FAC19_MYCTU
ID FAC19_MYCTU Reviewed; 548 AA.
AC P9WQ51; L0TEC7; Q6MWW5; Q7D5D8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase {ECO:0000303|PubMed:15042094, ECO:0000303|PubMed:24244004};
DE Short=FACL {ECO:0000303|PubMed:15042094};
DE EC=6.2.1.2 {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
DE EC=6.2.1.3 {ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
DE EC=6.2.1.42 {ECO:0000269|PubMed:24244004};
DE AltName: Full=Acyl-CoA synthetase {ECO:0000303|PubMed:15042094};
DE AltName: Full=FACL19 {ECO:0000303|PubMed:19182784};
DE AltName: Full=Steroid-CoA ligase {ECO:0000303|PubMed:24244004};
DE AltName: Full=Steroid-coenzyme A ligase {ECO:0000303|PubMed:24244004};
GN Name=fadD19 {ECO:0000303|PubMed:15042094, ECO:0000303|PubMed:24244004};
GN OrderedLocusNames=Rv3515c;
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, AND CATALYTIC ACTIVITY.
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, AND CATALYTIC ACTIVITY.
RX PubMed=15984864; DOI=10.1021/ja052991s;
RA Arora P., Vats A., Saxena P., Mohanty D., Gokhale R.S.;
RT "Promiscuous fatty acyl CoA ligases produce acyl-CoA and acyl-SNAC
RT precursors for polyketide biosynthesis.";
RL J. Am. Chem. Soc. 127:9388-9389(2005).
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 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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=24244004; DOI=10.1128/jb.01012-13;
RA Casabon I., Swain K., Crowe A.M., Eltis L.D., Mohn W.W.;
RT "Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain
RT catabolism.";
RL J. Bacteriol. 196:579-587(2014).
CC -!- FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as
CC acyl-coenzyme A (acyl-CoA), which are then transferred to the
CC multifunctional polyketide synthase (PKS) type III for further chain
CC extension (PubMed:15042094, PubMed:15984864, PubMed:19182784). Also
CC involved in the degradation of cholesterol via the degradation of the
CC side chains of C-24 branched-chain sterols. Catalyzes the ATP-dependent
CC CoA thioesterification of the sterol 3-oxocholest-4-en-26-oate to yield
CC 3-oxocholest-4-en-26-oyl-CoA. It can also use 3beta-hydroxy-5-
CC cholesten-26-oate (PubMed:24244004). {ECO:0000269|PubMed:15042094,
CC ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784,
CC ECO:0000269|PubMed:24244004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:15984864,
CC ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:15984864,
CC ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3-oxocholest-4-en-26-oate + ATP + CoA = (25S)-3-
CC oxocholest-4-en-26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:29291,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:71541, ChEBI:CHEBI:83819, ChEBI:CHEBI:456215;
CC EC=6.2.1.42; Evidence={ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29292;
CC Evidence={ECO:0000269|PubMed:24244004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864,
CC ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15042094,
CC ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:15984864,
CC ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864,
CC ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-
CC CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxytetradecanoate + ATP + CoA = 3-hydroxytetradecanoyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:44212, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84197,
CC ChEBI:CHEBI:84198, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44213;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-hydroxyoctadecanoate + ATP + CoA = 12-hydroxyoctadecanoyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:44216, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84201,
CC ChEBI:CHEBI:84202, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44217;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=15-hydroxypentadecanoate + ATP + CoA = 15-
CC hydroxypentadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44220,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:84203, ChEBI:CHEBI:84205, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44221;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16-hydroxyhexadecanoate + ATP + CoA = 16-hydroxyhexadecanoyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:44224, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:55329, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:84207, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44225;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylhexadecanoate + ATP + CoA = 2-methylhexadecanoyl-CoA +
CC AMP + diphosphate; Xref=Rhea:RHEA:44192, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84175,
CC ChEBI:CHEBI:84182, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44193;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylundecanoate + ATP + CoA = 3-methylundecanoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:44196, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84183,
CC ChEBI:CHEBI:84184, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44197;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-methyltridecanoate + ATP + CoA = 12-methyltridecanoyl-CoA +
CC AMP + diphosphate; Xref=Rhea:RHEA:44208, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84193,
CC ChEBI:CHEBI:84195, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44209;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-methyloctadecanoate + ATP + CoA = 12-methyloctadecanoyl-CoA
CC + AMP + diphosphate; Xref=Rhea:RHEA:44200, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84176,
CC ChEBI:CHEBI:84181, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15984864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44201;
CC Evidence={ECO:0000269|PubMed:15984864};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25S)-3beta-hydroxy-5-cholestenoate + ATP + CoA = (25S)-3beta-
CC hydroxy-5-cholestenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:43880,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:71567, ChEBI:CHEBI:83783, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43881;
CC Evidence={ECO:0000269|PubMed:24244004};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for 3-oxo-4-cholesten-26-oate (at pH 7.3 and 22 degrees
CC Celsius) {ECO:0000269|PubMed:24244004};
CC Vmax=2.3 umol/min/mg enzyme with 3-oxo-4-cholesten-26-oate as
CC substrate (at pH 7.3 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:24244004};
CC Note=kcat is 0.75 sec(-1) for 3-oxo-4-cholesten-26-oate--CoA ligase
CC activity (at pH 7.3 and 22 degrees Celsius).
