Q7D5D8 (FAC19_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Long-chain-fatty-acid--CoA ligase FadD19
Short name=FACL
EC=6.2.1.3

Alternative name(s):
Acyl-CoA synthetase

Gene names

Name:	fadD19
Ordered Locus Names:	Rv3515c, MT3616

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	548 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the activation of long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Ref.3
Catalytic activity	ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.
Pathway	Lipid metabolism; fatty acid biosynthesis.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to host immune response Inferred from expression pattern PubMed 12953091. Source: MTBBASE
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain fatty acid-CoA ligase 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 – 548	548	Long-chain-fatty-acid--CoA ligase FadD19		PRO_0000406790

Sequences

	Sequence		Length	Mass (Da)
	Q7D5D8 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: E574B4BFA86F324E	FASTA	548	59,741
	10 20 30 40 50 60 MAVALNIADL AEHAIDAVPD RVAVICGDEQ LTYAQLEDKA NRLAHHLIDQ GVQKDDKVGL 70 80 90 100 110 120 YCRNRIEIVI AMLGIVKAGA ILVNVNFRYV EGELRYLFDN SDMVALVHER RYADRVANVL 130 140 150 160 170 180 PDTPHVRTIL VVEDGSDQDY RRYGGVEFYS AIAAGSPERD FGERSADAIY LLYTGGTTGF 190 200 210 220 230 240 PKGVMWRHED IYRVLFGGTD FATGEFVKDE YDLAKAAAAN PPMIRYPIPP MIHGATQSAT 250 260 270 280 290 300 WMALFSGQTT VLAPEFNADE VWRTIHKHKV NLLFFTGDAM ARPLVDALVK GNDYDLSSLF 310 320 330 340 350 360 LLASTAALFS PSIKEKLLEL LPNRVITDSI GSSETGFGGT SVVAAGQAHG GGPRVRIDHR 370 380 390 400 410 420 TVVLDDDGNE VKPGSGMRGV IAKKGNIPVG YYKDEKKTAE TFRTINGVRY AIPGDYAQVE 430 440 450 460 470 480 EDGTVTMLGR GSVSINSGGE KVYPEEVEAA LKGHPDVFDA LVVGVPDPRY GQQVAAVVQA 490 500 510 520 530 540 RPGCRPSLAE LDSFVRSEIA GYKVPRSLWF VDEVKRSPAG KPDYRWAKEQ TEARPADDVH AGHVTSGG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria." Trivedi O.A., Arora P., Sridharan V., Tickoo R., Mohanty D., Gokhale R.S. Nature 428:441-445(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN ACYL-COA SYNTHETASE. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000516 Genomic DNA. Translation: AAK47976.1. AL123456 Genomic DNA. Translation: CCP46337.1.
PIR	E70807.
RefSeq	NP_338162.1. NC_002755.2. YP_006517003.1. NC_018143.1. YP_177983.1. NC_000962.3.
3D structure databases
ProteinModelPortal	Q7D5D8.
SMR	Q7D5D8. Positions 20-521.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv3515c.
Proteomic databases
PRIDE	Q7D5D8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK47976; AAK47976; MT3616.
GeneID	13317122. 888275. 922878.
KEGG	mtc:MT3616. mtu:Rv3515c.
PATRIC	18129711. VBIMycTub22151_3951.
Organism-specific databases
TubercuList	Rv3515c.
Phylogenomic databases
eggNOG	COG0318.
HOGENOM	HOG000230015.
KO	K00666.
OMA	TAETFKT.
ProtClustDB	PRK07798.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16894.
UniPathway	UPA00094.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL5182.

Entry information

Entry name

FAC19_MYCTU

Accession

Primary (citable) accession number: Q7D5D8
Secondary accession number(s): L0TEC7, Q6MWW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 5, 2011
Last sequence update:	July 5, 2004
Last modified:	May 29, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program