FAA32_MYCTU
ID FAA32_MYCTU Reviewed; 637 AA.
AC O53580; L0TGT1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Long-chain-fatty-acid--AMP ligase FadD32 {ECO:0000305};
DE Short=FAAL {ECO:0000303|PubMed:19477415};
DE EC=6.2.1.20 {ECO:0000269|PubMed:19436070};
DE AltName: Full=Acyl-AMP synthetase;
DE AltName: Full=FAAL32 {ECO:0000303|PubMed:19182784};
GN Name=fadD32; OrderedLocusNames=Rv3801c;
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 FUNCTION, 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19436070; DOI=10.1074/jbc.m109.006940;
RA Gavalda S., Leger M., van der Rest B., Stella A., Bardou F., Montrozier H.,
RA Chalut C., Burlet-Schiltz O., Marrakchi H., Daffe M., Quemard A.;
RT "The Pks13/FadD32 crosstalk for the biosynthesis of mycolic acids in
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 284:19255-19264(2009).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=19477415; DOI=10.1016/j.chembiol.2009.03.012;
RA Leger M., Gavalda S., Guillet V., van der Rest B., Slama N., Montrozier H.,
RA Mourey L., Quemard A., Daffe M., Marrakchi H.;
RT "The dual function of the Mycobacterium tuberculosis FadD32 required for
RT mycolic acid biosynthesis.";
RL Chem. Biol. 16:510-519(2009).
RN [7]
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 [8]
RP MUTAGENESIS OF PHE-383 AND PHE-481, AND SUBSTRATE SELECTIVITY.
RX PubMed=22206988; DOI=10.1016/j.jmb.2011.12.031;
RA Goyal A., Verma P., Anandhakrishnan M., Gokhale R.S., Sankaranarayanan R.;
RT "Molecular basis of the functional divergence of fatty acyl-AMP ligase
RT biosynthetic enzymes of Mycobacterium tuberculosis.";
RL J. Mol. Biol. 416:221-238(2012).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION AS A DRUG TARGET.
RX PubMed=23364516; DOI=10.1177/1087057112474691;
RA Galandrin S., Guillet V., Rane R.S., Leger M., N R., Eynard N., Das K.,
RA Balganesh T.S., Mourey L., Daffe M., Marrakchi H.;
RT "Assay development for identifying inhibitors of the mycobacterial FadD32
RT activity.";
RL J. Biomol. Screen. 18:576-587(2013).
RN [10]
RP IDENTIFICATION AS A DRUG TARGET, AND MUTAGENESIS OF GLU-120 AND PHE-291.
RX PubMed=23798446; DOI=10.1073/pnas.1302114110;
RA Stanley S.A., Kawate T., Iwase N., Shimizu M., Clatworthy A.E.,
RA Kazyanskaya E., Sacchettini J.C., Ioerger T.R., Siddiqi N.A., Minami S.,
RA Aquadro J.A., Grant S.S., Rubin E.J., Hung D.T.;
RT "Diarylcoumarins inhibit mycolic acid biosynthesis and kill Mycobacterium
RT tuberculosis by targeting FadD32.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11565-11570(2013).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=26900152; DOI=10.1074/jbc.m115.712612;
RA Guillet V., Galandrin S., Maveyraud L., Ladeveze S., Mariaule V., Bon C.,
RA Eynard N., Daffe M., Marrakchi H., Mourey L.;
RT "Insight into structure-function relationships and inhibition of the fatty
RT acyl-AMP ligase (FadD32) orthologs from Mycobacteria.";
RL J. Biol. Chem. 291:7973-7989(2016).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT
RP THR-552, AND MUTAGENESIS OF THR-552.
RX PubMed=27590338; DOI=10.1074/jbc.m116.748053;
RA Le N.H., Molle V., Eynard N., Miras M., Stella A., Bardou F., Galandrin S.,
RA Guillet V., Andre-Leroux G., Bellinzoni M., Alzari P., Mourey L.,
RA Burlet-Schiltz O., Daffe M., Marrakchi H.;
RT "Ser/Thr phosphorylation regulates the fatty acyl-AMP ligase activity of
RT FadD32, an essential enzyme in mycolic acid biosynthesis.";
RL J. Biol. Chem. 291:22793-22805(2016).
RN [13]
RP IDENTIFICATION AS A DRUG TARGET.
RX PubMed=30316633; DOI=10.1016/j.bmcl.2018.09.037;
RA Fang C., Lee K.K., Nietupski R., Bates R.H., Fernandez-Menendez R.,
RA Lopez-Roman E.M., Guijarro-Lopez L., Yin Y., Peng Z., Gomez J.E.,
RA Fisher S., Barros-Aguirre D., Hubbard B.K., Serrano-Wu M.H., Hung D.T.;
RT "Discovery of heterocyclic replacements for the coumarin core of anti-
RT tubercular FadD32 inhibitors.";
RL Bioorg. Med. Chem. Lett. 28:3529-3533(2018).