CC {ECO:0000269|PubMed:24244004};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000305|PubMed:15042094}.
CC -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC {ECO:0000305|PubMed:24244004}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46337.1; -; Genomic_DNA.
DR PIR; E70807; E70807.
DR RefSeq; WP_003901660.1; NZ_KK339374.1.
DR RefSeq; YP_177983.1; NC_000962.3.
DR AlphaFoldDB; P9WQ51; -.
DR SMR; P9WQ51; -.
DR STRING; 83332.Rv3515c; -.
DR BindingDB; P9WQ51; -.
DR ChEMBL; CHEMBL5182; -.
DR SwissLipids; SLP:000000976; -.
DR PaxDb; P9WQ51; -.
DR PRIDE; P9WQ51; -.
DR DNASU; 888275; -.
DR GeneID; 888275; -.
DR KEGG; mtu:Rv3515c; -.
DR TubercuList; Rv3515c; -.
DR eggNOG; COG0318; Bacteria.
DR OMA; WRHEDVW; -.
DR PhylomeDB; P9WQ51; -.
DR BioCyc; MetaCyc:G185E-7792-MON; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00296; -.
DR PRO; PR:P9WQ51; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MTBBASE.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:UniProtKB.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0052572; P:response to host immune response; IEP:MTBBASE.
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 ATP-binding; Cholesterol metabolism; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Nucleotide-binding; Reference proteome;
KW Steroid metabolism; Sterol metabolism.
FT CHAIN 1..548
FT /note="Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-
FT 26-oate--CoA ligase"
FT /id="PRO_0000406790"
FT REGION 520..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 548 AA; 59741 MW; E574B4BFA86F324E CRC64;
MAVALNIADL AEHAIDAVPD RVAVICGDEQ LTYAQLEDKA NRLAHHLIDQ GVQKDDKVGL
YCRNRIEIVI AMLGIVKAGA ILVNVNFRYV EGELRYLFDN SDMVALVHER RYADRVANVL
PDTPHVRTIL VVEDGSDQDY RRYGGVEFYS AIAAGSPERD FGERSADAIY LLYTGGTTGF
PKGVMWRHED IYRVLFGGTD FATGEFVKDE YDLAKAAAAN PPMIRYPIPP MIHGATQSAT
WMALFSGQTT VLAPEFNADE VWRTIHKHKV NLLFFTGDAM ARPLVDALVK GNDYDLSSLF
LLASTAALFS PSIKEKLLEL LPNRVITDSI GSSETGFGGT SVVAAGQAHG GGPRVRIDHR
TVVLDDDGNE VKPGSGMRGV IAKKGNIPVG YYKDEKKTAE TFRTINGVRY AIPGDYAQVE
EDGTVTMLGR GSVSINSGGE KVYPEEVEAA LKGHPDVFDA LVVGVPDPRY GQQVAAVVQA
RPGCRPSLAE LDSFVRSEIA GYKVPRSLWF VDEVKRSPAG KPDYRWAKEQ TEARPADDVH
AGHVTSGG
