4CLL7_ARATH
ID 4CLL7_ARATH Reviewed; 544 AA.
AC Q9M0X9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=4-coumarate--CoA ligase-like 7 {ECO:0000303|PubMed:12805634};
DE EC=6.2.1.- {ECO:0000305|PubMed:15677481, ECO:0000305|PubMed:18267944};
DE AltName: Full=4-coumarate--CoA ligase isoform 6;
DE Short=At4CL6;
GN Name=4CLL7 {ECO:0000303|PubMed:12805634};
GN OrderedLocusNames=At4g05160 {ECO:0000312|Araport:AT4G05160};
GN ORFNames=C17L7.80 {ECO:0000312|EMBL:CAB81058.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY ORGANIZATION.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12805634; DOI=10.1104/pp.103.020552;
RA Shockey J.M., Fulda M.S., Browse J.;
RT "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme
RT a synthetases.";
RL Plant Physiol. 132:1065-1076(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY ORGANIZATION.
RX PubMed=12819348; DOI=10.1073/pnas.1430550100;
RA Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D.,
RA Kombrink E., Stuible H.-P.;
RT "The substrate specificity-determining amino acid code of 4-coumarate:CoA
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15677481; DOI=10.1074/jbc.m413578200;
RA Schneider K., Kienow L., Schmelzer E., Colby T., Bartsch M., Miersch O.,
RA Wasternack C., Kombrink E., Stuible H.-P.;
RT "A new type of peroxisomal acyl-coenzyme A synthetase from Arabidopsis
RT thaliana has the catalytic capacity to activate biosynthetic precursors of
RT jasmonic acid.";
RL J. Biol. Chem. 280:13962-13972(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=18267944; DOI=10.1093/jxb/erm325;
RA Kienow L., Schneider K., Bartsch M., Stuible H.-P., Weng H., Miersch O.,
RA Wasternack C., Kombrink E.;
RT "Jasmonates meet fatty acids: functional analysis of a new acyl-coenzyme A
RT synthetase family from Arabidopsis thaliana.";
RL J. Exp. Bot. 59:403-419(2008).
CC -!- FUNCTION: Contributes to jasmonic acid biosynthesis by initiating the
CC beta-oxidative chain shortening of its precursors.
CC {ECO:0000269|PubMed:15677481, ECO:0000269|PubMed:18267944}.
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:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:18267944};
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:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000269|PubMed:18267944};
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:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC Evidence={ECO:0000269|PubMed:18267944};
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:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + heptanoate = AMP + diphosphate + heptanoyl-CoA;
CC Xref=Rhea:RHEA:44088, ChEBI:CHEBI:30616, ChEBI:CHEBI:32362,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78811,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44089;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-
CC octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + OPC-6 = AMP + diphosphate + OPC-6-CoA;
CC Xref=Rhea:RHEA:54956, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:138430, ChEBI:CHEBI:138431,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54957;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=75 uM for hexanoic acid {ECO:0000269|PubMed:15677481,
CC ECO:0000269|PubMed:18267944};
CC KM=6 uM for nonanoic acid {ECO:0000269|PubMed:15677481,
CC ECO:0000269|PubMed:18267944};
CC KM=54 uM for tetradecanoic acid {ECO:0000269|PubMed:15677481,
CC ECO:0000269|PubMed:18267944};
CC KM=93 uM for OPDA {ECO:0000269|PubMed:15677481,
CC ECO:0000269|PubMed:18267944};
CC KM=187 uM for OPC-6:0 {ECO:0000269|PubMed:15677481,
CC ECO:0000269|PubMed:18267944};
CC Note=kcat is 1.26 sec(-1) with hexanoic acid as substrate
CC (PubMed:18267944, PubMed:15677481). kcat is 1.38 sec(-1) with
CC nonanoic acid as substrate (PubMed:18267944, PubMed:15677481). kcat
CC is 2.31 sec(-1) with tetradecanoic acid as substrate
CC (PubMed:18267944, PubMed:15677481). kcat is 0.3 sec(-1) with OPDA as
CC substrate (PubMed:18267944, PubMed:15677481). kcat is 0.41 sec(-1)
CC with OPC-6:0 as substrate (PubMed:18267944, PubMed:15677481).
