ID   FAA29_MYCBO             Reviewed;         619 AA.
AC   Q7TXK5; A0A1R3Y3G5; X2BMY4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=4-hydroxyphenylalkanoate adenylyltransferase;
DE            EC=6.2.1.51 {ECO:0000250|UniProtKB:P95141};
DE   AltName: Full=Acyl-AMP synthase;
DE   AltName: Full=Long-chain-fatty-acid--AMP ligase FadD29;
DE            Short=FAAL;
GN   Name=fadD29; OrderedLocusNames=BQ2027_MB2974C;
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).
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:0000250|UniProtKB:P95141}.
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:0000250|UniProtKB:P95141};
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:0000250|UniProtKB:P95141};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P95141}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIU01596.1; -; Genomic_DNA.
DR   RefSeq; WP_011799304.1; NC_002945.4.
DR   AlphaFoldDB; Q7TXK5; -.
DR   SMR; Q7TXK5; -.
DR   EnsemblBacteria; SIU01596; SIU01596; BQ2027_MB2974C.
DR   OMA; VMFEGEL; -.
DR   BioCyc; MetaCyc:MON-19624; -.
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: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   3: Inferred from homology;
KW   ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding.
FT   CHAIN           1..619
FT                   /note="4-hydroxyphenylalkanoate adenylyltransferase"
FT                   /id="PRO_0000406358"
SQ   SEQUENCE   619 AA;  67477 MW;  DAF006E5A38E7C0A CRC64;
     MKTNSSFHAA GEVATQPAWG TGEQAAQPLN GSTSRFAMSE SSLADLLQKA ASQYPNRAAY
     KFIDYDTDPA GFTETVTWWQ VHRRAMIVAE ELWIYASSGD RVAILAPQGL EYIIAFMGVL
     QAGLIAVPLP VPQFGIHDER ISSALRDSAP SIILTTSSVI DEVTTYAPHA CAAQGQSAPI
     VVAVDALDLS SSRALDPTRF ERPSTAYLQY TSGSTRAPAG VVLSHKNVIT NCVQLMSDYI
     GDSEKVPSTP VSWLPFYHDM GLMLGIILPM INQDTAVLMS PMAFLQRPAR WMQLLAKHRA
     QISSAPNFGF ELAVRRTSDD DMAGLDLGHV RTIVTGAERV NVATLRRFTE RFAPFNLSET
     AIRPSYGLAE ATVYVATAGP GRAPKSVCFD YQQLSVGQAK RTENGSEGAN LVSYGAPRAS
     TVRIVDPETR MENPAGTVGE IWVQGDNVGL GYWRNPQQTE ATFRARLVTP SPGTSEGPWL
     RTGDLGVIFE GELFITGRIK ELLVVDGANH YPEDIEATIQ EITGGRVVAI AVPDDRTEKL
     VTIIELMKRG RTDEEEKNRL RTVKREVASA ISRSHRLRVA DVVMVAPGSI PVTTSGKVRR
     SASVERYLHH EFSRLDAMA