Rv3801c - fatty-acid-CoA ligase fadD32

Expression: Most Significant Conditions for Rv3801c

Protein Domains

Gene Information
Locus	Rv3801c
Symbol	fadD32
Gene Name	fatty-acid-CoA ligase fadD32
Location	4261153 - 4263066 (-)
Species	Mycobacterium tuberculosis H37Rv complete genome.
Length	Gene:1914 bp Protein:638 aa
External Links	Tuberculist Target Gene Information String Protein-Protein Interactions STITCH Chemical-Protein Interactions Search Google Scholar
Orthologs
Orthogroup Number	31110
Related Genes	CE2705 CE2706 cg3178 cg3179 DIP2189 DIP2190 jk0137 jk0138 MAP0219 MAP0220 MAV_0217 MAV_0218 Mkms_5098 Mkms_5099 ML0100 ML0101 Mmcs_5010 Mmcs_5011 MSMEG_6392 MSMEG_6393 MT3907 MT3908 MUL_4983 MUL_4984 Mvan_5640 Mvan_5641 nfa1880 nfa1890 Rv3800c
Transcriptional Regulation
Operons	View gene in operon browser
Regulatory Network	Search for regulators of Rv3801c
Expression Correlation	Genes with Correlated Expression Scatterplot of Gene Expression

Sequence

Proteins

>Rv3801c Transcript 1
MFVTGESGMAYHNPFIVNGKIRFPANTNLVRHVEKWAKVRGDKLAYRFLDFSTERDGVAR
DILWSDFSARNRAVGARLQQVTQPGDRVAILCPQNLDYLISFFGALYSGRIAVPLFDPAE
PGHVGRLHAVLDDCAPSTILTTTDSAEGVRKFIRARSAKERPRVIAVDAVPTEVAATWQQ
PEANEETVAYLQYTSGSTRIPSGVQITHLNLPTNVVQVLNALEGQEGDRGVSWLPFFHDM
GLITVLLASVLGHSFTFMTPAAFVRRPGRWIRELARKPGETGGTFSAAPNFAFEHAAVRG
VPRDDEPPLDLSNVKGILNGSEPVSPASMRKFFEAFAPYGLKQTAVKPSYGLAEATLFVS
TTPMDEVPTVIHVDRDELNNQRFVEVAADAPNAVAQVSAGKVGVSEWAVIVDADTASELP
DGQIGEIWLHGNNLGTGYWGKEEESAQTFKNILKSRISESRAEGAPDDALWVRTGDYGTY
FKDHLYIAGRIKDLVIIDGRNHYPQDLECTAQESTKALRVGYAAAFSVPANQLPQTVFDD
SHAGLKFDPEDTSEQLVIVGERAAGTHKLDHQPIVDDIRAAIAVGHGVTVRDVLLVSAGT
IPRTSSGKIGRRACRAAYLDGSLRSGVGSPTVFATSD*

