FAA28_MYCBO
ID FAA28_MYCBO Reviewed; 580 AA.
AC Q02278; A0A1R3Y2T9; Q7TXL1; X2BM82;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 108.
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 {ECO:0000312|EMBL:SIU01587.1};
GN OrderedLocusNames=BQ2027_MB2966;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-375.
RC STRAIN=BCG;
RX PubMed=1527058; DOI=10.1016/s0021-9258(18)41788-7;
RA Mathur M., Kolattukudy P.E.;
RT "Molecular cloning and sequencing of the gene for mycocerosic acid
RT synthase, a novel fatty acid elongating multifunctional enzyme, from
RT Mycobacterium tuberculosis var. bovis Bacillus Calmette-Guerin.";
RL J. Biol. Chem. 267:19388-19395(1992).
RN [4]
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=BCG;
RX PubMed=9525903; DOI=10.1074/jbc.273.14.8033;
RA Fitzmaurice A.M., Kolattukudy P.E.;
RT "An acyl-CoA synthase (acoas) gene adjacent to the mycocerosic acid
RT synthase (mas) locus is necessary for mycocerosyl lipid synthesis in
RT Mycobacterium tuberculosis var. bovis BCG.";
RL J. Biol. Chem. 273:8033-8039(1998).
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:9525903}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant lacks the ability to produce
CC mycosides and mycocerosyl phthiocerol esters.
CC {ECO:0000269|PubMed:9525903}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25367.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; LT708304; SIU01587.1; -; Genomic_DNA.
DR EMBL; M95808; AAA25367.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_856611.1; NC_002945.3.
DR RefSeq; WP_010950803.1; NC_002945.4.
DR AlphaFoldDB; Q02278; -.
DR SMR; Q02278; -.
DR EnsemblBacteria; SIU01587; SIU01587; BQ2027_MB2966.
DR PATRIC; fig|233413.5.peg.3255; -.
DR OMA; MLATSSH; -.
DR BioCyc; MetaCyc:MON-19638; -.
DR BRENDA; 6.2.1.49; 3494.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001419; 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_0000193139"
FT REGION 421..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="I -> S (in Ref. 3; AAA25367)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="A -> R (in Ref. 3; AAA25367)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="R -> P (in Ref. 3; AAA25367)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="S -> R (in Ref. 3; AAA25367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 62695 MW; 9FB7A792CA51452E CRC64;
MIVRSLPAAL RACARLQPHD PAFTFMDYEQ DWDGVAITLT WSQLYRRTLN VARELSRCGS
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
