ID   FAA29_MYCMM             Reviewed;         622 AA.
AC   B2HIL4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=4-hydroxyphenylalkanoate adenylyltransferase;
DE            EC=6.2.1.51 {ECO:0000305|PubMed:25561717};
DE   AltName: Full=Acyl-AMP synthase;
DE   AltName: Full=Long-chain-fatty-acid--AMP ligase FadD29;
DE            Short=FAAL;
GN   Name=fadD29; OrderedLocusNames=MMAR_1759;
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, 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       Involved in the biosynthesis of phenolphthiocerol, which is an
CC       important intermediate in the biosynthesis of phenolic glycolipid
CC       (PGL), also called mycosid B. {ECO:0000269|PubMed:25561717}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17-(4-hydroxyphenyl)heptadecanoate + ATP + holo-
CC         [(phenol)carboxyphthiodiolenone synthase] = 17-(4-
CC         hydroxyphenyl)heptadecanoyl-[(phenol)carboxyphthiodiolenone synthase]
CC         + AMP + diphosphate; Xref=Rhea:RHEA:55720, Rhea:RHEA-COMP:14271,
CC         Rhea:RHEA-COMP:14272, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:91233, ChEBI:CHEBI:133300,
CC         ChEBI:CHEBI:456215; EC=6.2.1.51;
CC         Evidence={ECO:0000305|PubMed:25561717};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=19-(4-hydroxyphenyl)nonadecanoate + ATP + holo-
CC         [(phenol)carboxyphthiodiolenone synthase] = 19-(4-
CC         hydroxyphenyl)nonadecanoyl-[(phenol)carboxyphthiodiolenone synthase]
CC         + AMP + diphosphate; Xref=Rhea:RHEA:55728, Rhea:RHEA-COMP:14271,
CC         Rhea:RHEA-COMP:14273, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:91236, ChEBI:CHEBI:133301,
CC         ChEBI:CHEBI:456215; EC=6.2.1.51;
CC         Evidence={ECO:0000305|PubMed:25561717};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene leads to selective loss of
CC       phenolic glycolipids (PGL). {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; ACC40208.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2HIL4; -.
DR   SMR; B2HIL4; -.
DR   STRING; 216594.MMAR_1759; -.
DR   EnsemblBacteria; ACC40208; ACC40208; MMAR_1759.
DR   KEGG; mmi:MMAR_1759; -.
DR   eggNOG; COG0318; Bacteria.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   OMA; VMFEGEL; -.
DR   BRENDA; 6.2.1.51; 3506.
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:0071766; P:Actinobacterium-type cell wall biogenesis; ISS:UniProtKB.
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   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..622
FT                   /note="4-hydroxyphenylalkanoate adenylyltransferase"
FT                   /id="PRO_0000406359"
SQ   SEQUENCE   622 AA;  67674 MW;  76DB1FE9748F5DA0 CRC64;
     MIMDTNAVSF RARDEVTTQL APGTGGQAVP TSNGMMTRFA MSESSLTDLL HKAATQYPNR
     AAYKFIDYDV NPDGFTETLT WWQIYRRAKI VAEELRGYGA SGDRVAVLAP QGLEYIIAFL
     GVLEAGLIAV PLPVPQFGIH DERISAALQD STPSVILTTS PVIDEVTKYA PHARAGQGGT
     PIVVAVDLLD LDSARELDLT PPAHSSTAYL QYTSGSTRSP AGVVLSHKNV ITNCVQLMSD
     YLGETEKVPS TAVSWLPFYH DMGLMLGIIL PMINQDTAVL LNPMAFLQRP ARWMQLMGKF
     RGQISCAPNF GFELAVRRTS DEDMAGLDLG HVRGIGSGAE RVNPATLQRF IDRFAPFNLR
     DTAIRPSYGL AEATVFVATA EPGRPPRSVN FDYQSLSVGR VERCANEADD GAKLVSYGSS
     WTSEVRIVDP EARTECPAGT VGEIWVQGDN VAMGYWRNPQ LTERTFDAKL TDPSPGTSIG
     PWLRTGDLGV MFEGELFITG RIKDLLIVDG SNHYPDDIES TIQEITGGRV VAIAVPDADG
     EKLVTIVEFA SWGHSGQEAI DKLRSVKREI TSAISRAHRV RVADVVLVAT GSIPVTTSGK
     VRRSSCAERY RNDGFTRLDR SA