SAT_PYRAB
ID SAT_PYRAB Reviewed; 379 AA.
AC P56863; G8ZKF1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4;
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
GN Name=sat; OrderedLocusNames=PYRAB11700; ORFNames=PAB1595;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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;
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AJ248286; CAB50081.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70594.1; -; Genomic_DNA.
DR PIR; D75097; D75097.
DR RefSeq; WP_010868287.1; NC_000868.1.
DR AlphaFoldDB; P56863; -.
DR SMR; P56863; -.
DR STRING; 272844.PAB1595; -.
DR EnsemblBacteria; CAB50081; CAB50081; PAB1595.
DR GeneID; 1496540; -.
DR KEGG; pab:PAB1595; -.
DR PATRIC; fig|272844.11.peg.1240; -.
DR eggNOG; arCOG04191; Archaea.
DR HOGENOM; CLU_022950_1_1_2; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 15586at2157; -.
DR PhylomeDB; P56863; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..379
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000105947"
SQ SEQUENCE 379 AA; 44026 MW; 7597ECEC3BFE9C7E CRC64;
MVSKPHGGKL IRRIAAPRTR ERILSEQHEY PKVQIDHGRA IDLENIAHGV YSPLKGFLTR
EDFESVLDHM RLSDDTPWTI PIVLDVEKPE FEEGDAILLY HKETPIARMH VEDIYTYEKE
EFALKVFKTK DANHPGVAKV YSMGKYLVGG EIELLNELPN PFAKYTLRPI ETRVLFKEKG
WKTVVAFQTR NVPHLGHEYV QKAALTFVDG LFINPVLGRK KRGDYKDEVI IKAYEVLFEH
YYPKDVAVLA TVRYEMRYAG PREAIHHAIM RKNFGATHFI VGRDHAGVGN YYGPYEAWDL
FDEFPDLGIT PMFIREAFYC KKCGGMVNEK ICPHDEKYHV RISGTKLRNM IMRGEKPPEY
MMRPEVYEVI RSFDNPFVE