O06543 (O06543_MYCTU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
PROBABLE ALPHA-METHYLACYL-CoA RACEMASE MCR (2-methylacyl-CoA racemase) (2-arylpropionyl-CoA epimerase ) EMBL CAB09031.1
EC=5.1.99.4 EMBL CAB09031.1

Gene names

Name:	mcr EMBL CAB09031.1
Ordered Locus Names:	Rv1143

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Isomerase EMBL CAB09031.1
Technical term	3D-structure PDB 1X74 PDB 2GCE PDB 2GD2 PDB 2GD0 PDB 2GD6 PDB 2GCI Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acyl-CoA metabolic process Inferred from direct assay Ref.2. Source: MTBBASE
Molecular function	alpha-methylacyl-CoA racemase activity Inferred from direct assay Ref.2. Source: MTBBASE protein homodimerization activity Inferred from physical interaction Ref.2. Source: MTBBASE
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	O06543 [UniParc]. Last modified July 5, 2004. Version 3. Checksum: 52633107358AC843	FASTA	360	38,685
	10 20 30 40 50 60 MAGPLSGLRV VELAGIGPGP HAAMILGDLG ADVVRIDRPS SVDGISRDAM LRNRRIVTAD 70 80 90 100 110 120 LKSDQGLELA LKLIAKADVL IEGYRPGVTE RLGLGPEECA KVNDRLIYAR MTGWGQTGPR 130 140 150 160 170 180 SQQAGHDINY ISLNGILHAI GRGDERPVPP LNLVGDFGGG SMFLLVGILA ALWERQSSGK 190 200 210 220 230 240 GQVVDAAMVD GSSVLIQMMW AMRATGMWTD TRGANMLDGG APYYDTYECA DGRYVAVGAI 250 260 270 280 290 300 EPQFYAAMLA GLGLDAAELP PQNDRARWPE LRALLTEAFA SHDRDHWGAV FANSDACVTP 310 320 330 340 350 360 VLAFGEVHNE PHIIERNTFY EANGGWQPMP APRFSRTASS QPRPPAATID IEAVLTDWDG

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]	"Alpha-methylacyl-CoA racemase from Mycobacterium tuberculosis. Mutational and structural characterization of the active site and the fold." Savolainen K., Bhaumik P., Schmitz W., Kotti T.J., Conzelmann E., Wierenga R.K., Hiltunen J.K. J. Biol. Chem. 280:12611-12620(2005) [PubMed: 15632186] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS).
[3]	"The catalysis of the 1,1-proton transfer by alpha-methyl-acyl-CoA racemase is coupled to a movement of the fatty acyl moiety over a hydrophobic, methionine-rich surface." Bhaumik P., Schmitz W., Hassinen A., Hiltunen J.K., Conzelmann E., Wierenga R.K. J. Mol. Biol. 367:1145-1161(2007) [PubMed: 17320106] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842575 Genomic DNA. Translation: CAB09031.1.

PIR

H70553.

RefSeq

NP_215659.1. NC_000962.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X74	X-ray	1.79	A/B/C/D	1-360	[»]
2GCE	X-ray	1.85	A/B/C/D	1-360	[»]
2GCI	X-ray	1.60	A/B/C/D	1-360	[»]
2GD0	X-ray	1.70	A/B/C/D	1-360	[»]
2GD2	X-ray	1.70	A/B/C/D	1-360	[»]
2GD6	X-ray	2.30	A/B/C/D	1-360	[»]

ProteinModelPortal

O06543.

SMR

O06543. Positions 2-360.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000002298; EBMYCP00000002298; EBMYCG00000002296.

GeneID

885067.

GenomeReviews

Gene locus Rv1143 in contig AL123456_GR.

KEGG

mtu:Rv1143.

PATRIC

18151086. VBIMycTub87468_1281.

Organism-specific databases

TubercuList

Rv1143.

Phylogenomic databases

GeneTree

EBGT00050000014649.

HOGENOM

HBG659028.

OMA

TGFGQQG.

PhylomeDB

O06543.

ProtClustDB

CLSK790974.

Family and domain databases

InterPro

IPR003673. CoA-Trfase_fam_III.
IPR023606. CoA-Trfase_III_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.10540. CoA-Trfase_fam_III. 1 hit.

KO

K01796.

PANTHER

PTHR11837. CAIB_BAIF. 1 hit.

Pfam

PF02515. CoA_transf_3. 1 hit.
[Graphical view]

SUPFAM

SSF89796. CoA-Trfase_fam_III. 1 hit.

ProtoNet

Search...

Entry information

Entry name

O06543_MYCTU

Accession

Primary (citable) accession number: O06543

Entry history

Integrated into UniProtKB/TrEMBL:	July 1, 1997
Last sequence update:	July 5, 2004
Last modified:	December 14, 2011
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)