APK4_ARATH
ID APK4_ARATH Reviewed; 310 AA.
AC Q84JF0; Q8LF64; Q9FJX1;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Adenylyl-sulfate kinase 4, chloroplastic;
DE EC=2.7.1.25 {ECO:0000305|PubMed:19304933};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase 4;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase 4 {ECO:0000303|PubMed:19304933};
DE Short=APS kinase 4 {ECO:0000303|PubMed:19304933};
DE Flags: Precursor;
GN Name=APK4; OrderedLocusNames=At5g67520; ORFNames=K9I9.8;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19304933; DOI=10.1105/tpc.109.065581;
RA Mugford S.G., Yoshimoto N., Reichelt M., Wirtz M., Hill L., Mugford S.T.,
RA Nakazato Y., Noji M., Takahashi H., Kramell R., Gigolashvili T.,
RA Fluegge U.I., Wasternack C., Gershenzon J., Hell R., Saito K., Kopriva S.;
RT "Disruption of adenosine-5'-phosphosulfate kinase in Arabidopsis reduces
RT levels of sulfated secondary metabolites.";
RL Plant Cell 21:910-927(2009).
RN [6]
RP FUNCTION.
RX PubMed=19903478; DOI=10.1016/j.febslet.2009.11.014;
RA Mugford S.G., Matthewman C.A., Hill L., Kopriva S.;
RT "Adenosine-5'-phosphosulfate kinase is essential for Arabidopsis
RT viability.";
RL FEBS Lett. 584:119-123(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of adenosine 5'-phosphosulfate
CC to 3'-phosphoadenylyl sulfate, which is the activated sulfate form for
CC sulfation reactions. Essential for plant reproduction and viability.
CC {ECO:0000269|PubMed:19304933, ECO:0000269|PubMed:19903478}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000305|PubMed:19304933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153;
CC Evidence={ECO:0000305|PubMed:19304933};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for adenosine 5'-phosphosulfate
CC {ECO:0000269|PubMed:19304933};
CC Vmax=12.7 mmol/min/mg enzyme with adenosine 5'-phosphosulfate as
CC substrate {ECO:0000269|PubMed:19304933};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- INTERACTION:
CC Q84JF0; Q9FFS3: WRKY24; NbExp=3; IntAct=EBI-25520113, EBI-4431481;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19304933}.
CC -!- TISSUE SPECIFICITY: Expressed in root vasculature, root tips, leaf
CC epidermal and guard cells, pollen grains and radicle of immature seeds.
CC {ECO:0000269|PubMed:19304933}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:19304933}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM61589.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB08460.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB013390; BAB08460.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98355.1; -; Genomic_DNA.
DR EMBL; BT003977; AAO42019.1; -; mRNA.
DR EMBL; BT005193; AAO50726.1; -; mRNA.
DR EMBL; AY085031; AAM61589.1; ALT_INIT; mRNA.
DR RefSeq; NP_569050.1; NM_126152.5.
DR AlphaFoldDB; Q84JF0; -.
DR SMR; Q84JF0; -.
DR BioGRID; 22130; 1.
DR IntAct; Q84JF0; 1.
DR STRING; 3702.AT5G67520.1; -.
DR PaxDb; Q84JF0; -.
DR PRIDE; Q84JF0; -.
DR ProteomicsDB; 244475; -.
DR EnsemblPlants; AT5G67520.1; AT5G67520.1; AT5G67520.
DR GeneID; 836888; -.
DR Gramene; AT5G67520.1; AT5G67520.1; AT5G67520.
DR KEGG; ath:AT5G67520; -.
DR Araport; AT5G67520; -.
DR TAIR; locus:2158626; AT5G67520.
DR eggNOG; KOG0635; Eukaryota.
DR HOGENOM; CLU_046932_0_2_1; -.
DR InParanoid; Q84JF0; -.
DR OMA; NGNIVWH; -.
DR OrthoDB; 1320063at2759; -.
DR PhylomeDB; Q84JF0; -.
DR BioCyc; ARA:AT5G67520-MON; -.
DR SABIO-RK; Q84JF0; -.
DR UniPathway; UPA00140; UER00205.
DR PRO; PR:Q84JF0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84JF0; baseline and differential.
DR Genevisible; Q84JF0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0009536; C:plastid; TAS:TAIR.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR CDD; cd02027; APSK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Chloroplast; Cysteine biosynthesis;
KW Disulfide bond; Kinase; Nucleotide-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..310
FT /note="Adenylyl-sulfate kinase 4, chloroplastic"
FT /id="PRO_0000424067"
FT ACT_SITE 190
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 116..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 158
FT /note="Participates in a stacking interaction with the
FT adenine ring of adenylyl-sulfate"
FT /evidence="ECO:0000250"
FT DISULFID 94
FT /note="Interchain (with C-127)"
FT /evidence="ECO:0000250"
FT DISULFID 127
FT /note="Interchain (with C-94)"
FT /evidence="ECO:0000250"
FT CONFLICT 107
FT /note="Q -> H (in Ref. 4; AAM61589)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="N -> D (in Ref. 4; AAM61589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 310 AA; 34065 MW; C1AC01A4242A0BDF CRC64;
MDVAAMARCV GRCYVSPAFG ESESHRLSER RFLKLSSSTN SDPAGSKSLK LRGKIHRRMS
YFRPIMAKDE SISSRSGETK QINGKQKNIV WHDCPVTKSD RQELIKQKGC VIWITGLSGS
GKSSLACALS RALHNRGKLS YILDGDNVRH GLNSDLSFEA DDRAENIRRV GEVAKLFADS
GIICIASLIS PYRIERAACR ALLPQGDFIE VFMDVPLHVC EARDPKGLYK RARAGKIKGF
TGVDDPYEAP LDCEIVIQNS RDKGLSSSSS SSSSPSSSSS SLCEMADIVV SYLDQNGYLK
KHSTKSRNCM
