FAA28_MYCMM
ID FAA28_MYCMM Reviewed; 580 AA.
AC B2HIM0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Long-chain-fatty-acid--AMP ligase FadD28 {ECO:0000305};
DE EC=6.2.1.49 {ECO:0000250|UniProtKB:P9WQ59};
DE AltName: Full=Acyl-AMP synthetase;
DE AltName: Full=Long-chain fatty acid adenylyltransferase FadD28 {ECO:0000305};
GN Name=fadD28; OrderedLocusNames=MMAR_1765;
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 PATHWAY, AND DISRUPTION PHENOTYPE.
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: Involved in the biosynthesis of phthiocerol dimycocerosate
CC (PDIM), a cell wall-associated lipid found only in pathogenic
CC mycobacteria. Catalyzes the activation of long-chain fatty acids as
CC acyl-adenylates (acyl-AMP), which are then transferred to the
CC multifunctional polyketide synthase Mas for further chain extension.
CC {ECO:0000250|UniProtKB:P9WQ59}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-[mycocerosate synthase] =
CC AMP + diphosphate + long-chain fatty acyl-[mycocerosate synthase];
CC Xref=Rhea:RHEA:10696, Rhea:RHEA-COMP:12641, Rhea:RHEA-COMP:13239,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:133243, ChEBI:CHEBI:456215;
CC EC=6.2.1.49; Evidence={ECO:0000250|UniProtKB:P9WQ59};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10697;
CC Evidence={ECO:0000250|UniProtKB:P9WQ59};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + H(+) = a long-chain fatty
CC acyl-AMP + diphosphate; Xref=Rhea:RHEA:52336, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:136562; Evidence={ECO:0000250|UniProtKB:P9WQ59};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52337;
CC Evidence={ECO:0000250|UniProtKB:P9WQ59};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-AMP + holo-[mycocerosate synthase] =
CC AMP + H(+) + long-chain fatty acyl-[mycocerosate synthase];
CC Xref=Rhea:RHEA:52340, Rhea:RHEA-COMP:12641, Rhea:RHEA-COMP:13239,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:133243,
CC ChEBI:CHEBI:136562, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:P9WQ59};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52341;
CC Evidence={ECO:0000250|UniProtKB:P9WQ59};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:25561717}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to defects in phenolic
CC glycolipids (PGL) and phthiocerol dimycocerosates (PDIM) production.
CC {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; ACC40214.1; -; Genomic_DNA.
DR RefSeq; WP_012393572.1; NC_010612.1.
DR AlphaFoldDB; B2HIM0; -.
DR SMR; B2HIM0; -.
DR STRING; 216594.MMAR_1765; -.
DR EnsemblBacteria; ACC40214; ACC40214; MMAR_1765.
DR KEGG; mmi:MMAR_1765; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_23_7_11; -.
DR OMA; MLATSSH; -.
DR OrthoDB; 572620at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001190; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..580
FT /note="Long-chain-fatty-acid--AMP ligase FadD28"
FT /id="PRO_0000406356"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 62274 MW; 777F0BA82DF5BFB3 CRC64;
MSVRSLPAAL RACARLQPND PAFTFMNYEQ NWDGAAETLT WSQLYRRTLN VARELSSCGS
VGDRAVILAP QGLEYVVAFL GALQAGRIAV PLSVPQGGAS DERATSVLRD ASPVAILTTS
PVIDDVTQHV SAQSAGPAPS IIELDRLDLD AAAGSGAGTE NYPATAYLQY TSGSTREPAG
VMLSHQNLVT NFEQLMSGYF ADTDGIAPPD STLVSWLPFY HDMGLVLGVC APILGGYQAV
LTSPVSFLQR PARWLQMLAT SSHAFSAAPN FAFELAAKKV SDDDMAGLDL GNVLTILSGS
ERVQPATLKR FADRFARFNL QEKVLRPSYG LAEATVYVST SRPGQPPELV EFDAESLSTG
QAKQCESGAG TQLVSYVLPR SPIVRVVDPD TCTECPDGTV GEIWVCGDNV AIGYWNKPEE
SERTFGGKLA SPSEGTPEGP WLRTGDSGFI TDGKMFIIGR IKDLLIVYGR NHSPDDIEAT
IQEITRSRCA AISVPGDRST EKLVAIIEYR RRGDSDQEAM DMLVAVKREV TSALSNSHGL
SVADLVLVAP GSIPTTTSGK VRRAACVEQY RQQQFARLDV
