(data stored in ACNUC7421 zone)

SWISSPROT: Q47SW0_THEFY

ID   Q47SW0_THEFY            Unreviewed;       309 AA.
AC   Q47SW0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Sulfate adenylyltransferase {ECO:0000256|SAAS:SAAS00751631};
DE            EC=2.7.7.4 {ECO:0000256|SAAS:SAAS00751631};
GN   OrderedLocusNames=Tfu_0419 {ECO:0000313|EMBL:AAZ54457.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54457.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC         diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58243; EC=2.7.7.4;
CC         Evidence={ECO:0000256|SAAS:SAAS01122030};
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysD subfamily.
CC       {ECO:0000256|SAAS:SAAS00751627}.
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DR   EMBL; CP000088; AAZ54457.1; -; Genomic_DNA.
DR   RefSeq; WP_011290866.1; NC_007333.1.
DR   STRING; 269800.Tfu_0419; -.
DR   EnsemblBacteria; AAZ54457; AAZ54457; Tfu_0419.
DR   KEGG; tfu:Tfu_0419; -.
DR   eggNOG; ENOG4105C11; Bacteria.
DR   eggNOG; COG0175; LUCA.
DR   HOGENOM; HOG000263604; -.
DR   KO; K00957; -.
DR   OMA; FGQWQPK; -.
DR   OrthoDB; 499077at2; -.
DR   BioCyc; TFUS269800:G1G4Q-425-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019419; P:sulfate reduction; IEA:InterPro.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR011784; SO4_adenylTrfase_ssu.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF002936; CysDAde_trans; 1.
DR   TIGRFAMs; TIGR02039; CysD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47SW0.
DR   SWISS-2DPAGE; Q47SW0.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00751628};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00751622};
KW   Nucleotidyltransferase {ECO:0000256|SAAS:SAAS00751634,
KW   ECO:0000313|EMBL:AAZ54457.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|SAAS:SAAS00751625,
KW   ECO:0000313|EMBL:AAZ54457.1}.
FT   DOMAIN       37    263       PAPS_reduct. {ECO:0000259|Pfam:PF01507}.
SQ   SEQUENCE   309 AA;  35549 MW;  E7F6F27AEA955210 CRC64;
     MSQVSDAVGR YQLSQLDFLE AEAIFIMREV AAEFERPVLL FSGGKDSVVM LRIAEKAFWP
     APIPFPVMHV DTGHNFPEVI EFRDKRVAEL GVRLIVASVQ DLIDAGKVVE PKGRWASRNR
     LQTAALLEAI EKYGFDAAFG GARRDEEKAR AKERVFSFRD EFGQWDPKNQ RPELWNLYNT
     RVHRGENIRV FPLSNWTELD VWHYIRREGL RLPSIYFAHR RRVFERDGIL LPDSPYVTRD
     EDEEVFEASV RYRTVGDMTC TGAVLSTATT LDEVIAEIAA TRITERGQTR ADDRGSEAAM
     EERKREGYF
//

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