CYSC_ACAM1
ID CYSC_ACAM1 Reviewed; 205 AA.
AC B0CAX3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=AM1_0406;
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC Acaryochloris.
OX NCBI_TaxID=329726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017;
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW25463.1; -; Genomic_DNA.
DR RefSeq; WP_012161073.1; NC_009925.1.
DR AlphaFoldDB; B0CAX3; -.
DR SMR; B0CAX3; -.
DR STRING; 329726.AM1_0406; -.
DR EnsemblBacteria; ABW25463; ABW25463; AM1_0406.
DR KEGG; amr:AM1_0406; -.
DR eggNOG; COG0529; Bacteria.
DR HOGENOM; CLU_046932_1_0_3; -.
DR OMA; GVTIWFT; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00205.
DR Proteomes; UP000000268; 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;
KW Reference proteome; Transferase.
FT CHAIN 1..205
FT /note="Adenylyl-sulfate kinase"
FT /id="PRO_1000202404"
FT ACT_SITE 109
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT BINDING 35..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
SQ SEQUENCE 205 AA; 22861 MW; 564E341EE163DC7D CRC64;
MIMKSSNVVW HKSTVTRQNR QEQNGHLSTI LWFTGLSGAG KSTLAHTVED ALSKMNCRTF
VIDGDNIRHG LCADLGFSSE DRVENIRRIG EVAKLFTEAG IIVLSAFISP FRADRDRVRE
LVPEGDFIEI YCQASLEVCE ERDVKGLYKK ARSGEIPNFT GISSPYEPPE EPEIIVKTGE
DSLEVCAQQV IEFLQERGIV QPTSA
