMA

SCASAFR.

PhylomeDB

P0C5C2.

ProtClustDB

CLSK790562.

Family and domain databases

InterPro

IPR003333. Mycolic_cyclopropane_synthase.
[Graphical view]

KO

K00574.

Pfam

PF02353. CMAS. 1 hit.
[Graphical view]

PIRSF

PIRSF003085. CMAS. 1 hit.

ProtoNet

Search...

Entry information

Entry name

CMAS1_MYCTU

Accession

Primary (citable) accession number: P0C5C2
Secondary accession number(s): Q11195

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program