FAA28_MYCTO
ID FAA28_MYCTO Reviewed; 580 AA.
AC P9WQ58; L0TCP5; P96290; Q7D6E4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 35.
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; Synonyms=acoas; OrderedLocusNames=MT3011;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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:0000250|UniProtKB:P9WQ59}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK47338.1; -; Genomic_DNA.
DR PIR; B70668; B70668.
DR RefSeq; WP_003414857.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQ58; -.
DR SMR; P9WQ58; -.
DR EnsemblBacteria; AAK47338; AAK47338; MT3011.
DR KEGG; mtc:MT3011; -.
DR PATRIC; fig|83331.31.peg.3252; -.
DR HOGENOM; CLU_000022_23_7_11; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..580
FT /note="Long-chain-fatty-acid--AMP ligase FadD28"
FT /id="PRO_0000426833"
FT REGION 421..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 227
FT /note="Important for substrate selectivity"
FT /evidence="ECO:0000250"
FT SITE 330
FT /note="Important for substrate selectivity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 580 AA; 62641 MW; 60842A083746AFD3 CRC64;
MSVRSLPAAL RACARLQPHD PAFTFMDYEQ DWDGVAITLT WSQLYRRTLN VAQELSRCGS
TGDRVVISAP QGLEYVVAFL GALQAGRIAV PLSVPQGGVT DERSDSVLSD SSPVAILTTS
SAVDDVVQHV ARRPGESPPS IIEVDLLDLD APNGYTFKED EYPSTAYLQY TSGSTRTPAG
VVMSHQNVRV NFEQLMSGYF ADTDGIPPPN SALVSWLPFY HDMGLVIGIC APILGGYPAV
LTSPVSFLQR PARWMHLMAS DFHAFSAAPN FAFELAARRT TDDDMAGRDL GNILTILSGS
ERVQAATIKR FADRFARFNL QERVIRPSYG LAEATVYVAT SKPGQPPETV DFDTESLSAG
HAKPCAGGGA TSLISYMLPR SPIVRIVDSD TCIECPDGTV GEIWVHGDNV ANGYWQKPDE
SERTFGGKIV TPSPGTPEGP WLRTGDSGFV TDGKMFIIGR IKDLLIVYGR NHSPDDIEAT
IQEITRGRCA AISVPGDRST EKLVAIIELK KRGDSDQDAM ARLGAIKREV TSALSSSHGL
SVADLVLVAP GSIPITTSGK VRRGACVEQY RQDQFARLDA
