ID C9P271_VIBME Unreviewed; 205 AA.
AC C9P271;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 ORFNames=VIB_000574 {ECO:0000313|EMBL:EEX38200.1};
OS Vibrio metschnikovii CIP 69.14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX38200.1, ECO:0000313|Proteomes:UP000005604};
RN [1] {ECO:0000313|EMBL:EEX38200.1, ECO:0000313|Proteomes:UP000005604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX38200.1,
RC ECO:0000313|Proteomes:UP000005604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; ACZO01000005; EEX38200.1; -; Genomic_DNA.
DR RefSeq; WP_004394558.1; NZ_ACZO01000005.1.
DR AlphaFoldDB; C9P271; -.
DR STRING; 675813.VIB_000574; -.
DR GeneID; 79888760; -.
DR eggNOG; COG0529; Bacteria.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000005604; Unassembled WGS sequence.
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:UP000005604};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00065}.
FT ACT_SITE 113
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00065"
SQ SEQUENCE 205 AA; 23019 MW; 9C867841517B2A30 CRC64;
MHTIDNVTEP TIVWHEHHVD KAHRARLKQQ RPAVLWFTGL SGAGKSTIAG ALEQRLAELG
YHTYLLDGDN VRHGLCADLG FSEQDRRENI RRIGELAKLM ADAGLIVLTA FISPHRAERQ
RVRALMPEGE FLEVFVNTHL AVCEQRDPKG LYKKARAGEI PQFTGIDSVY EAPLEAEIDL
PAGEEPVEVL VERCIMALQQ RGIIR
//
