KAPS_CATRO
ID KAPS_CATRO Reviewed; 312 AA.
AC O49204;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Adenylyl-sulfate kinase, chloroplastic;
DE EC=2.7.1.25;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
DE Short=APS kinase;
DE Flags: Precursor;
GN Name=AKN;
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Schiffmann S., Schwenn J.-D.;
RT "Isolation of cDNA clones encoding adenosine-5'-phosphosulfate-kinase (EC
RT 2.7.1.25) from Catharanthus roseus and an isoform (akn2) from
RT Arabidopsis.";
RL (er) Plant Gene Register PGR98-116(1998).
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
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 -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; AF044285; AAC31145.1; -; mRNA.
DR PIR; T08076; T08076.
DR AlphaFoldDB; O49204; -.
DR SMR; O49204; -.
DR UniPathway; UPA00140; UER00205.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Amino-acid biosynthesis; ATP-binding; Chloroplast; Cysteine biosynthesis;
KW Kinase; Nucleotide-binding; Phosphoprotein; Plastid; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..312
FT /note="Adenylyl-sulfate kinase, chloroplastic"
FT /id="PRO_0000006637"
FT ACT_SITE 216
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 142..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 312 AA; 33657 MW; 16BBD11FB4B1FE27 CRC64;
MIGSVKRPVV SCVLPEFDFT ESTGLGKKSS SVKLPVNFGA FGSGGGEVKL GFLAPIKATE
GSKTSSFQVN GKVDNFRHLQ PSDCNSNSDS SLNNCNGFPG KKILQTTTVG NSTNILWHKC
AVEKSERQEP LQQRGCVIWI TGLSGSGKST LACALSRGLH AKGKLTYILD GDNVRHGLNS
DLSFKAEDRA ENIRRIGEVA KLFADAGVIC IASLISPYRK PPDACRSLLP EGDFIEVFMD
VPLKVCEARD PKGLYKLARA GKIKGFTGID DPYEPPLKSE IVLHQKLGMC DSPCDLADIV
ISYLEENGYL KA