SAT_RUBXD
ID SAT_RUBXD Reviewed; 393 AA.
AC Q1AXE5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=Rxyl_0966;
OS Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC Bacteria; Actinobacteria; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC Rubrobacter.
OX NCBI_TaxID=266117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9941 / NBRC 16129 / PRD-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG03933.1; -; Genomic_DNA.
DR RefSeq; WP_011563951.1; NC_008148.1.
DR AlphaFoldDB; Q1AXE5; -.
DR SMR; Q1AXE5; -.
DR STRING; 266117.Rxyl_0966; -.
DR EnsemblBacteria; ABG03933; ABG03933; Rxyl_0966.
DR KEGG; rxy:Rxyl_0966; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_11; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR PhylomeDB; Q1AXE5; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000006637; 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..393
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340630"
SQ SEQUENCE 393 AA; 44645 MW; D5E090CCC16C3155 CRC64;
MMRTEYTTIT PHGGTLVDRR VPVGEREERR QRAAELPRIV LGPRNLSDLE MIGTGVFSPL
TGFMGREDYE SVVEEMRLAD GLPWSIPITL SVSEEEARSF EEGDEVALAN GEGEIVATMV
VEDRYTYDRA HEAKLVYRTT DTDHPGVAAL FRQGDVLVGG EVSLLDDGTT TRPFPRYYYE
PRELRAIFRQ KGWRRVVGFQ TRNPVHRAHE YIQKSALETV DGLLLNPLVG ETKSDDIPAH
VRMRSYEVLL ERYYPRDRTV LAVFPAAMRY AGPREAVFHA ICRKNYGCTH FIVGRDHAGV
GNYYGTYDAH RIFDEFEPGE LGITPLFFEH AFFCLNCGGM ATTKTCPHDK DSHVFFSGTR
VREMLRNGEY PPPEFSRPEV IEVLISGLRQ QEG