CYSC_AERPE
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