FAA30_MYCTU
ID FAA30_MYCTU Reviewed; 585 AA.
AC P9WQ57; L0T3F7; P95213; Q7D9V7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Probable long-chain-fatty-acid--AMP ligase FadD30 {ECO:0000305};
DE Short=FAAL;
DE EC=6.2.1.- {ECO:0000269|PubMed:15042094};
DE AltName: Full=Acyl-AMP synthetase;
DE AltName: Full=FAAL30 {ECO:0000303|PubMed:19182784};
GN Name=fadD30; OrderedLocusNames=Rv0404;
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 SYNTHETASE.
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 IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP 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 [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 a multifunctional
CC polyketide synthase (PKS) for further chain extension.
CC {ECO:0000305|PubMed:15042094}.
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:15042094};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713;
CC Evidence={ECO:0000269|PubMed:15042094};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43135.1; -; Genomic_DNA.
DR PIR; C70634; C70634.
DR RefSeq; NP_214918.1; NC_000962.3.
DR RefSeq; WP_003900139.1; NZ_NVQJ01000002.1.
DR AlphaFoldDB; P9WQ57; -.
DR SMR; P9WQ57; -.
DR STRING; 83332.Rv0404; -.
DR SwissLipids; SLP:000000987; -.
DR PaxDb; P9WQ57; -.
DR DNASU; 886409; -.
DR GeneID; 886409; -.
DR KEGG; mtu:Rv0404; -.
DR TubercuList; Rv0404; -.
DR eggNOG; COG0318; Bacteria.
DR OMA; HATIRDK; -.
DR PhylomeDB; P9WQ57; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001584; Chromosome.
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; IMP:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0052559; P:induction by symbiont of host immune response; IDA:MTBBASE.
DR GO; GO:0008610; P:lipid biosynthetic process; IMP: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 1: Evidence at protein level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..585
FT /note="Probable long-chain-fatty-acid--AMP ligase FadD30"
FT /id="PRO_0000406631"
SQ SEQUENCE 585 AA; 63843 MW; B16A77089F760F18 CRC64;
MSVISTLRDR ATTTPSDEAF VFMDYDTKTG DQIDRMTWSQ LYSRVTAVSA YLISYGRHAD
RRRTAAISAP QGLDYVAGFL GALCAGWTPV PLPEPLGSLR DKRTGLAVLD CAADVVLTTS
QAETRVRATI ATHGASVTTP VIALDTLDEP SGDNCDLDSQ LSDWSSYLQY TSGSTANPRG
VVLSMRNVTE NVDQIIRNYF RHEGGAPRLP SSVVSWLPLY HDMGLMVGLF IPLFVGCPVI
LTSPEAFIRK PARWMQLLAK HQAPFSAAPN FAFDLAVAKT SEEDMAGLDL GHVNTIINGA
EQVQPNTITK FLRRFRPYNL MPAAVKPSYG MAEAVVYLAT TKAGSPPTST EFDADSLARG
HAELSTFETE RATRLIRYHS DDKEPLLRIV DPDSNIELGP GRIGEIWIHG KNVSTGYHNA
DDALNRDKFQ ASIREASAGT PRSPWLRTGD LGFIVGDEFY IVGRMKDLII QDGVNHYPDD
IETTVKEFTG GRVAAFSVSD DGVEHLVIAA EVRTEHGPDK VTIMDFSTIK RLVVSALSKL
HGLHVTDFLL VPPGALPKTT SGKISRAACA KQYGANKLQR VATFP