CYSC_SHEB5
ID CYSC_SHEB5 Reviewed; 205 AA.
AC A3D819;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Adenylyl-sulfate kinase {ECO:0000255|HAMAP-Rule:MF_00065};
DE EC=2.7.1.25 {ECO:0000255|HAMAP-Rule:MF_00065};
DE AltName: Full=APS kinase {ECO:0000255|HAMAP-Rule:MF_00065};
DE AltName: Full=ATP adenosine-5'-phosphosulfate 3'-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00065};
DE AltName: Full=Adenosine-5'-phosphosulfate kinase {ECO:0000255|HAMAP-Rule:MF_00065};
GN Name=cysC {ECO:0000255|HAMAP-Rule:MF_00065}; OrderedLocusNames=Sbal_3405;
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC {ECO:0000255|HAMAP-Rule:MF_00065}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00065};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 2/3. {ECO:0000255|HAMAP-Rule:MF_00065}.
CC -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00065}.
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DR EMBL; CP000563; ABN62882.1; -; Genomic_DNA.
DR RefSeq; WP_011847639.1; NC_009052.1.
DR AlphaFoldDB; A3D819; -.
DR SMR; A3D819; -.
DR STRING; 325240.Sbal_3405; -.
DR EnsemblBacteria; ABN62882; ABN62882; Sbal_3405.
DR KEGG; sbl:Sbal_3405; -.
DR HOGENOM; CLU_046932_1_0_6; -.
DR OMA; GVTIWFT; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000001557; 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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
FT CHAIN 1..205
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_1000009022"
FT ACT_SITE 105
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
SQ SEQUENCE 205 AA; 22364 MW; 9C39760CE68B0B11 CRC64;
MTNILWHQHP VDQAARAEQK GQNPVLLWFT GLSGAGKSTL AGALERALFE AGFHTYLLDG
DNVRHGLCKD LGFTVEDRDE NLRRVGEVAK LMVDAGLVVL SAFISPTREE RDSIRARFPT
SQFIEVHVST PLSVCEQRDP KGLYVKARSG EISNFTGISS PYEAPLAAEL TIDTSKGDLA
TQVRALIDYL TAINVINADK AKALA
