4CLL5_ARATH
ID 4CLL5_ARATH Reviewed; 546 AA.
AC Q84P21; Q9C5H2; Q9LMV8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=4-coumarate--CoA ligase-like 5 {ECO:0000303|PubMed:12805634};
DE EC=6.2.1.- {ECO:0000305|PubMed:16963437, ECO:0000305|PubMed:18267944};
DE AltName: Full=4-coumarate--CoA ligase isoform 9;
DE Short=At4CL9;
DE AltName: Full=Peroxisomal OPC-8:0-CoA ligase 1 {ECO:0000303|PubMed:18267944, ECO:0000303|PubMed:19704801};
GN Name=4CLL5 {ECO:0000303|PubMed:12805634};
GN Synonyms=OPCL1 {ECO:0000303|PubMed:18267944, ECO:0000303|PubMed:19704801};
GN OrderedLocusNames=At1g20510 {ECO:0000312|Araport:AT1G20510};
GN ORFNames=F5M15.17 {ECO:0000312|EMBL:AAF79611.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16963437; DOI=10.1074/jbc.m607854200;
RA Koo A.J.K., Chung H.S., Kobayashi Y., Howe G.A.;
RT "Identification of a peroxisomal acyl-activating enzyme involved in the
RT biosynthesis of jasmonic acid in Arabidopsis.";
RL J. Biol. Chem. 281:33511-33520(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP REVIEW.
RX PubMed=19704801; DOI=10.4161/psb.2.1.3612;
RA Koo A.J., Howe G.A.;
RT "Role of peroxisomal beta-oxidation in the production of plant signaling
RT compounds.";
RL Plant Signal. Behav. 2:20-22(2007).
RN [9]
RP FUNCTION, MUTAGENESIS OF LYS-530, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY,
RP INDUCTION BY WOUNDING; JASMONIC ACID AND PSEUDOMONAS SYRINGAE,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
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 (PubMed:16963437,
CC PubMed:18267944). Converts 12-oxo-phytodienoic acid (OPDA) and 3-oxo-2-
CC (2'-pentenyl)-cyclopentane-1-octanoic acid (OPC-8:0) into OPDA-CoA and
CC OPC-8:0-CoA, respectively (PubMed:16963437, PubMed:18267944).
CC {ECO:0000269|PubMed:16963437, 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:16963437, ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000269|PubMed:16963437, ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + OPC-8 = AMP + diphosphate + OPC8-CoA;
CC Xref=Rhea:RHEA:54888, ChEBI:CHEBI:15720, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:138396,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:16963437,
CC ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54889;
CC Evidence={ECO:0000269|PubMed:16963437, ECO:0000269|PubMed:18267944};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(10Z,15Z)-12-oxophytodienoate + ATP + CoA = (10Z,15Z)-12-
CC oxophytodienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54896,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57411, ChEBI:CHEBI:138398, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:16963437, ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54897;
CC Evidence={ECO:0000269|PubMed:16963437, 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:16963437, ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC Evidence={ECO:0000269|PubMed:16963437, ECO:0000269|PubMed:18267944};
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:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000269|PubMed:18267944};
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:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
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 + 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dinor-OPDA = AMP + dinor-OPDA-CoA + diphosphate;
CC Xref=Rhea:RHEA:54960, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:138432, ChEBI:CHEBI:138433,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18267944};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54961;
CC Evidence={ECO:0000269|PubMed:18267944};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=24 uM for OPDA {ECO:0000269|PubMed:16963437};
CC KM=47 uM for OPC-8:0 {ECO:0000269|PubMed:16963437};
CC KM=36 uM for tetradecanoic acid {ECO:0000269|PubMed:18267944};
CC KM=27 uM for OPDA {ECO:0000269|PubMed:18267944};
CC KM=76 uM for dnOPDA {ECO:0000269|PubMed:18267944};
CC KM=19 uM for OPC-8:0 {ECO:0000269|PubMed:18267944};
CC KM=94 uM for OPC-6:0 {ECO:0000269|PubMed:18267944};
CC Note=kcat is 0.96 sec(-1) with tetradecanoic acid as substrate
CC (PubMed:18267944). kcat is 1.56 sec(-1) with OPDA as substrate
CC (PubMed:18267944). kcat is 1.78 sec(-1) with dnOPDA as substrate
CC (PubMed:18267944). kcat is 1.27 sec(-1) with OPC-8:0 as substrate
CC (PubMed:18267944). kcat is 1.49 sec(-1) with OPC-6:0 as substrate
CC (PubMed:18267944). {ECO:0000269|PubMed:18267944};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16963437,
CC ECO:0000269|PubMed:18267944}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q84P21-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in seedlings, cotyledons,
CC leaves, hypocotyls and roots. {ECO:0000269|PubMed:18267944}.