CC {ECO:0000269|PubMed:15677481, ECO:0000269|PubMed:18267944};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15677481}.
CC -!- TISSUE SPECIFICITY: Expressed at low level in leaves.
CC {ECO:0000269|PubMed:18267944}.
CC -!- INDUCTION: By methyl jasmonate. {ECO:0000269|PubMed:15677481}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype in growth, root and flower
CC development, fertility, reproduction and morphology.
CC {ECO:0000269|PubMed:18267944}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY250839; AAP03022.1; -; mRNA.
DR EMBL; AL161502; CAB81058.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82486.1; -; Genomic_DNA.
DR EMBL; AY091079; AAM13899.1; -; mRNA.
DR EMBL; AY122950; AAM67483.1; -; mRNA.
DR PIR; H85064; H85064.
DR RefSeq; NP_192425.1; NM_116755.5.
DR AlphaFoldDB; Q9M0X9; -.
DR SMR; Q9M0X9; -.
DR STRING; 3702.AT4G05160.1; -.
DR SwissLipids; SLP:000001791; -.
DR PaxDb; Q9M0X9; -.
DR PRIDE; Q9M0X9; -.
DR ProteomicsDB; 243266; -.
DR DNASU; 825864; -.
DR EnsemblPlants; AT4G05160.1; AT4G05160.1; AT4G05160.
DR GeneID; 825864; -.
DR Gramene; AT4G05160.1; AT4G05160.1; AT4G05160.
DR KEGG; ath:AT4G05160; -.
DR Araport; AT4G05160; -.
DR TAIR; locus:2115673; AT4G05160.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q9M0X9; -.
DR OMA; FAIPSMG; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q9M0X9; -.
DR BioCyc; ARA:AT4G05160-MON; -.
DR SABIO-RK; Q9M0X9; -.
DR PRO; PR:Q9M0X9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0X9; baseline and differential.
DR Genevisible; Q9M0X9; AT.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IDA:TAIR.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IDA:TAIR.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
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; Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Oxylipin biosynthesis; Peroxisome; Reference proteome.
FT CHAIN 1..544
FT /note="4-coumarate--CoA ligase-like 7"
FT /id="PRO_0000299180"
FT REGION 269..338
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 339..403
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT MOTIF 542..544
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 198..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 316..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 338..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
SQ SEQUENCE 544 AA; 59850 MW; B2422848E70D2909 CRC64;
MEKSGYGRDG IYRSLRPTLV LPKDPNTSLV SFLFRNSSSY PSKLAIADSD TGDSLTFSQL
KSAVARLAHG FHRLGIRKND VVLIFAPNSY QFPLCFLAVT AIGGVFTTAN PLYTVNEVSK
QIKDSNPKII ISVNQLFDKI KGFDLPVVLL GSKDTVEIPP GSNSKILSFD NVMELSEPVS
EYPFVEIKQS DTAALLYSSG TTGTSKGVEL THGNFIAASL MVTMDQDLMG EYHGVFLCFL
PMFHVFGLAV ITYSQLQRGN ALVSMARFEL ELVLKNIEKF RVTHLWVVPP VFLALSKQSI
VKKFDLSSLK YIGSGAAPLG KDLMEECGRN IPNVLLMQGY GMTETCGIVS VEDPRLGKRN
SGSAGMLAPG VEAQIVSVET GKSQPPNQQG EIWVRGPNMM KGYLNNPQAT KETIDKKSWV
HTGDLGYFNE DGNLYVVDRI KELIKYKGFQ VAPAELEGLL VSHPDILDAV VIPFPDEEAG
EVPIAFVVRS PNSSITEQDI QKFIAKQVAP YKRLRRVSFI SLVPKSAAGK ILRRELVQQV
RSKM
