ID FAA22_MYCBO Reviewed; 705 AA.
AC Q7TXK7; A0A1R3Y2P5; X2BM70;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=p-hydroxybenzoic acid--AMP ligase FadD22;
DE Short=p-HB--AMP ligase FadD22;
DE EC=6.2.1.50 {ECO:0000269|PubMed:25561717};
DE AltName: Full=p-hydroxybenzoic acid-AMP synthetase;
DE Short=p-HB-AMP synthetase;
GN Name=fadD22; OrderedLocusNames=BQ2027_MB2972C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 FUNCTION IN THE BIOSYNTHESIS OF PHENOLPHTHIOCEROL, REACTION MECHANISM, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=18158259; DOI=10.1016/j.chembiol.2007.11.010;
RA Ferreras J.A., Stirrett K.L., Lu X., Ryu J.S., Soll C.E., Tan D.S.,
RA Quadri L.E.;
RT "Mycobacterial phenolic glycolipid virulence factor biosynthesis: mechanism
RT and small-molecule inhibition of polyketide chain initiation.";
RL Chem. Biol. 15:51-61(2008).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 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. This intermediate primes the biosynthesis of the
CC phenolphthiocerol (PPOL) by presenting the pHBA starter unit for
CC elongation by Pks15/1. PPOL is an important intermediate in the
CC biosynthesis of phenolic glycolipid (mycosid B).
CC {ECO:0000269|PubMed:18158259, ECO:0000269|PubMed:25561717}.
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:0000269|PubMed:25561717};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC -!- DISRUPTION PHENOTYPE: Disruption of fadD22 abolishes the production of
CC phenolphthioceroL. {ECO:0000269|PubMed:18158259}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT708304; SIU01594.1; -; Genomic_DNA.
DR RefSeq; NP_856617.1; NC_002945.3.
DR RefSeq; WP_003414884.1; NC_002945.4.
DR AlphaFoldDB; Q7TXK7; -.
DR SMR; Q7TXK7; -.
DR PATRIC; fig|233413.5.peg.3264; -.
DR BioCyc; MetaCyc:MONOMER-19623; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0016874; F:ligase activity; IMP:UniProtKB.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR CDD; cd05919; BCL_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43352; ACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR43352:SF1; P-HYDROXYBENZOIC ACID--AMP LIGASE FADD22; 1.
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; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Phosphopantetheine;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..705
FT /note="p-hydroxybenzoic acid--AMP ligase FadD22"
FT /id="PRO_0000406351"
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
//
