SAT_HYPBU
ID SAT_HYPBU Reviewed; 389 AA.
AC A2BMW0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Hbut_1499;
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX PubMed=17350933; DOI=10.1155/2007/745987;
RA Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.-P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(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; CP000493; ABM81321.1; -; Genomic_DNA.
DR RefSeq; WP_011822639.1; NC_008818.1.
DR AlphaFoldDB; A2BMW0; -.
DR SMR; A2BMW0; -.
DR STRING; 415426.Hbut_1499; -.
DR EnsemblBacteria; ABM81321; ABM81321; Hbut_1499.
DR GeneID; 4781530; -.
DR KEGG; hbu:Hbut_1499; -.
DR eggNOG; arCOG04191; Archaea.
DR HOGENOM; CLU_022950_1_1_2; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 15586at2157; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002593; 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;
KW Reference proteome; Transferase.
FT CHAIN 1..389
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_1000009040"
SQ SEQUENCE 389 AA; 44698 MW; 6DE72C75C3BAE512 CRC64;
MVSRPHGGRL VDRTVSDKRR ERLREEAREL PAIRLTAGLA ADVANIAHGV YSPLEGFMLQ
EDYLSVLDEM RLSNDLPWTI PIILDVDPGE IAGVREGDDI ALVYNGKPIA LMRVEEIYGW
DRKEYAAKVF KTTDPAHPGV AKTMKRKELL IGGPIDLIED PPEPFERYRL WPKETRVLFK
ARGWKTIAAF QTRNVPHLGH EYVQKAALTF TDGLFVNPLV GWKKPGDYRD EVIVEAYQAL
IKHYFPVESV VFSVLRMEMR YAGPREAIHH AIVRKNFGAT HFIVGRDHAG VGNYYGPYEA
WELFREFPDL GITPLFVREA FYCRKCGQMV NEKICPHPEE YRVRISGTKL RRMLLEGQRP
PEYMMRPEVV DVVLKHPNPF IEGDEAFQE