CC -!- DEVELOPMENTAL STAGE: In seedlings, present at low levels in the
CC vascular system of cotyledons, leaves, hypocotyls, roots and hydathodes
CC (PubMed:18267944). In roots, accumulates mostly in the zone of cell
CC division proximal to the root tip, in the vascular system and
CC primordial cells of lateral roots and, at low levels, in some
CC superficial cells of the elongation zone (PubMed:18267944). In mature
CC plants, observed in the vasculature of leaves, stems, and roots, with a
CC progressive expression increase in mesophyll cells during aging
CC (PubMed:18267944). Weakly detected in the young parts of the bolting
CC stem (PubMed:18267944). {ECO:0000269|PubMed:18267944}.
CC -!- INDUCTION: By wounding or by jasmonic acid (MeJA) treatment
CC (PubMed:16963437, PubMed:18267944). Accumulates upon infection by
CC incompatible pathogens (e.g. Pseudomonas syringae pv. tomato (Pst)
CC carrying avrRpm1) (PubMed:18267944). {ECO:0000269|PubMed:16963437,
CC ECO:0000269|PubMed:18267944}.
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 (PubMed:18267944).
CC Reduced jasmonic acid (JA) accumulation after wounding
CC (PubMed:18267944). {ECO:0000269|PubMed:18267944}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY250838; AAP03021.1; -; mRNA.
DR EMBL; EF014466; ABJ98946.1; -; mRNA.
DR EMBL; AC027665; AAF79611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29980.1; -; Genomic_DNA.
DR EMBL; AF360250; AAK25960.1; -; mRNA.
DR EMBL; AY040047; AAK64105.1; -; mRNA.
DR RefSeq; NP_564115.1; NM_101901.4. [Q84P21-1]
DR AlphaFoldDB; Q84P21; -.
DR SMR; Q84P21; -.
DR STRING; 3702.AT1G20510.1; -.
DR SwissLipids; SLP:000001781; -.
DR PaxDb; Q84P21; -.
DR PRIDE; Q84P21; -.
DR ProteomicsDB; 244550; -. [Q84P21-1]
DR EnsemblPlants; AT1G20510.1; AT1G20510.1; AT1G20510. [Q84P21-1]
DR GeneID; 838639; -.
DR Gramene; AT1G20510.1; AT1G20510.1; AT1G20510. [Q84P21-1]
DR KEGG; ath:AT1G20510; -.
DR Araport; AT1G20510; -.
DR TAIR; locus:2034392; AT1G20510.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_2_1; -.
DR InParanoid; Q84P21; -.
DR OMA; WLMQRAF; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q84P21; -.
DR BRENDA; 6.2.1.B3; 399.
DR SABIO-RK; Q84P21; -.
DR PRO; PR:Q84P21; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84P21; baseline and differential.
DR Genevisible; Q84P21; AT.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IDA:UniProtKB.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0009695; P:jasmonic acid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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 Alternative splicing; ATP-binding; Jasmonic acid signaling pathway; Ligase;
KW Nucleotide-binding; Peroxisome; Reference proteome.
FT CHAIN 1..546
FT /note="4-coumarate--CoA ligase-like 5"
FT /id="PRO_0000299178"
FT REGION 267..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 544..546
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 197..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT BINDING 242
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"
FT MUTAGEN 530
FT /note="K->N: Lossed enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18267944"
FT CONFLICT 247
FT /note="A -> T (in Ref. 1; AAP03021)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 546 AA; 59375 MW; 628BB0F1CD0AC9BE CRC64;
MASVNSRSGF CNSNSTFYSK RTPIPLPPNP SLDVTTFISS QAHRGRIAFI DASTGQNLTF
TELWRAVESV ADCLSEIGIR KGHVVLLLSP NSILFPVVCL SVMSLGAIIT TTNPLNTSNE
IAKQIKDSNP VLAFTTSQLL PKISAAAKKL PIVLMDEERV DSVGDVRRLV EMMKKEPSGN
RVKERVDQDD TATLLYSSGT TGMSKGVISS HRNLIAMVQT IVNRFGSDDG EQRFICTVPM
FHIYGLAAFA TGLLAYGSTI IVLSKFEMHE MMSAIGKYQA TSLPLVPPIL VAMVNGADQI
KAKYDLSSMH TVLCGGAPLS KEVTEGFAEK YPTVKILQGY GLTESTGIGA STDTVEESRR
YGTAGKLSAS MEGRIVDPVT GQILGPKQTG ELWLKGPSIM KGYFSNEEAT SSTLDSEGWL
RTGDLCYIDE DGFIFVVDRL KELIKYKGYQ VAPAELEALL LTHPEITDAA VIPFPDKEVG
QFPMAYVVRK TGSSLSEKTI MEFVAKQVAP YKRIRKVAFV SSIPKNPSGK ILRKDLIKIA
TSNSKL
