ID   KAP1_ARATH              Reviewed;         276 AA.
AC   Q43295;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Adenylyl-sulfate kinase 1, chloroplastic;
DE            EC=2.7.1.25;
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE            Short=APS kinase;
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE   Flags: Precursor;
GN   Name=AKN1; OrderedLocusNames=At2g14750; ORFNames=F26C24.11, T6B13.1;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   MEDLINE=94325358; PubMed=8049272; DOI=10.1016/0167-4781(94)90203-8;
RA   Arz H.E., Gisselmann G., Schiffmann S., Schwenn J.-D.;
RT   "A cDNA for adenylyl sulphate (APS)-kinase from Arabidopsis
RT   thaliana.";
RL   Biochim. Biophys. Acta 1218:447-452(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94345022; PubMed=8066145; DOI=10.1104/pp.105.2.771;
RA   Jain A., Leustek T.;
RT   "A cDNA clone for 5'-adenylylphosphosulfate kinase from Arabidopsis
RT   thaliana.";
RL   Plant Physiol. 105:771-772(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9636674; DOI=10.1006/bbrc.1998.8751;
RA   Lee S., Leustek T.;
RT   "APS kinase from Arabidopsis thaliana: genomic organization,
RT   expression, and kinetic analysis of the recombinant enzyme.";
RL   Biochem. Biophys. Res. Commun. 247:171-175(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC   -!- CATALYTIC ACTIVITY: ATP + adenylyl sulfate = ADP + 3'-
CC       phosphoadenylyl sulfate.
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
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DR   EMBL; X75782; CAA53426.1; -; mRNA.
DR   EMBL; U05238; AAC50035.1; -; mRNA.
DR   EMBL; U59759; AAC50034.1; -; Genomic_DNA.
DR   EMBL; AC004705; AAC24182.1; -; Genomic_DNA.
DR   EMBL; AY054287; AAL06946.1; -; mRNA.
DR   EMBL; AY132010; AAM91043.1; -; mRNA.
DR   IPI; IPI00516504; -.
DR   PIR; S47640; S47640.
DR   RefSeq; NP_179082.1; -.
DR   UniGene; At.10821; -.
DR   HSSP; Q12657; 1M7G.
DR   PRIDE; Q43295; -.
DR   GeneID; 815963; -.
DR   GenomeReviews; CT485783_GR; AT2G14750.
DR   KEGG; ath:AT2G14750; -.
DR   NMPDR; fig|3702.1.peg.8486; -.
DR   TAIR; At2g14750; -.
DR   OMA; Q43295; DAGIICI.
DR   BRENDA; 2.7.1.25; 302.
DR   ArrayExpress; Q43295; -.
DR   GermOnline; AT2G14750; Arabidopsis thaliana.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IDA:TAIR.
DR   GO; GO:0010439; P:regulation of glucosinolate biosynthetic pr...; IGI:TAIR.
DR   GO; GO:0000103; P:sulfate assimilation; IGI:TAIR.
DR   InterPro; IPR002891; APS_kinase_C.
DR   Pfam; PF01583; APS_kinase; 1.
DR   ProDom; PD002350; APS_kinase; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; ATP-binding; Chloroplast; Complete proteome;
KW   Cysteine biosynthesis; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Plastid; Transferase; Transit peptide.
FT   TRANSIT       1     37       Chloroplast (Potential).
FT   CHAIN        38    276       Adenylyl-sulfate kinase 1, chloroplastic.
FT                                /FTId=PRO_0000006635.
FT   NP_BIND     108    115       ATP (Potential).
FT   ACT_SITE    182    182       Phosphoserine intermediate (By
FT                                similarity).
SQ   SEQUENCE   276 AA;  29787 MW;  CB698643AA09D811 CRC64;
     MIAAGAKSLL GLSMASPKGI FDSNSMSNSR SVVVVRACVS MDGSQTLSHN KNGSIPEVKS
     INGHTGQKQG PLSTVGNSTN IKWHECSVEK VDRQRLLDQK GCVIWVTGLS GSGKSTLACA
     LNQMLYQKGK LCYILDGDNV RHGLNRDLSF KAEDRAENIR RVGEVAKLFA DAGIICIASL
     ISPYRTDRDA CRSLLPEGDF VEVFMDVPLS VCEARDPKGL YKLARAGKIK GFTGIDDPYE
     PPLNCEISLG REGGTSPIEM AEKVVGYLDN KGYLQA
//