UniProt: D5V0B9

Database: UniProt
Entry: D5V0B9_ARCNC

LinkDB:  D5V0B9_ARCNC 
Original site:  D5V0B9_ARCNC

All links

Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (3)   
   InterPro (2)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (12)   

Download RDF

ID   D5V0B9_ARCNC            Unreviewed;       220 AA.
AC   D5V0B9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|ARBA:ARBA00012121, 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=Arnit_2077 {ECO:0000313|EMBL:ADG93731.1};
OS   Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS   7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Arcobacteraceae; Arcobacter.
OX   NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG93731.1, ECO:0000313|Proteomes:UP000000939};
RN   [1] {ECO:0000313|EMBL:ADG93731.1, ECO:0000313|Proteomes:UP000000939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC   {ECO:0000313|Proteomes:UP000000939};
RX   PubMed=21304714; DOI=10.4056/sigs.912121;
RA   Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA   Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL   Stand. Genomic Sci. 2:300-308(2010).
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}.
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; CP001999; ADG93731.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5V0B9; -.
DR   STRING; 572480.Arnit_2077; -.
DR   KEGG; ant:Arnit_2077; -.
DR   eggNOG; COG0529; Bacteria.
DR   HOGENOM; CLU_046932_1_0_7; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000000939; 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:UP000000939};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00065}.
FT   ACT_SITE        124
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT   BINDING         50..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ   SEQUENCE   220 AA;  25521 MW;  B5DEB2908E16E526 CRC64;
     MKNSEQKIKP LKQLESELMT NNIIWYDSHI TKEDRVKQLS QKPCILWFTG LSGSGKSTIA
     NVLEVKLYKM GIKTYLLDGD NIRHGLNRDL GFSKKDRTEN IRRISEVAKL FVDSGSIVLT
     AFISPFQRDR ELARKLVKED EFIEIFIDTS LEICEQRDPK GLYKKVKEGK IKDFTGIDSP
     YEVPINSEIH LKTNELTIEQ ASEEVISYLK RFNYLKDLKE
//

DBGET integrated database retrieval system