CYSC_PYRAB
ID CYSC_PYRAB Reviewed; 174 AA.
AC P56858; G8ZKF4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable adenylyl-sulfate kinase;
DE EC=2.7.1.25;
DE AltName: Full=APS kinase;
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenosine-5'-phosphosulfate kinase;
GN Name=cysC; OrderedLocusNames=PYRAB11720; ORFNames=PAB0781;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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 -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000305}.
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DR EMBL; AJ248286; CAB50083.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70597.1; -; Genomic_DNA.
DR PIR; F75097; F75097.
DR RefSeq; WP_010868289.1; NC_000868.1.
DR AlphaFoldDB; P56858; -.
DR SMR; P56858; -.
DR STRING; 272844.PAB0781; -.
DR PRIDE; P56858; -.
DR EnsemblBacteria; CAB50083; CAB50083; PAB0781.
DR GeneID; 1496543; -.
DR KEGG; pab:PAB0781; -.
DR PATRIC; fig|272844.11.peg.1243; -.
DR eggNOG; arCOG01040; Archaea.
DR HOGENOM; CLU_046932_2_3_2; -.
DR OMA; GVTIWFT; -.
DR OrthoDB; 89532at2157; -.
DR PhylomeDB; P56858; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN 1..174
FT /note="Probable adenylyl-sulfate kinase"
FT /id="PRO_0000105930"
FT ACT_SITE 84
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 174 AA; 19829 MW; 2BE71A04D4A46897 CRC64;
MEGFTIWLTG PSGAGKTTLA VKLAKKLREM GYKVEILDGD TIRKTLYPNL GFSKEAREMH
NRIVIYMAKL LTRNGVIAIV SLISPYKRIR EYARKEIGRF MEVYVYAPLE VRIKRDPKGL
YAKAIRGEIR GLTGYDGVYE EPENPEVKVD SSRMTPDEEA ELVIRKAKEL GYLP
