FAA10_MYCTU
ID FAA10_MYCTU Reviewed; 540 AA.
AC P9WQ55; F2GLP5; L0T2G2; Q10878; Q7DAH0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase FadD10 {ECO:0000305};
DE EC=6.2.1.20 {ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
DE EC=6.2.1.47 {ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
DE AltName: Full=FAAL10 {ECO:0000303|PubMed:22451903};
GN Name=fadD10; OrderedLocusNames=Rv0099;
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 INDUCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15882420; DOI=10.1111/j.1365-2958.2005.04609.x;
RA Rickman L., Scott C., Hunt D.M., Hutchinson T., Menendez M.C., Whalan R.,
RA Hinds J., Colston M.J., Green J., Buxton R.S.;
RT "A member of the cAMP receptor protein family of transcription regulators
RT in Mycobacterium tuberculosis is required for virulence in mice and
RT controls transcription of the rpfA gene coding for a resuscitation
RT promoting factor.";
RL Mol. Microbiol. 56:1274-1286(2005).
RN [3]
RP PRELIMINARY FUNCTION AS FATTY-ACID--COA LIGASE.
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 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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22451903; DOI=10.1073/pnas.1118680109;
RA Chhabra A., Haque A.S., Pal R.K., Goyal A., Rai R., Joshi S., Panjikar S.,
RA Pasha S., Sankaranarayanan R., Gokhale R.S.;
RT "Nonprocessive [2 + 2]e- off-loading reductase domains from mycobacterial
RT nonribosomal peptide synthetases.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:5681-5686(2012).
RN [6] {ECO:0007744|PDB:4IR7, ECO:0007744|PDB:4ISB}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF APOENYZME AND IN COMPLEX WITH
RP DODECANOYL-AMP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DOMAIN.
RX PubMed=23625916; DOI=10.1074/jbc.m113.466912;
RA Liu Z., Ioerger T.R., Wang F., Sacchettini J.C.;
RT "Structures of Mycobacterium tuberculosis FadD10 protein reveal a new type
RT of adenylate-forming enzyme.";
RL J. Biol. Chem. 288:18473-18483(2013).
CC -!- FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as
CC acyl-adenylates (acyl-AMP), which are then transferred to the
CC phosphopantetheine arm of the acyl carrier protein (ACP) Rv0100
CC (PubMed:22451903, PubMed:23625916). Can use octanoate (C8), decanoate
CC (C10), dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16),
CC but not hexanoate (C6) (PubMed:22451903, PubMed:23625916). Long chain
CC saturated fatty acids are the preferred substrates (PubMed:23625916).
CC Cannot use coenzyme A to form acyl-CoA (PubMed:22451903,
CC PubMed:23625916). {ECO:0000269|PubMed:22451903,
CC ECO:0000269|PubMed:23625916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:50460,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12681, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59558, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133242, ChEBI:CHEBI:456215; EC=6.2.1.47;
CC Evidence={ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50461;
CC Evidence={ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC Evidence={ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589;
CC Evidence={ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[ACP] + octanoate = AMP + diphosphate + octanoyl-
CC [ACP]; Xref=Rhea:RHEA:28022, Rhea:RHEA-COMP:9636, Rhea:RHEA-
CC COMP:9685, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78463, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:22451903};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28023;
CC Evidence={ECO:0000269|PubMed:22451903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + decanoate + holo-[ACP] = AMP + decanoyl-[ACP] +
CC diphosphate; Xref=Rhea:RHEA:65004, Rhea:RHEA-COMP:9640, Rhea:RHEA-
CC COMP:9685, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78468, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:22451903};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65005;
CC Evidence={ECO:0000269|PubMed:22451903};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dodecanoate + holo-[ACP] = AMP + diphosphate +
CC dodecanoyl-[ACP]; Xref=Rhea:RHEA:63620, Rhea:RHEA-COMP:9644,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:65264,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22451903,
CC ECO:0000269|PubMed:23625916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63621;
CC Evidence={ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[ACP] + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-[ACP]; Xref=Rhea:RHEA:64888, Rhea:RHEA-COMP:9648,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:78477,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23625916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64889;
CC Evidence={ECO:0000269|PubMed:23625916};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hexadecanoate + holo-[ACP] = AMP + diphosphate +
CC hexadecanoyl-[ACP]; Xref=Rhea:RHEA:63628, Rhea:RHEA-COMP:9652,
CC Rhea:RHEA-COMP:9685, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:64479, ChEBI:CHEBI:78483,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22451903,
CC ECO:0000269|PubMed:23625916};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63629;
CC Evidence={ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23625916}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed by CRP. {ECO:0000269|PubMed:15882420}.
