CYSC_SYNY3
ID CYSC_SYNY3 Reviewed; 177 AA.
AC P72940;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
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=slr0676;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-8.
RX PubMed=9298645; DOI=10.1002/elps.1150180806;
RA Sazuka T., Ohara O.;
RT "Towards a proteome project of cyanobacterium Synechocystis sp. strain
RT PCC6803: linking 130 protein spots with their respective genes.";
RL Electrophoresis 18:1252-1258(1997).
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; BA000022; BAA16957.1; -; Genomic_DNA.
DR PIR; S74917; S74917.
DR PDB; 5CB6; X-ray; 2.79 A; A/B/C/D/E/F=1-177.
DR PDB; 5CB8; X-ray; 1.88 A; A/B=1-177.
DR PDBsum; 5CB6; -.
DR PDBsum; 5CB8; -.
DR AlphaFoldDB; P72940; -.
DR SMR; P72940; -.
DR IntAct; P72940; 2.
DR STRING; 1148.1652032; -.
DR PaxDb; P72940; -.
DR EnsemblBacteria; BAA16957; BAA16957; BAA16957.
DR KEGG; syn:slr0676; -.
DR eggNOG; COG0529; Bacteria.
DR InParanoid; P72940; -.
DR OMA; GVTIWFT; -.
DR PhylomeDB; P72940; -.
DR BRENDA; 2.7.1.25; 382.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000001425; 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:0004781; F:sulfate adenylyltransferase (ATP) activity; IBA:GO_Central.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IBA:GO_Central.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); 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 3D-structure; ATP-binding; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..177
FT /note="Probable adenylyl-sulfate kinase"
FT /id="PRO_0000105922"
FT ACT_SITE 86
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:5CB8"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:5CB8"
FT TURN 45..51
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 56..74
FT /evidence="ECO:0007829|PDB:5CB8"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5CB8"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:5CB8"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:5CB8"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5CB6"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:5CB8"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5CB8"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5CB8"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:5CB8"
SQ SEQUENCE 177 AA; 19674 MW; E24D5B5452FCD7D8 CRC64;
MQQRGVTIWL TGLSGAGKTT ITHALEKKLR DSGYRLEVLD GDVVRTNLTK GLGFSKEDRD
TNIRRIGFVS HLLTRNGVIV LVSAISPYAA IRQEVKHTIG DFLEVFVNAP LAVCEERDVK
GLYAKARSGE IKGFTGIDDP YEPPTNPDVE CRTDLEELDE SVGKIWQKLV DLKYIEG
