(data stored in SCRATCH zone)

SWISSPROT: D1CDF6_THET1

ID   D1CDF6_THET1            Unreviewed;       392 AA.
AC   D1CDF6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE            EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00066};
DE   AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_00066};
DE   AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE            Short=SAT {ECO:0000256|HAMAP-Rule:MF_00066};
GN   Name=sat {ECO:0000256|HAMAP-Rule:MF_00066};
GN   OrderedLocusNames=Tter_0039 {ECO:0000313|EMBL:ACZ40962.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ40962.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ40962.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00066, ECO:0000256|SAAS:SAAS01118665};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite
CC       from sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_00066,
CC       ECO:0000256|SAAS:SAAS00020412}.
CC   -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00066}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001825; ACZ40962.1; -; Genomic_DNA.
DR   RefSeq; WP_012873997.1; NC_013525.1.
DR   STRING; 525904.Tter_0039; -.
DR   EnsemblBacteria; ACZ40962; ACZ40962; Tter_0039.
DR   KEGG; ttr:Tter_0039; -.
DR   eggNOG; ENOG4107RIQ; Bacteria.
DR   eggNOG; COG2046; LUCA.
DR   HOGENOM; HOG000069044; -.
DR   KO; K00958; -.
DR   OMA; RMRCYEI; -.
DR   OrthoDB; 1574819at2; -.
DR   BioCyc; TTER525904:G1GGS-39-MONOMER; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; 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; cd00517; ATPS; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00066; Sulf_adenylyltr; 1.
DR   InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR020792; SO4_adenylyltransferase_pro.
DR   InterPro; IPR024951; Sulfurylase_cat_dom.
DR   InterPro; IPR002650; Sulphate_adenylyltransferase.
DR   Pfam; PF01747; ATP-sulfurylase; 1.
DR   Pfam; PF14306; PUA_2; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR00339; sopT; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1CDF6.
DR   SWISS-2DPAGE; D1CDF6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00066,
KW   ECO:0000256|SAAS:SAAS00426025};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00066,
KW   ECO:0000256|SAAS:SAAS00426026};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00066,
KW   ECO:0000256|SAAS:SAAS00020416, ECO:0000313|EMBL:ACZ40962.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00066,
KW   ECO:0000256|SAAS:SAAS00426032, ECO:0000313|EMBL:ACZ40962.1}.
FT   DOMAIN        6    162       PUA_2. {ECO:0000259|Pfam:PF14306}.
FT   DOMAIN      170    380       ATP-sulfurylase. {ECO:0000259|Pfam:
FT                                PF01747}.
SQ   SEQUENCE   392 AA;  43842 MW;  50E5050D48B6A56E CRC64;
     MQQELIDPHG GKLINRMAPQ ELLEDLRAEA ANLPKIPINA REQSDLDLIA VGAFSPLEGF
     MSSDDYRSVV NNMRLSNGLP WSLPVTLSTT EDVARSLSIG SKAALTRDEK IVATIEVQDI
     FSYDKVSDAE KVFRTSEEAH PGVRAMYAQG EILIGGPVTV FERAPLQFPK YNRTPAETRK
     LIQEKGWKTV VGFQTRNPVH RAHEYIQKCA LETVDGLLLH PLVGETKSDD VPADVRMKCY
     EVLLENYYPR DRVILGVLPA AMRYAGPREA IFHALIRKNY GCTHFIVGRD HAGVGNYYGT
     YDAQKLFDEF EPSELGITPM KFEHAFWCNQ CEAMASTKTC PHPESSRVVL SGTKVRNMLA
     SGQMPPKEFS RPEVAQILIE AYRSRQSVAD LA
//

If you have problems or comments...

PBIL Back to PBIL home page