SAT_SYNJA
ID SAT_SYNJA Reviewed; 393 AA.
AC Q2JU97;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_00066};
DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_00066};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_00066};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_00066};
GN Name=sat {ECO:0000255|HAMAP-Rule:MF_00066}; OrderedLocusNames=CYA_1559;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00066};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00066}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00066}.
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DR EMBL; CP000239; ABC99723.1; -; Genomic_DNA.
DR RefSeq; WP_011430401.1; NC_007775.1.
DR AlphaFoldDB; Q2JU97; -.
DR SMR; Q2JU97; -.
DR STRING; 321327.CYA_1559; -.
DR EnsemblBacteria; ABC99723; ABC99723; CYA_1559.
DR KEGG; cya:CYA_1559; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_3; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000008818; Chromosome.
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;
KW ATP-binding; Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..393
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340635"
SQ SEQUENCE 393 AA; 44127 MW; B25A8CC95521328D CRC64;
MTVSGDAIPP HGGTLVNRIA SPEQAQELRS KAEHCPILHL DERAQSDLEM IAIGGFSPLT
GFMGREDYQS VLETMHLANG LAWSLPVTLP VSAEIAADLK EGQTIALANA EGRLLGLLEL
TEKFTYDKTR EAQQVYRTTD EQHPGVKVLY QQGSVYLAGP VTLLQRDPHP LFPAYQIDPA
QSRQLFRERG WKTIVGFQTR NPIHRAHEYI QKCALEIVDG LFLHPLVGAT KSDDIPAEVR
MRCYEVLIEK YYPKERVILA INPAAMRYAG PREAIFHALV RKNYGCTHFI VGRDHAGVGN
YYGPYDAQHI FDEFRPEELG IIPLKFEHAF YCTVTGTMAT AKTSPSQPHQ RIHLSGTKVR
EMLRRGEIPP PEFSRPEVAQ LLAEAMRERG QPE
