FAA26_MYCBO
ID FAA26_MYCBO Reviewed; 583 AA.
AC Q7TXM1; A0A1R3Y3F0; X2BLX3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Long-chain-fatty-acid--AMP ligase FadD26;
DE Short=FAAL;
DE EC=6.2.1.59 {ECO:0000250|UniProtKB:P9WQ43};
DE AltName: Full=Acyl-AMP synthetase;
GN Name=fadD26; OrderedLocusNames=BQ2027_MB2955;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
RN [3]
RP FUNCTION IN THE BIOSYNTHESIS OF PHTHIOCEROL, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20553505; DOI=10.1111/j.1742-4658.2010.07688.x;
RA Simeone R., Leger M., Constant P., Malaga W., Marrakchi H., Daffe M.,
RA Guilhot C., Chalut C.;
RT "Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis
RT of phthiocerol dimycocerosates and related compounds in Mycobacterium
RT tuberculosis.";
RL FEBS J. 277:2715-2725(2010).
CC -!- FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl-
CC adenylates (acyl-AMP), which are then transferred to the
CC multifunctional polyketide synthase PpsA for further chain extension.
CC Catalyzes the adenylation of the long-chain fatty acids eicosanoate
CC (C20) or docosanoate (C22), and potentially the very-long-chain fatty
CC acid lignocerate (C24). Involved in the biosynthesis of phthiocerol
CC dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B).
CC {ECO:0000269|PubMed:20553505}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-
CC [(phenol)carboxyphthiodiolenone synthase] = a long-chain fatty acyl-
CC [(phenol)carboxyphthiodiolenone synthase] + AMP + diphosphate;
CC Xref=Rhea:RHEA:64660, Rhea:RHEA-COMP:14271, Rhea:RHEA-COMP:16648,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215;
CC EC=6.2.1.59; Evidence={ECO:0000250|UniProtKB:P9WQ43};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + eicosanoate + holo-[(phenol)carboxyphthiodiolenone
CC synthase] = AMP + diphosphate + icosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase]; Xref=Rhea:RHEA:59156,
CC Rhea:RHEA-COMP:14271, Rhea:RHEA-COMP:14985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:87848, ChEBI:CHEBI:456215; EC=6.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:P9WQ43};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + docosanoate + holo-[(phenol)carboxyphthiodiolenone
CC synthase] = AMP + diphosphate + docosanoyl-
CC [(phenol)carboxyphthiodiolenone synthase]; Xref=Rhea:RHEA:59160,
CC Rhea:RHEA-COMP:14271, Rhea:RHEA-COMP:14987, ChEBI:CHEBI:23858,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:142238, ChEBI:CHEBI:456215; EC=6.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:P9WQ43};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:20553505}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes the production
CC of phthiocerol dimycocerosate (DIM A) and of phthiodiolone
CC dimycocerosate (DIM B). Mutant can still produce mycoside B.
CC {ECO:0000269|PubMed:20553505}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU01576.1; -; Genomic_DNA.
DR RefSeq; NP_856600.1; NC_002945.3.
DR RefSeq; WP_003904960.1; NC_002945.4.
DR AlphaFoldDB; Q7TXM1; -.
DR SMR; Q7TXM1; -.
DR EnsemblBacteria; SIU01576; SIU01576; BQ2027_MB2955.
DR PATRIC; fig|233413.5.peg.3243; -.
DR OMA; AMRCESE; -.
DR BioCyc; MetaCyc:MON-19625; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR CDD; cd05931; FAAL; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR Pfam; PF00501; AMP-binding; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Ligase; Lipid metabolism.
FT CHAIN 1..583
FT /note="Long-chain-fatty-acid--AMP ligase FadD26"
FT /id="PRO_0000406353"
SQ SEQUENCE 583 AA; 63012 MW; 9DCD9DF3F5A416CB CRC64;
MPVTDRSVPS LLQERADQQP DSTAYTYIDY GSDPKGFADS LTWSQVYSRA CIIAEELKLC
GLPGDRVAVL APQGLEYVLA FLGALQAGFI AVPLSTPQYG IHDDRVSAVL QDSKPVAILT
TSSVVGDVTK YAASHDGQPA PVVVEVDLLD LDSPRQMPAF SRQHTGAAYL QYTSGSTRTP
AGVIVSHTNV IANVTQSMYG YFGDPAKIPT GTVVSWLPLY HDMGLILGIC APLVARRRAV
LMSPMSFLRR PARWMQLLAT SGRCFSAAPN FAFELAVRRT SDQDMAGLDL RDVVGIVSGS
ERIHVATVRR FIERFAPYNL SPTAIRPSYG LAEATLYVAA PEAGAAPKTV RFDYEQLTAG
QARPCGTDGS VGTELISYGS PDPSSVRIVN PETMVENPPG VVGEIWVHGD HVTMGYWQKP
KQTAQVFDAK LVDPAPAAPE GPWLRTGDLG VISDGELFIM GRIKDLLIVD GRNHYPDDIE
ATIQEITGGR AAAIAVPDDI TEQLVAIIEF KRRGSTAEEV MLKLRSVKRE VTSAISKSHS
LRVADLVLVS PGSIPITTSG KIRRSACVER YRSDGFKRLD VAV