RN [14] {ECO:0007744|PDB:5HM3}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 2-637 IN COMPLEX WITH PHU-AMS
RP INHIBITOR, FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=27547819; DOI=10.1021/acsinfecdis.6b00082;
RA Kuhn M.L., Alexander E., Minasov G., Page H.J., Warwrzak Z., Shuvalova L.,
RA Flores K.J., Wilson D.J., Shi C., Aldrich C.C., Anderson W.F.;
RT "Structure of the essential Mtb FadD32 enzyme: a promising drug target for
RT treating tuberculosis.";
RL ACS Infect. Dis. 2:579-591(2016).
CC -!- FUNCTION: Involved in the biosynthesis of mycolic acids
CC (PubMed:19436070, PubMed:19477415). Catalyzes the activation of long-
CC chain fatty acids as acyl-adenylates (acyl-AMP), which are then
CC transferred to the phosphopantetheine arm of the polyketide synthase
CC Pks13 for further chain extension (PubMed:15042094, PubMed:19436070,
CC PubMed:19477415, PubMed:27547819, PubMed:27590338). Can use dodecanoate
CC (C12), tetradecanoate (C14) and hexadecanoate (C16) (PubMed:19182784,
CC PubMed:19436070, PubMed:19477415, PubMed:23364516, PubMed:26900152,
CC PubMed:27590338). In vitro, displays a preference for long-chain over
CC medium and short-chain fatty acid substrates (PubMed:19477415).
CC {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784,
CC ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:19477415,
CC ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:26900152,
CC ECO:0000269|PubMed:27547819, ECO:0000269|PubMed:27590338}.
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:19436070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589;
CC Evidence={ECO:0000269|PubMed:19436070};
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:19436070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63621;
CC Evidence={ECO:0000269|PubMed:19436070};
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:19477415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64889;
CC Evidence={ECO:0000269|PubMed:19477415};
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:19436070};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63629;
CC Evidence={ECO:0000269|PubMed:19436070};
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:19477415, ECO:0000269|PubMed:23364516,
CC ECO:0000269|PubMed:26900152, ECO:0000269|PubMed:27590338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713;
CC Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:23364516,
CC ECO:0000269|PubMed:26900152, ECO:0000269|PubMed:27590338};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + tetradecanoate = diphosphate + tetradecanoyl-AMP;
CC Xref=Rhea:RHEA:43704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:83626;
CC Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:26900152};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43705;
CC Evidence={ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:26900152};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + hexadecanoate = diphosphate + hexadecanoyl-AMP;
CC Xref=Rhea:RHEA:43708, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83627;
CC Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:19477415};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43709;
CC Evidence={ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:19477415};
CC -!- ACTIVITY REGULATION: Fatty acyl-AMP ligase activity and transferase
CC activity onto Pks13 are both inhibited by phosphorylation
CC (PubMed:27590338). The acyl-AMP ligase activity is inhibited by the
CC alkylphosphate ester of AMP, adenosine 50-dodecylphosphate (AMPC12)
CC (PubMed:19477415, PubMed:26900152). Also inhibited by eicosyl-AMP
CC (AMPC20) (PubMed:26900152). Loading of the acyl-AMP onto Pks13 is
CC inhibited by 5'-O-[N-(11-phenoxyundecanoyl)sulfamoyl]adenosine (PhU-
CC AMS) (PubMed:27547819). {ECO:0000269|PubMed:19477415,
CC ECO:0000269|PubMed:26900152, ECO:0000269|PubMed:27547819,
CC ECO:0000269|PubMed:27590338}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2640 uM for dodecanoate {ECO:0000269|PubMed:19477415};
CC KM=72.09 uM for dodecanoate {ECO:0000269|PubMed:26900152};
CC KM=20.5 uM for tetradecanoate {ECO:0000269|PubMed:19477415};
CC KM=4.77 uM for tetradecanoate {ECO:0000269|PubMed:26900152};
CC KM=3.2 uM for hexadecanoate {ECO:0000269|PubMed:19477415};
CC KM=2020 uM for ATP {ECO:0000269|PubMed:19477415};
CC KM=248 uM for ATP {ECO:0000269|PubMed:26900152};
CC Note=kcat is 0.150 min(-1) with dodecanoate as substrate
CC (PubMed:19477415). kcat is 2.04 min(-1) with dodecanoate as substrate
CC (PubMed:26900152). kcat is 0.123 min(-1) with tetradecanoate as
CC substrate (PubMed:19477415). kcat is 0.98 min(-1) with tetradecanoate
CC as substrate (PubMed:26900152). kcat is 0.015 min(-1) with
CC hexadecanoate as substrate (PubMed:19477415).
CC {ECO:0000269|PubMed:19477415, ECO:0000269|PubMed:26900152};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000269|PubMed:19436070, ECO:0000269|PubMed:19477415}.
CC -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:19477415}.
CC -!- PTM: Phosphorylated on Thr-552 by PknA, PknB, PknD and PknF.
CC Dephosphorylated by PstP. Phosphorylation regulates activity.
CC {ECO:0000269|PubMed:27590338}.
