SAT_STACT
ID SAT_STACT Reviewed; 399 AA.
AC B9DLL5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Sca_0063;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL26977.1; -; Genomic_DNA.
DR RefSeq; WP_012664092.1; NC_012121.1.
DR AlphaFoldDB; B9DLL5; -.
DR SMR; B9DLL5; -.
DR STRING; 396513.SCA_0063; -.
DR GeneID; 60546257; -.
DR KEGG; sca:SCA_0063; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_9; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR BioCyc; SCAR396513:SCA_RS00300-MON; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000444; 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..399
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_1000117969"
SQ SEQUENCE 399 AA; 45092 MW; 0874DD499BE92BD8 CRC64;
MATATQIINY TSTPHGGELI NRQLEGAERE ALIKEAEAFP KLTLNAWSLS DLELIAIGGF
SPLTGFMGEA DYTNVVENLH LADGTLWSIP ITLPVTEEQA DAYELGSKIA LYGEDDKLYG
VLDLQEKFTY DKEKEAENVY GTTEEAHPGV KKVYEKGNVY LAGPIQLVNR PDHSEFEEFE
LDPIEVRQMF HDLGWKTVVG FQTRNPVHRA HEYIQKSALE TVDGLLLNPL VGETKADDIP
ADVRMESYQV ILKNYFPENR ARLAIYPAAM RYAGPREAIL HAIVRLNYGC THFIVGRDHA
GVGDYYGTYE AQELISQYED ELGINIMKFE HAFYCTKCEN MATAKTCPHD KKYHVHLSGT
KVREKLRNGE PLPKEFSRPE VAEVLIRGLR RHREQNGEG