Genomic Sequence

>Rv3801c
ATGTTTGTGACAGGAGAGAGTGGGATGGCGTACCACAACCCGTTCATCGTGAATGGAAAG
ATCAGGTTCCCAGCCAACACCAACCTGGTTCGTCACGTCGAAAAGTGGGCGAAGGTTCGT
GGCGACAAGCTGGCCTACCGGTTCCTGGACTTTTCCACCGAACGAGACGGTGTCGCGCGC
GACATCTTGTGGTCTGACTTCAGCGCGCGCAACCGTGCGGTGGGAGCCCGCCTGCAGCAA
GTCACCCAGCCGGGTGACCGCGTCGCCATCCTGTGCCCGCAGAACCTGGACTACCTCATC
TCCTTCTTCGGCGCCCTCTACTCCGGCCGCATTGCGGTGCCGTTGTTCGACCCGGCCGAG
CCGGGGCACGTCGGTCGGTTACACGCGGTGCTCGACGACTGTGCCCCGTCGACGATCCTG
ACCACCACCGACTCCGCCGAAGGGGTCCGCAAGTTCATCCGGGCCCGATCGGCCAAGGAG
CGCCCGCGCGTCATTGCCGTCGACGCGGTGCCCACCGAAGTCGCCGCCACCTGGCAGCAG
CCCGAGGCCAACGAGGAAACCGTCGCGTACTTGCAGTACACGTCGGGTTCCACCCGCATA
CCGAGCGGCGTGCAGATCACCCATCTGAACCTGCCCACCAATGTGGTGCAGGTGCTCAAT
GCCCTGGAAGGACAGGAAGGCGACCGCGGGGTCAGCTGGCTCCCGTTCTTCCACGACATG
GGTCTGATCACGGTGCTGCTGGCGTCGGTGCTAGGCCACAGCTTCACCTTTATGACGCCC
GCGGCGTTCGTGCGGCGGCCCGGTCGCTGGATCCGCGAGCTCGCCCGCAAGCCCGGAGAA
ACCGGTGGCACCTTCTCTGCGGCGCCGAACTTCGCATTCGAACACGCCGCGGTGCGCGGT
GTGCCTCGAGACGACGAGCCGCCGCTGGACCTGAGCAACGTCAAGGGCATCCTCAACGGC
AGCGAGCCGGTGTCGCCGGCGTCGATGCGCAAGTTCTTCGAAGCATTTGCGCCGTACGGT
TTGAAGCAGACCGCCGTCAAGCCGTCCTATGGGCTAGCGGAGGCCACGCTGTTCGTCTCG
ACCACGCCGATGGACGAGGTGCCCACCGTGATCCACGTGGACCGCGACGAGCTGAACAAC
CAGCGGTTCGTTGAGGTGGCCGCCGATGCACCCAACGCCGTCGCCCAGGTCTCTGCGGGC
AAGGTCGGGGTCAGCGAATGGGCGGTCATCGTCGACGCCGACACGGCCAGCGAACTGCCG
GACGGACAGATCGGTGAGATCTGGCTGCACGGCAACAACTTGGGTACCGGTTATTGGGGC
AAAGAAGAAGAGTCCGCCCAGACCTTCAAGAACATCCTCAAATCGCGGATCAGCGAGTCG
CGCGCCGAGGGCGCCCCAGACGACGCGCTGTGGGTGCGTACCGGCGACTACGGCACCTAC
TTCAAGGACCACCTCTACATAGCCGGCCGGATCAAGGACCTCGTCATCATCGACGGCCGC
AATCACTACCCACAGGATCTCGAGTGCACGGCGCAGGAGTCGACCAAGGCGTTGCGGGTT
GGCTACGCGGCGGCCTTCTCGGTTCCGGCCAACCAGCTTCCTCAGACAGTGTTCGACGAC
TCGCACGCCGGGCTGAAATTCGACCCCGAGGACACCTCCGAGCAGCTGGTGATCGTCGGC
GAACGGGCGGCCGGCACGCATAAGCTCGACCACCAGCCCATCGTCGATGACATCCGGGCG
GCCATCGCCGTCGGGCATGGGGTGACCGTGCGTGACGTCCTGCTGGTGTCGGCCGGCACG
ATTCCGCGAACCTCCAGCGGCAAGATCGGCCGCCGCGCCTGCCGTGCGGCCTACCTCGAC
GGCAGCCTGCGCAGTGGCGTGGGTTCCCCGACGGTCTTCGCCACTTCGGACTGA

Community Annotations Pending Curatorial Review

Field	Value	Status	Creator	Date
Interaction	PhysicalInteraction Rv3280	active	sourish10	2012-10-05
	Affinity purification (Physical interaction) SK. Parker, RM. Barkley et al. Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase and is inhibited by the antimycobacterial agent tetrahydrolipstatin. PLoS ONE 2009
Interaction	PhysicalInteraction Rv3285	active	sourish10	2012-10-05
	Affinity purification (Physical interaction) SK. Parker, RM. Barkley et al. Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase and is inhibited by the antimycobacterial agent tetrahydrolipstatin. PLoS ONE 2009
Interaction	PhysicalInteraction Rv3799c	active	sourish10	2012-10-05
	Affinity purification (Physical interaction) SK. Parker, RM. Barkley et al. Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase and is inhibited by the antimycobacterial agent tetrahydrolipstatin. PLoS ONE 2009
Interaction	PhysicalInteraction Rv3800c	active	sourish10	2012-10-05
	Affinity purification (Physical interaction) SK. Parker, RM. Barkley et al. Mycobacterium tuberculosis Rv3802c encodes a phospholipase/thioesterase and is inhibited by the antimycobacterial agent tetrahydrolipstatin. PLoS ONE 2009
Name	Fatty acyl-AMP ligase	active	mjackson	2012-10-05
	Claisen-type condensation
Name	Fatty acyl-AMP ligase	active	mjackson	2012-10-05
	Claisen-type condensation
Term	EC:2.3.1.86 Fatty-acyl-CoA synthase. - NR	active	extern:JZUCKER	2012-03-06
	Assay of protein purified to homogeneity OA. Trivedi,P. Arora,V. Sridharan,R. Tickoo,D. Mohanty,RS. Gokhale Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 2004
Term	EC:6.2.1.3 Long-chain-fatty-acid--CoA ligase. - NR	active	jjmcfadden	2012-03-05
	Inferred from direct assay D. Portevin, C. de Sousa-D'Auria et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J. Biol. Chem. 2005
Term	EC:6.2.1.- Ligases. Forming carbon-sulfur bonds. Acid--thiol ligases. - NR	active	jjmcfadden	2012-03-05
	Inferred from direct assay D. Portevin, C. de Sousa-D'Auria et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J. Biol. Chem. 2005