(data stored in ACNUC5340 zone)

SWISSPROT: 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   11-DEC-2019, entry version 69.
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}.
DR   EMBL; CP000828; ABW25463.1; -; Genomic_DNA.
DR   RefSeq; WP_012161073.1; NC_009925.1.
DR   SMR; B0CAX3; -.
DR   STRING; 329726.AM1_0406; -.
DR   PRIDE; B0CAX3; -.
DR   EnsemblBacteria; ABW25463; ABW25463; AM1_0406.
DR   KEGG; amr:AM1_0406; -.
DR   eggNOG; ENOG4107T1U; Bacteria.
DR   eggNOG; COG0529; LUCA.
DR   HOGENOM; HOG000228204; -.
DR   KO; K00860; -.
DR   OMA; IVWHQHS; -.
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:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd02027; APSK; 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;
DR   PRODOM; B0CAX3.
DR   SWISS-2DPAGE; B0CAX3.
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   NP_BIND         35..42
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00065"
FT   ACT_SITE        109
FT                   /note="Phosphoserine intermediate"
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
//

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