GenomeNet

Database: UniProt
Entry: G0JNQ9_9PROT
LinkDB: G0JNQ9_9PROT
Original site: G0JNQ9_9PROT 
ID   G0JNQ9_9PROT            Unreviewed;       557 AA.
AC   G0JNQ9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE            EC=2.7.1.25 {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=APS kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00065};
DE   AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
GN   Name=cysC {ECO:0000256|HAMAP-Rule:MF_00065};
GN   ORFNames=Acife_2287 {ECO:0000313|EMBL:AEM48398.1};
OS   Acidithiobacillus ferrivorans SS3.
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=743299 {ECO:0000313|EMBL:AEM48398.1, ECO:0000313|Proteomes:UP000009220};
RN   [1] {ECO:0000313|EMBL:AEM48398.1, ECO:0000313|Proteomes:UP000009220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS3 {ECO:0000313|EMBL:AEM48398.1,
RC   ECO:0000313|Proteomes:UP000009220};
RX   PubMed=21705598; DOI=10.1128/JB.05373-11;
RA   Liljeqvist M., Valdes J., Holmes D.S., Dopson M.;
RT   "Draft genome of the psychrotolerant acidophile Acidithiobacillus
RT   ferrivorans SS3.";
RL   J. Bacteriol. 193:4304-4305(2011).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000262};
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         Evidence={ECO:0000256|ARBA:ARBA00001823, ECO:0000256|HAMAP-
CC         Rule:MF_00065};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00065}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002985; AEM48398.1; -; Genomic_DNA.
DR   RefSeq; WP_014029649.1; NC_015942.1.
DR   AlphaFoldDB; G0JNQ9; -.
DR   STRING; 743299.Acife_2287; -.
DR   KEGG; afi:Acife_2287; -.
DR   eggNOG; COG0529; Bacteria.
DR   eggNOG; COG2046; Bacteria.
DR   HOGENOM; CLU_022950_0_0_6; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000009220; 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; IEA:UniProtKB-EC.
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; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   InterPro; IPR002650; Sulphate_adenylyltransferase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   NCBIfam; TIGR00339; sopT; 1.
DR   PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00065};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065, ECO:0000313|EMBL:AEM48398.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00065};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:AEM48398.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009220};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   DOMAIN          7..132
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          151..360
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
FT   ACT_SITE        451
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         376..383
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   557 AA;  60056 MW;  B43EFB0AC50D708E CRC64;
     MPTSPIHVLT ARQRCDLELL LTGAFAPLEG YLDAADWQSV LQDMRLSNGA LWPIPVVLDV
     SEALGQSLAA GDTLRLERSD GTPLGSVAVS ACYHPDKLLE AAAVYGTTDP SHPGVAELLA
     RGTYYVAGRV SAWDADTLTR AAAVEFPPEY QTPAMLQQHW SGAHPVVAFQ TRNPLHHAHI
     AVTQAGLEQA GAGARLLLHP AIGPTKPGDV EASYRMRVYR AVLSHYPQAT ALLSPLPLAM
     RMAGPREALW HALIRRNYGA THFIIGRGHA DPGTAAGGLF YPAFAAQELF ARHASEMGIT
     GIFLPEYAYS QTRRRYVPME EANGEALAGI SGTELRRRLA SREDIPEWFS PPEVIQILRQ
     AYRGADRRGL VIWFTGLSAS GKSTLAGMLA RTLEAGDERA VTLLDGDVVR RFLSKGLSFS
     RADRDENIRR IGFVASLVAR HGGIAVVAAI SPYRQARADA RRLVEEAGGL FIEVHVATPL
     EVCAERDPKG LYAKAMRGEI TGFTGVDDPY EVPEHAECVL GASLQKPPVA LATLMGVLRQ
     LGAVTAKPTV IAARKEA
//
DBGET integrated database retrieval system