CC -!- DOMAIN: Retains a single open conformational state for both the
CC apo- and ligand-bound forms. {ECO:0000269|PubMed:23625916}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a fatty acyl-CoA ligase (FACL)
CC (PubMed:19182784). However, although FadD10 has a primary sequence
CC similar to FACLs, it is indeed a fatty acyl-AMP ligase (FAAL) that is
CC only able to acylate an ACP (Rv0100) rather than coenzyme A
CC (PubMed:22451903, PubMed:23625916). {ECO:0000269|PubMed:19182784,
CC ECO:0000269|PubMed:22451903, ECO:0000269|PubMed:23625916}.
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DR EMBL; AL123456; CCP42824.1; -; Genomic_DNA.
DR PIR; C70751; C70751.
DR RefSeq; NP_214613.1; NC_000962.3.
DR RefSeq; WP_003400792.1; NC_000962.3.
DR PDB; 4IR7; X-ray; 2.80 A; A=1-540.
DR PDB; 4ISB; X-ray; 2.20 A; A/B=1-540.
DR PDBsum; 4IR7; -.
DR PDBsum; 4ISB; -.
DR AlphaFoldDB; P9WQ55; -.
DR SMR; P9WQ55; -.
DR STRING; 83332.Rv0099; -.
DR SwissLipids; SLP:000000979; -.
DR PaxDb; P9WQ55; -.
DR DNASU; 886933; -.
DR GeneID; 886933; -.
DR KEGG; mtu:Rv0099; -.
DR PATRIC; fig|83332.111.peg.113; -.
DR TubercuList; Rv0099; -.
DR eggNOG; COG0318; Bacteria.
DR OMA; ITEYAGS; -.
DR PhylomeDB; P9WQ55; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Nucleotide-binding; Reference proteome.
FT CHAIN 1..540
FT /note="Medium/long-chain-fatty-acid--[acyl-carrier-protein]
FT ligase FadD10"
FT /id="PRO_0000420403"
FT BINDING 315..316
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23625916"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23625916"
SQ SEQUENCE 540 AA; 56590 MW; 015A8EDD824964C8 CRC64;
MGGKKFQAMP QLPSTVLDRV FEQARQQPEA IALRRCDGTS ALRYRELVAE VGGLAADLRA
QSVSRGSRVL VISDNGPETY LSVLACAKLG AIAVMADGNL PIAAIERFCQ ITDPAAALVA
PGSKMASSAV PEALHSIPVI AVDIAAVTRE SEHSLDAASL AGNADQGSED PLAMIFTSGT
TGEPKAVLLA NRTFFAVPDI LQKEGLNWVT WVVGETTYSP LPATHIGGLW WILTCLMHGG
LCVTGGENTT SLLEILTTNA VATTCLVPTL LSKLVSELKS ANATVPSLRL VGYGGSRAIA
ADVRFIEATG VRTAQVYGLS ETGCTALCLP TDDGSIVKIE AGAVGRPYPG VDVYLAATDG
IGPTAPGAGP SASFGTLWIK SPANMLGYWN NPERTAEVLI DGWVNTGDLL ERREDGFFYI
KGRSSEMIIC GGVNIAPDEV DRIAEGVSGV REAACYEIPD EEFGALVGLA VVASAELDES
AARALKHTIA ARFRRESEPM ARPSTIVIVT DIPRTQSGKV MRASLAAAAT ADKARVVVRG
