FAA29_MYCTU
ID FAA29_MYCTU Reviewed; 619 AA.
AC P95141; L0TCQ6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=4-hydroxyphenylalkanoate adenylyltransferase {ECO:0000305};
DE EC=6.2.1.51 {ECO:0000269|PubMed:20553505};
DE AltName: Full=Acyl-AMP synthase;
DE AltName: Full=FAAL29 {ECO:0000303|PubMed:19182784};
DE AltName: Full=Long-chain-fatty-acid--AMP ligase FadD29;
DE Short=FAAL;
GN Name=fadD29; OrderedLocusNames=Rv2950c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN ACYL-AMP SYNTHASE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15042094; DOI=10.1038/nature02384;
RA Trivedi O.A., Arora P., Sridharan V., Tickoo R., Mohanty D., Gokhale R.S.;
RT "Enzymic activation and transfer of fatty acids as acyl-adenylates in
RT mycobacteria.";
RL Nature 428:441-445(2004).
RN [3]
RP FUNCTION IN FATTY ACID ACTIVATION, AND CATALYTIC ACTIVITY.
RX PubMed=19182784; DOI=10.1038/nchembio.143;
RA Arora P., Goyal A., Natarajan V.T., Rajakumara E., Verma P., Gupta R.,
RA Yousuf M., Trivedi O.A., Mohanty D., Tyagi A., Sankaranarayanan R.,
RA Gokhale R.S.;
RT "Mechanistic and functional insights into fatty acid activation in
RT Mycobacterium tuberculosis.";
RL Nat. Chem. Biol. 5:166-173(2009).
RN [4]
RP FUNCTION IN THE BIOSYNTHESIS OF PHENOLIC GLYCOLIPID, CATALYTIC ACTIVITY,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20553505; DOI=10.1111/j.1742-4658.2010.07688.x;
RA Simeone R., Leger M., Constant P., Malaga W., Marrakchi H., Daffe M.,
RA Guilhot C., Chalut C.;
RT "Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis
RT of phthiocerol dimycocerosates and related compounds in Mycobacterium
RT tuberculosis.";
RL FEBS J. 277:2715-2725(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 (PubMed:15042094, PubMed:19182784, PubMed:20553505). Involved in the
CC biosynthesis of phenolphthiocerol, which is an important intermediate
CC in the biosynthesis of phenolic glycolipid (PGL), also called mycosid B
CC (PubMed:20553505). {ECO:0000269|PubMed:15042094,
CC ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20553505}.
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:0000269|PubMed:20553505};
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:0000269|PubMed:20553505};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP;
CC Xref=Rhea:RHEA:43712, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83623;
CC Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20553505};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713;
CC Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:20553505};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000269|PubMed:20553505}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes the production
CC of phenolic glycolipid (PGL). Mutant can still produce phthiocerol
CC dimycocerosate (DIM A) and phthiodiolone dimycocerosate (DIM B).
CC {ECO:0000269|PubMed:20553505}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45754.1; -; Genomic_DNA.
DR PIR; C70669; C70669.
DR RefSeq; NP_217466.3; NC_000962.3.
DR RefSeq; WP_003899553.1; NC_000962.3.
DR AlphaFoldDB; P95141; -.
DR SMR; P95141; -.
DR STRING; 83332.Rv2950c; -.
DR SwissLipids; SLP:000000986; -.
DR PaxDb; P95141; -.
DR DNASU; 887202; -.
DR GeneID; 887202; -.
DR KEGG; mtu:Rv2950c; -.
DR TubercuList; Rv2950c; -.
DR eggNOG; COG0318; Bacteria.
DR InParanoid; P95141; -.
DR OMA; VMFEGEL; -.
DR BRENDA; 6.2.1.51; 3445.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016878; F:acid-thiol ligase activity; IDA:MTBBASE.
DR GO; GO:0070566; F:adenylyltransferase activity; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IMP:UniProtKB.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:MTBBASE.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0097040; P:phthiocerol biosynthetic process; IDA:MTBBASE.
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..619
FT /note="4-hydroxyphenylalkanoate adenylyltransferase"
FT /id="PRO_0000406357"
SQ SEQUENCE 619 AA; 67447 MW; ED3F2E536CAF24B5 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 RAENGSEGAN LVSYGAPRAS
TVRIVDPETR MENPAGTVGE IWVQGDNVGL GYWRNPQQTE ATFRARLVTP SPGTSEGPWL
RTGDLGVIFE GELFITGRIK ELLVVDGANH YPEDIEATIQ EITGGRVVAI AVPDDRTEKL
VTIIELMKRG RTDEEEKNRL RTVKREVASA ISRSHRLRVA DVVMVAPGSI PVTTSGKVRR
SASVERYLHH EFSRLDAMA
