FAA22_MYCMM
ID FAA22_MYCMM Reviewed; 702 AA.
AC B2HIL6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=MMAR_1761;
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 IN THE BIOSYNTHESIS OF PHENOLPHTHIOCEROL, AND MUTAGENESIS OF
RP SER-576.
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).
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}.
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}.
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; CP000854; ACC40210.1; -; Genomic_DNA.
DR RefSeq; WP_012393569.1; NC_010612.1.
DR AlphaFoldDB; B2HIL6; -.
DR SMR; B2HIL6; -.
DR STRING; 216594.MMAR_1761; -.
DR EnsemblBacteria; ACC40210; ACC40210; MMAR_1761.
DR KEGG; mmi:MMAR_1761; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_10_11; -.
DR OMA; PLRDYNA; -.
DR OrthoDB; 377638at2; -.
DR BRENDA; 6.2.1.50; 3506.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001190; 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 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 1: Evidence at protein level;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Phosphopantetheine;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..702
FT /note="p-hydroxybenzoic acid--AMP ligase FadD22"
FT /id="PRO_0000406352"
FT DOMAIN 538..616
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 576
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MUTAGEN 576
FT /note="S->A: Catalyzes pHBA-AMP formation, indicating this
FT residue is not essential for adenylation activity."
FT /evidence="ECO:0000269|PubMed:18158259"
SQ SEQUENCE 702 AA; 75181 MW; AFAAFC5996F683F7 CRC64;
MRNENVAGLL AERASEAGWT DQPAYYAPDV VTHGQIHDGA ARLGAVLANR GLCRGDRVLL
CMPDSPELVQ VLLACLARGI LAFLANPELH RDDHAFQERD TQAALVITSG PLCDRFAPST
VVDAADLFSE AARVGPADYE ILGGDAAAYA TYTSGTTGPP KAAIHRHCDV FAFVEAMCRN
ALRLTPADIG LSSARMYFAY GLGNSVWFPL ATGSSAVVNP LPVGAEVAAT LSARFEPSVL
YGVPNFFARV VDACSADSFR SVRCVVSAGE ALEVGLAERL TEFFGGIPIL DGVGSTEVGQ
TFVSNTVDEW RPGSLGKVLP PYQIRVVAPD GAAAGPGVEG DLWVRGPSIA ESYWNWPEPL
LTDEGWLDTR DRVCIDDDGW VTYACRADDT EIVGAVNINP REIERLIVEE DAVAEVAVVG
VKEATGASTL QAFLVPASAE GIDGSVMRDI HRRLLTRLSA FKVPHRFAVV ERLPRTANGK
LLRSALRGQT PAKPIWELAS AEHRSGAPGQ LDDQSASALV SGSREVSLKE RLAALQQERH
RLVLDAVCGE TAKMLGEPDP RSVNRDLAFS ELGFDSQMTV ELCHRLAAAT GLRVPETVGW
DYGSISGLAQ YLEAELSGAD RRVTPQSARS GARALPLIEA QLNKVEELTA AIADGEKPRV
AERLRALLGT ITEGQEHWGQ RIAAASTPDE IFQLIDSEFG ES
