(data stored in ACNUC7421 zone)

SWISSPROT: Q47SV4_THEFY

ID   Q47SV4_THEFY            Unreviewed;       493 AA.
AC   Q47SV4;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Adenylyl-sulfate kinase {ECO:0000256|HAMAP-Rule:MF_00065};
DE            EC=2.7.1.25 {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=Tfu_0425 {ECO:0000313|EMBL:AAZ54463.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54463.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Catalyzes the synthesis of activated sulfate.
CC       {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl
CC         sulfate + 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:0000256|HAMAP-
CC         Rule:MF_00065};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00065}.
CC   -!- SIMILARITY: Belongs to the APS kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00065}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00065}.
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DR   EMBL; CP000088; AAZ54463.1; -; Genomic_DNA.
DR   RefSeq; WP_011290872.1; NC_007333.1.
DR   STRING; 269800.Tfu_0425; -.
DR   EnsemblBacteria; AAZ54463; AAZ54463; Tfu_0425.
DR   KEGG; tfu:Tfu_0425; -.
DR   eggNOG; ENOG4108WF4; Bacteria.
DR   eggNOG; COG0529; LUCA.
DR   HOGENOM; HOG000069044; -.
DR   KO; K00958; -.
DR   OMA; KEHRDLN; -.
DR   OrthoDB; 1574819at2; -.
DR   BioCyc; TFUS269800:G1G4Q-431-MONOMER; -.
DR   UniPathway; UPA00140; UER00205.
DR   Proteomes; UP000000434; 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:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:InterPro.
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   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR   InterPro; IPR002891; APS_kinase.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00455; apsK; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SV4.
DR   SWISS-2DPAGE; Q47SV4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000256|SAAS:SAAS01092249, ECO:0000313|EMBL:AAZ54463.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00065};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00065,
KW   ECO:0000313|EMBL:AAZ54463.1}.
FT   DOMAIN       18     93       PUA_2. {ECO:0000259|Pfam:PF14306}.
FT   DOMAIN      117    309       ATP-sulfurylase. {ECO:0000259|Pfam:
FT                                PF01747}.
FT   NP_BIND     325    332       ATP. {ECO:0000256|HAMAP-Rule:MF_00065}.
SQ   SEQUENCE   493 AA;  52104 MW;  50134CD203C14899 CRC64;
     MTQPTGGRAV FTPGPQGLAH LELLLSGVCP LPGFMAQAEA AELDRPGPPP AGAAWPVPVT
     LTVPETLADV RELVLADPEG APLAELTVTE SFRDGTVRLA GPIRPAAPPA YGSHRSLRAT
     AADVRSARDE RRPLLAVVTD RPLHHRALAQ IRAALATLGD ADLLVLVDTP LDGEGAATVV
     LAARPCLPEH TRFAVLTLPT APADGAPEWS AERRGLLAAH VAAAYGATHL MLEGVGELPG
     TAAELPVKPV AATEWVYDTV HERWRPADEV PPAQARPEWD TAAVDEALAQ GTPLPAWLTP
     EPVAAALART RPARTRRGLV LFFTGLSGSG KSTVARGVAE QIRQAGRTVT LLDGDVVRRL
     LSAGLTFSRA DRDLNIRRIG YVAAEIARHG GVAVCAPIAP YAATRAEVRR MAEETGDFFL
     VYVATPLEVC EARDRKGLYA KARAGEIPAF TGISDPYEPP EDADLVLDTS TESEEESVAR
     VVAALRAGGW LPR
//

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