UniProt: A4SXV1

Database: UniProt
Entry: A4SXV1_POLAQ

LinkDB:  A4SXV1_POLAQ 
Original site:  A4SXV1_POLAQ

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   A4SXV1_POLAQ            Unreviewed;       195 AA.
AC   A4SXV1;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00018163, ECO:0000256|HAMAP-Rule:MF_00065};
DE            EC=2.7.1.25 {ECO:0000256|ARBA:ARBA00012121, 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   OrderedLocusNames=Pnuc_1099 {ECO:0000313|EMBL:ABP34315.1};
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP34315.1, ECO:0000313|Proteomes:UP000000231};
RN   [1] {ECO:0000313|EMBL:ABP34315.1, ECO:0000313|Proteomes:UP000000231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1
RC   {ECO:0000313|Proteomes:UP000000231};
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA   Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA   Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|ARBA:ARBA00002632, ECO:0000256|HAMAP-Rule:MF_00065,
CC       ECO:0000256|RuleBase:RU004347}.
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, ECO:0000256|RuleBase:RU004347};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 2/3. {ECO:0000256|ARBA:ARBA00004806, ECO:0000256|HAMAP-
CC       Rule:MF_00065, ECO:0000256|RuleBase:RU004347}.
CC   -!- SIMILARITY: Belongs to the APS kinase family.
CC       {ECO:0000256|ARBA:ARBA00007008, ECO:0000256|HAMAP-Rule:MF_00065,
CC       ECO:0000256|RuleBase:RU004347}.
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DR   EMBL; CP000655; ABP34315.1; -; Genomic_DNA.
DR   RefSeq; WP_011902940.1; NC_009379.1.
DR   AlphaFoldDB; A4SXV1; -.
DR   GeneID; 31481476; -.
DR   KEGG; pnu:Pnuc_1099; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_0_4; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000000231; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00455; apsK; 1.
DR   PANTHER; PTHR11055; BIFUNCTIONAL 3'-PHOSPHOADENOSINE 5'-PHOSPHOSULFATE SYNTHASE; 1.
DR   PANTHER; PTHR11055:SF1; PAPS SYNTHETASE, ISOFORM D; 1.
DR   Pfam; PF01583; APS_kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:0000256|RuleBase:RU004347};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00065}; Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000231};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   ACT_SITE        103
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   195 AA;  21588 MW;  80AE45E3B6E8BDCC CRC64;
     MKINQQFDIT KGDRALANGH RPLCFWFTGL SGSGKSTIAN AFEKKLHANG IKTYVLDGDN
     LRQGLNSSLG FDLESRIENI RRTAEVAKLM VDAGLVVLVT LISPLKIGRD SARALFGLDE
     FVEVYINTPL DICEARDPKG IYKKARQGKI LDFTGIDSPY DVPINPDVML DTSKNNLDEI
     VITLLNLTDF KLTKS
//

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