CC -!- MISCELLANEOUS: Was identified as a drug target (PubMed:23364516,
CC PubMed:23798446, PubMed:30316633). Inhibited by a series of 4,6-diaryl-
CC 5,7-dimethyl coumarins that directly inhibit the acyl-acyl carrier
CC protein synthetase activity of FadD32 and kill M.tuberculosis. They
CC effectively block bacterial replication both in vitro and in animal
CC models of tuberculosis (PubMed:23798446). Quinoline-2-carboxamides have
CC also potent anti-tubercular activity (PubMed:30316633).
CC {ECO:0000269|PubMed:23364516, ECO:0000269|PubMed:23798446,
CC ECO:0000269|PubMed:30316633}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46630.1; -; Genomic_DNA.
DR PIR; E70887; E70887.
DR RefSeq; NP_218318.1; NC_000962.3.
DR RefSeq; WP_003899700.1; NC_000962.3.
DR PDB; 5HM3; X-ray; 2.25 A; A=2-637.
DR PDBsum; 5HM3; -.
DR AlphaFoldDB; O53580; -.
DR SMR; O53580; -.
DR STRING; 83332.Rv3801c; -.
DR BindingDB; O53580; -.
DR ChEMBL; CHEMBL4295665; -.
DR SwissLipids; SLP:000000972; -.
DR PaxDb; O53580; -.
DR DNASU; 886130; -.
DR GeneID; 886130; -.
DR KEGG; mtu:Rv3801c; -.
DR PATRIC; fig|83332.111.peg.4226; -.
DR TubercuList; Rv3801c; -.
DR eggNOG; COG0318; Bacteria.
DR InParanoid; O53580; -.
DR OMA; NGRNIWP; -.
DR PhylomeDB; O53580; -.
DR BioCyc; MetaCyc:G185E-8097-MON; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA: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:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
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:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0071769; P:mycolate cell wall layer assembly; IMP: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 3D-structure; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..637
FT /note="Long-chain-fatty-acid--AMP ligase FadD32"
FT /id="PRO_0000406634"
FT BINDING 194..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 349
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 490
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:27590338"
FT MUTAGEN 120
FT /note="E->A: Confers resistance to the coumarin
FT inhibitors."
FT /evidence="ECO:0000269|PubMed:23798446"
FT MUTAGEN 291
FT /note="F->L: Confers resistance to the coumarin
FT inhibitors."
FT /evidence="ECO:0000269|PubMed:23798446"
FT MUTAGEN 383
FT /note="F->A: Catalyzes the formation of acyl-CoA; when
FT associated with A-481."
FT /evidence="ECO:0000269|PubMed:22206988"
FT MUTAGEN 481
FT /note="F->A: Catalyzes the formation of acyl-CoA; when
FT associated with A-383."
FT /evidence="ECO:0000269|PubMed:22206988"
FT MUTAGEN 552
FT /note="T->D: Phosphomimetic mutant. 55% decrease in
FT activity."
FT /evidence="ECO:0000269|PubMed:27590338"
FT MUTAGEN 552
FT /note="T->V: Cannot be phosphorylated. No change in
FT activity."
FT /evidence="ECO:0000269|PubMed:27590338"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 64..81
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 442..449
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 461..464
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 470..481
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 484..490
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 518..529
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 535..537
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 554..562
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 571..586
FT /evidence="ECO:0007829|PDB:5HM3"
FT STRAND 592..596
FT /evidence="ECO:0007829|PDB:5HM3"
FT HELIX 611..619
FT /evidence="ECO:0007829|PDB:5HM3"
FT TURN 620..624
FT /evidence="ECO:0007829|PDB:5HM3"
SQ SEQUENCE 637 AA; 69232 MW; 0A3A86CED9AE0EDC CRC64;
MFVTGESGMA YHNPFIVNGK IRFPANTNLV RHVEKWAKVR GDKLAYRFLD FSTERDGVAR
DILWSDFSAR NRAVGARLQQ VTQPGDRVAI LCPQNLDYLI SFFGALYSGR IAVPLFDPAE
PGHVGRLHAV LDDCAPSTIL TTTDSAEGVR KFIRARSAKE RPRVIAVDAV PTEVAATWQQ
PEANEETVAY LQYTSGSTRI PSGVQITHLN LPTNVVQVLN ALEGQEGDRG VSWLPFFHDM
GLITVLLASV LGHSFTFMTP AAFVRRPGRW IRELARKPGE TGGTFSAAPN FAFEHAAVRG
VPRDDEPPLD LSNVKGILNG SEPVSPASMR KFFEAFAPYG LKQTAVKPSY GLAEATLFVS
TTPMDEVPTV IHVDRDELNN QRFVEVAADA PNAVAQVSAG KVGVSEWAVI VDADTASELP
DGQIGEIWLH GNNLGTGYWG KEEESAQTFK NILKSRISES RAEGAPDDAL WVRTGDYGTY
FKDHLYIAGR IKDLVIIDGR NHYPQDLECT AQESTKALRV GYAAAFSVPA NQLPQTVFDD
SHAGLKFDPE DTSEQLVIVG ERAAGTHKLD HQPIVDDIRA AIAVGHGVTV RDVLLVSAGT
IPRTSSGKIG RRACRAAYLD GSLRSGVGSP TVFATSD
