SAT_STAES
ID SAT_STAES Reviewed; 392 AA.
AC Q8CR03;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=SE_2175;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05817.1; -; Genomic_DNA.
DR RefSeq; NP_765730.1; NC_004461.1.
DR RefSeq; WP_002438012.1; NZ_WBME01000005.1.
DR AlphaFoldDB; Q8CR03; -.
DR SMR; Q8CR03; -.
DR STRING; 176280.SE_2175; -.
DR EnsemblBacteria; AAO05817; AAO05817; SE_2175.
DR KEGG; sep:SE_2175; -.
DR PATRIC; fig|176280.10.peg.2124; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_9; -.
DR OMA; LQHMIIR; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001411; 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..392
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105942"
SQ SEQUENCE 392 AA; 44354 MW; 907BD810DBAA0490 CRC64;
MSNNETITNY TIKPHGGELI NRVVEGNERE RLIEEALKFK PITLNPWGIS DLELIGIGGF
SPLTGFMNKE DYTKVIEETH LSNGLVWSIP ITLPVTESEA DKLEIGDDIA LYGEDGQLYG
TLKLEEKYTY DKEKEARLVY GTTEEAHPGV KKVYEKGNIY LGGPIKLLNR PKHDAFSNYH
LDPSETRQLF HDLGWKTVVG FQTRNPVHRA HEYIQKSALE IVDGLLLNPL VGETKSDDIP
ADVRMESYEV ILKNYYPEDR ARLVIYPAAM RYAGPREAIL HATVRKNYGC THFIVGRDHA
GVGDYYGTYE AQELITQFED ELGIQILKFE HAFYCEACGN MATAKTCPHD ASQHLHLSGT
KVREKLRNGE SLPTKFSRPE VAEVLIKGLR EK
