SAT_GLOVI
ID SAT_GLOVI Reviewed; 392 AA.
AC Q7NLN7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=glr1084;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(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; BA000045; BAC89025.1; -; Genomic_DNA.
DR RefSeq; NP_924030.1; NC_005125.1.
DR RefSeq; WP_011141086.1; NC_005125.1.
DR AlphaFoldDB; Q7NLN7; -.
DR SMR; Q7NLN7; -.
DR STRING; 251221.35211647; -.
DR EnsemblBacteria; BAC89025; BAC89025; BAC89025.
DR KEGG; gvi:glr1084; -.
DR PATRIC; fig|251221.4.peg.1111; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_3; -.
DR InParanoid; Q7NLN7; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR PhylomeDB; Q7NLN7; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000557; 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..392
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340623"
SQ SEQUENCE 392 AA; 43700 MW; A1FC90D2242C8436 CRC64;
MSSAPKQTIA PHGGTLINQV ATAEQRQKYQ DGAGGFKRVR IDDRAVSDLE LIAIGGFSPL
TGFMGSEDYH SVVEKMRLTS GVVWSIPITL PVSAEVAETL EIGESLGLED STGTLVGILD
LAEKYTYDKL REAEMVYRTT DEKHPGVKVV YGQGDVYLAG PIMLLERRPH PLFASRQLDP
ADSRQAFIDK GWRSVVGFQT RNPIHRAHEY IQKCALEIVD GLFLHPLVGA TKSDDIPADV
RMHCYEVLIE KYYPLDRVIL AINPAAMRYA GPREAIFHAL VRKNYGCTHF IVGRDHAGVG
DYYGTYDAQY IFYEFEPQDL GITPLMFEHA FYCKRIAGMA TTKTSPSGPE DRIHLSGTKV
RAMLREGLEP PPEFTRPEVA RILIEAIQKQ GQ