UniProtKB - P9WQ42 (FAA26_MYCTO)
Protein
Long-chain-fatty-acid--AMP ligase FadD26
Gene
fadD26
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Status
Functioni
Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase PpsA for further chain extension. Catalyzes the adenylation of the long-chain fatty acids eicosanoate (C20) or docosanoate (C22), and potentially the very-long-chain fatty acid lignocerate (C24). Involved in the biosynthesis of phthiocerol dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B).By similarity
Catalytic activityi
- a long-chain fatty acid + ATP + holo-[(phenol)carboxyphthiodiolenone synthase] = a long-chain fatty acyl-[(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphateBy similarityEC:6.2.1.59By similarity
- ATP + eicosanoate + holo-[(phenol)carboxyphthiodiolenone synthase] = AMP + diphosphate + icosanoyl-[(phenol)carboxyphthiodiolenone synthase]By similarityEC:6.2.1.59By similarity
- ATP + docosanoate + holo-[(phenol)carboxyphthiodiolenone synthase] = AMP + diphosphate + docosanoyl-[(phenol)carboxyphthiodiolenone synthase]By similarityEC:6.2.1.59By similarity
: fatty acid biosynthesis Pathwayi
This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.By similarityView all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ligase activity Source: UniProtKB-KW
GO - Biological processi
- fatty acid biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Ligase |
Biological process | Fatty acid metabolism, Lipid metabolism |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Names & Taxonomyi
Protein namesi | Recommended name: Long-chain-fatty-acid--AMP ligase FadD26 (EC:6.2.1.59By similarity)Short name: FAAL Alternative name(s): Acyl-AMP synthetase |
Gene namesi | Name:fadD26 Ordered Locus Names:MT2999 |
Organismi | Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) |
Taxonomic identifieri | 83331 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000426841 | 1 – 583 | Long-chain-fatty-acid--AMP ligase FadD26Add BLAST | 583 |
Family & Domainsi
Sequence similaritiesi
Belongs to the ATP-dependent AMP-binding enzyme family.Curated
Phylogenomic databases
HOGENOMi | CLU_000022_23_7_11 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR000873, AMP-dep_Synth/Lig IPR042099, AMP-dep_Synthh-like_sf |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit |
i Sequence
Sequence statusi: Complete.
P9WQ42-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MPVTDRSVPS LLQERADQQP DSTAYTYIDY GSDPKGFADS LTWSQVYSRA
60 70 80 90 100
CIIAEELKLC GLPGDRVAVL APQGLEYVLA FLGALQAGFI AVPLSTPQYG
110 120 130 140 150
IHDDRVSAVL QDSKPVAILT TSSVVGDVTK YAASHDGQPA PVVVEVDLLD
160 170 180 190 200
LDSPRQMPAF SRQHTGAAYL QYTSGSTRTP AGVIVSHTNV IANVTQSMYG
210 220 230 240 250
YFGDPAKIPT GTVVSWLPLY HDMGLILGIC APLVARRRAM LMSPMSFLRR
260 270 280 290 300
PARWMQLLAT SGRCFSAAPN FAFELAVRRT SDQDMAGLDL RDVVGIVSGS
310 320 330 340 350
ERIHVATVRR FIERFAPYNL SPTAIRPSYG LAEATLYVAA PEAGAAPKTV
360 370 380 390 400
RFDYEQLTAG QARPCGTDGS VGTELISYGS PDPSSVRIVN PETMVENPPG
410 420 430 440 450
VVGEIWVHGD HVTMGYWQKP KQTAQVFDAK LVDPAPAAPE GPWLRTGDLG
460 470 480 490 500
VISDGELFIM GRIKDLLIVD GRNHYPDDIE ATIQEITGGR AAAIAVPDDI
510 520 530 540 550
TEQLVAIIEF KRRGSTAEEV MLKLRSVKRE VTSAISKSHS LRVADLVLVS
560 570 580
PGSIPITTSG KIRRSACVER YRSDGFKRLD VAV
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000516 Genomic DNA Translation: AAK47327.1 |
PIRi | B70749 |
RefSeqi | WP_003900597.1, NZ_KK341227.1 |
Genome annotation databases
EnsemblBacteriai | AAK47327; AAK47327; MT2999 |
GeneIDi | 23490829 |
KEGGi | mtc:MT2999 |
PATRICi | fig|83331.31.peg.3240 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000516 Genomic DNA Translation: AAK47327.1 |
PIRi | B70749 |
RefSeqi | WP_003900597.1, NZ_KK341227.1 |
3D structure databases
SMRi | P9WQ42 |
ModBasei | Search... |
Genome annotation databases
EnsemblBacteriai | AAK47327; AAK47327; MT2999 |
GeneIDi | 23490829 |
KEGGi | mtc:MT2999 |
PATRICi | fig|83331.31.peg.3240 |
Phylogenomic databases
HOGENOMi | CLU_000022_23_7_11 |
Enzyme and pathway databases
UniPathwayi | UPA00094 |
Family and domain databases
Gene3Di | 3.40.50.12780, 1 hit |
InterProi | View protein in InterPro IPR000873, AMP-dep_Synth/Lig IPR042099, AMP-dep_Synthh-like_sf |
Pfami | View protein in Pfam PF00501, AMP-binding, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | FAA26_MYCTO | |
Accessioni | P9WQ42Primary (citable) accession number: P9WQ42 Secondary accession number(s): L0TDT5, Q10976 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | December 2, 2020 | |
This is version 29 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Documents
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families