ID   FAA22_MYCTO             Reviewed;         705 AA.
AC   P9WQ60; L0TE13; P96283; Q7D6D9;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=p-hydroxybenzoic acid--AMP ligase FadD22;
DE            Short=p-HB--AMP ligase FadD22;
DE            EC=6.2.1.50 {ECO:0000250|UniProtKB:Q7TXK7};
DE   AltName: Full=p-hydroxybenzoic acid-AMP synthetase;
DE            Short=p-HB-AMP synthetase;
GN   Name=fadD22; OrderedLocusNames=MT3021;
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: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to
CC       form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly
CC       to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in
CC       a CoA-independent manner by attack of the phosphopantetheine thiol of
CC       FadD22. Usually, this intermediate primes the biosynthesis of the
CC       phenolphthiocerol (PPOL) by presenting the pHBA starter unit for
CC       elongation by Pks15/1, but M.tuberculosis lacks Pks15/1 due to a
CC       natural frameshift and thus is unable to produce PPOL.
CC       {ECO:0000250|UniProtKB:P9WQ61}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxybenzoate + ATP + holo-[4-hydroxyphenylalkanoate
CC         synthase] = 4-hydroxyphenyl-[4-hydroxyphenylalkanoate synthase] + AMP
CC         + diphosphate; Xref=Rhea:RHEA:54696, Rhea:RHEA-COMP:12684, Rhea:RHEA-
CC         COMP:13969, ChEBI:CHEBI:17879, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138321, ChEBI:CHEBI:456215;
CC         EC=6.2.1.50; Evidence={ECO:0000250|UniProtKB:Q7TXK7};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47347.1; -; Genomic_DNA.
DR   PIR; A70669; A70669.
DR   RefSeq; WP_003414884.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ60; -.
DR   SMR; P9WQ60; -.
DR   EnsemblBacteria; AAK47347; AAK47347; MT3021.
DR   KEGG; mtc:MT3021; -.
DR   PATRIC; fig|83331.31.peg.3261; -.
DR   HOGENOM; CLU_000022_59_10_11; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Phosphopantetheine;
KW   Phosphoprotein.
FT   CHAIN           1..705
FT                   /note="p-hydroxybenzoic acid--AMP ligase FadD22"
FT                   /id="PRO_0000426832"
FT   DOMAIN          541..619
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         579
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   705 AA;  75198 MW;  600F2D0EABFDF1DC CRC64;
     MRNGNLAGLL AEQASEAGWY DRPAFYAADV VTHGQIHDGA ARLGEVLRNR GLSSGDRVLL
     CLPDSPDLVQ LLLACLARGV MAFLANPELH RDDHALAARN TEPALVVTSD ALRDRFQPSR
     VAEAAELMSE AARVAPGGYE PMGGDALAYA TYTSGTTGPP KAAIHRHADP LTFVDAMCRK
     ALRLTPEDTG LCSARMYFAY GLGNSVWFPL ATGGSAVINS APVTPEAAAI LSARFGPSVL
     YGVPNFFARV IDSCSPDSFR SLRCVVSAGE ALELGLAERL MEFFGGIPIL DGIGSTEVGQ
     TFVSNRVDEW RLGTLGRVLP PYEIRVVAPD GTTAGPGVEG DLWVRGPAIA KGYWNRPDSP
     VANEGWLDTR DRVCIDSDGW VTYRCRADDT EVIGGVNVDP REVERLIIED EAVAEAAVVA
     VRESTGASTL QAFLVATSGA TIDGSVMRDL HRGLLNRLSA FKVPHRFAVV DRLPRTPNGK
     LVRGALRKQS PTKPIWELSL TEPGSGVRAQ RDDLSASNMT IAGGNDGGAT LRERLVALRQ
     ERQRLVVDAV CAEAAKMLGE PDPWSVDQDL AFSELGFDSQ MTVTLCKRLA AVTGLRLPET
     VGWDYGSISG LAQYLEAELA GGHGRLKSAG PVNSGATGLW AIEEQLNKVE ELVAVIADGE
     KQRVADRLRA LLGTIAGSEA GLGKLIQAAS TPDEIFQLID SELGK