ID   CYSC_AERPE              Reviewed;         183 AA.
AC   Q9YCR6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 114.
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=APE_1195.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
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; BA000002; BAA80181.2; -; Genomic_DNA.
DR   PIR; G72590; G72590.
DR   PDB; 2YVU; X-ray; 2.10 A; A/B=2-183.
DR   PDBsum; 2YVU; -.
DR   AlphaFoldDB; Q9YCR6; -.
DR   SMR; Q9YCR6; -.
DR   STRING; 272557.APE_1195.1; -.
DR   EnsemblBacteria; BAA80181; BAA80181; APE_1195.1.
DR   KEGG; ape:APE_1195.1; -.
DR   PATRIC; fig|272557.25.peg.823; -.
DR   eggNOG; arCOG01040; Archaea.
DR   UniPathway; UPA00140; UER00205.
DR   EvolutionaryTrace; Q9YCR6; -.
DR   Proteomes; UP000002518; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..183
FT                   /note="Probable adenylyl-sulfate kinase"
FT                   /id="PRO_0000105928"
FT   ACT_SITE        91
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         17..24
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           23..36
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           46..50
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   TURN            51..56
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           61..79
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           94..106
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   STRAND          111..117
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           120..126
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           144..147
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   STRAND          157..161
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:2YVU"
FT   HELIX           167..181
FT                   /evidence="ECO:0007829|PDB:2YVU"
SQ   SEQUENCE   183 AA;  20783 MW;  FE883B88FC435093 CRC64;
     MTTYKCIEKG IVVWLTGLPG SGKTTIATRL ADLLQKEGYR VEVLDGDWAR TTVSEGAGFT
     REERLRHLKR IAWIARLLAR NGVIVICSFV SPYKQARNMV RRIVEEEGIP FLEIYVKASL
     EEVIRRDPKG LYKKALKGEL ENFTGITDPY EPPENPQLVL DTESNTIEHN VSYLYSLVKA
     VIE