P63405 (ACCD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
Short name=ACCase beta chain
EC=6.4.1.2

Gene names

Name:	accD3
Ordered Locus Names:	Rv0904c, MT0927
ORF Names:	MTCY31.32c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA By similarity.
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
Disruption phenotype	Not essential for growth. Ref.3
Miscellaneous	Was identified as a high-confidence drug target.
Sequence similarities	Belongs to the AccD/PCCB family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mycolic acid biosynthetic process Inferred from mutant phenotype PubMed 15308633. Source: MTBBASE
Cellular_component	acetyl-CoA carboxylase complex Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase 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 – 495	495	Putative acetyl-coenzyme A carboxylase carboxyl transferase subunit beta		PRO_0000199773

Sequences

	Sequence		Length	Mass (Da)
	P63405 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 156C96E927FF950C	FASTA	495	51,772
	10 20 30 40 50 60 MSRITTDQLR HAVLDRGSFV SWDSEPLAVP VADSYARELA AARAATGADE SVQTGEGRVF 70 80 90 100 110 120 GRRVAVVACE FDFLGGSIGV AAAERITAAV ERATAERLPL LASPSSGGTR MQEGTVAFLQ 130 140 150 160 170 180 MVKIAAAIQL HNQARLPYLV YLRHPTTGGV FASWGSLGHL TVAEPGALIG FLGPRVYELL 190 200 210 220 230 240 YGDPFPSGVQ TAENLRRHGI IDGVVALDRL RPMLDRALTV LIDAPEPLPA PQTPAPVPDV 250 260 270 280 290 300 PTWDSVVASR RPDRPGVRQL LRHGATDRVL LSGTDQGEAA TTLLALARFG GQPTVVLGQQ 310 320 330 340 350 360 RAVGGGGSTV GPAALREARR GMALAAELCL PLVLVIDAAG PALSAAAEQG GLAGQIAHCL 370 380 390 400 410 420 AELVTLDTPT VSILLGQGSG GPALAMLPAD RVLAALHGWL APLPPEGASA IVFRDTAHAA 430 440 450 460 470 480 ELAAAQGIRS ADLLKSGIVD TIVPEYPDAA DEPIEFALRL SNAIAAEVHA LRKIPAPERL 490 ATRLQRYRRI GLPRD

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Genes required for mycobacterial growth defined by high density mutagenesis." Sassetti C.M., Boyd D.H., Rubin E.J. Mol. Microbiol. 48:77-84(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[4]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842574 Genomic DNA. Translation: CAA97379.1. AE000516 Genomic DNA. Translation: AAK45174.1. AL123456 Genomic DNA. Translation: CCP43652.1.
PIR	E70783.
RefSeq	NP_215419.1. NC_000962.3. NP_335360.1. NC_002755.2. YP_006514257.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P63405.
SMR	P63405. Positions 3-491.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv0904c.
Proteomic databases
PRIDE	P63405.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK45174; AAK45174; MT0927.
GeneID	13318808. 885279. 926242.
KEGG	mtc:MT0927. mtu:Rv0904c. mtv:RVBD_0904c.
PATRIC	18123786. VBIMycTub22151_1017.
Organism-specific databases
TubercuList	Rv0904c.
Phylogenomic databases
eggNOG	COG0777.
HOGENOM	HOG000244564.
KO	K01962. K01963.
OMA	GASAIVH.
ProtClustDB	CLSK790823.
Family and domain databases
InterPro	IPR000438. Acetyl_CoA_COase_Trfase_b_su. IPR000022. Carboxyl_trans. IPR011763. COA_CT_C. IPR011762. COA_CT_N. [Graphical view]
Pfam	PF01039. Carboxyl_trans. 1 hit. [Graphical view]
PRINTS	PR01070. ACCCTRFRASEB.
PROSITE	PS50989. COA_CT_CTER. 1 hit. PS50980. COA_CT_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACCD_MYCTU

Accession

Primary (citable) accession number: P63405
Secondary accession number(s): L0T824, Q10561

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program