FAA26_MYCMM
ID FAA26_MYCMM Reviewed; 584 AA.
AC B2HIN2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Long-chain-fatty-acid--AMP ligase FadD26;
DE Short=FAAL;
DE EC=6.2.1.59 {ECO:0000269|PubMed:25561717};
DE AltName: Full=Acyl-AMP synthetase;
GN Name=fadD26 {ECO:0000303|PubMed:25561717}; OrderedLocusNames=MMAR_1777;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=25561717; DOI=10.1128/jb.02546-14;
RA Vergnolle O., Chavadi S.S., Edupuganti U.R., Mohandas P., Chan C., Zeng J.,
RA Kopylov M., Angelo N.G., Warren J.D., Soll C.E., Quadri L.E.;
RT "Biosynthesis of cell envelope-associated phenolic glycolipids in
RT Mycobacterium marinum.";
RL J. Bacteriol. 197:1040-1050(2015).
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 (PubMed:25561717). Catalyzes the adenylation of the long-chain fatty
CC acids eicosanoate (C20) or docosanoate (C22), and potentially the very-
CC long-chain fatty acid lignocerate (C24) (By similarity). Involved in
CC the biosynthesis of phthiocerol dimycocerosate (DIM A) and
CC phthiodiolone dimycocerosate (DIM B) (PubMed:25561717) (By similarity).
CC {ECO:0000250|UniProtKB:P9WQ43, ECO:0000269|PubMed:25561717}.
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:0000269|PubMed:25561717};
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:25561717}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene produces selective loss of
CC phthiocerol dimycocerosates (PDIMs). {ECO:0000269|PubMed:25561717}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000854; ACC40226.1; -; Genomic_DNA.
DR RefSeq; WP_012393584.1; NC_010612.1.
DR AlphaFoldDB; B2HIN2; -.
DR SMR; B2HIN2; -.
DR STRING; 216594.MMAR_1777; -.
DR EnsemblBacteria; ACC40226; ACC40226; MMAR_1777.
DR GeneID; 64260474; -.
DR KEGG; mmi:MMAR_1777; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_23_7_11; -.
DR OMA; AMRCESE; -.
DR OrthoDB; 572620at2; -.
DR BRENDA; 6.2.1.59; 3506.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; ISS: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; Reference proteome.
FT CHAIN 1..584
FT /note="Long-chain-fatty-acid--AMP ligase FadD26"
FT /id="PRO_0000406354"
SQ SEQUENCE 584 AA; 62953 MW; 17194D4B2CD80EE9 CRC64;
MPVTDRSIPS LLKEQADQRP NETAFTFLDY DLDPNGFAET LTWSQVYARA CVVADELTMY
GVPGDRVAIL APQGLEYIVA FLGALQAGFI GVPLSTPQYG VHDERVSAVL RDSQPVAILT
TSAVVGDVTK YASSQDGQPA PSVIEVDLLD LDTPRPQQAL PQPASGSAYL QYTSGSTRTP
AGVIVSHENV IANVTQSLYG YFGGPDKFPA DTTVVSWLPL FHDMGLILGI CAPLVTGCTA
VLLSPMSFLR RPARWMQLLA SHPKCFSAAP NFAFELAVRR TTDEDLAGLD LGDVLGIVSG
SERIHVATIK RFTERFAPFN LSPAAVRPSY GLAEATLYVA APEPGTTPRT VRFDYESLTA
GHARPCRADG SVGTELISYG SPDPSAVRIV NPETMIENPS GTVGEIWAHG EHVAMGYWQK
PEQSDRTFNA RIVNPAPGTP EGPWLRTGDL GVMSNGELFI MGRIKDLVIV DGRNHYPDDI
EATIQEITGG RVAAIAVPDN ITEQLVAIIE LKRRGASAEE AMVKLRSVKR EITSAISKSH
SLRVADVVLV PPGSIPITTS GKIRRAACVE RYRSDGFNRL DVTV
