SAT_RUTMC
ID SAT_RUTMC Reviewed; 402 AA.
AC A1AVC7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Rmag_0085;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthia.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(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; CP000488; ABL01884.1; -; Genomic_DNA.
DR RefSeq; WP_011737510.1; NC_008610.1.
DR AlphaFoldDB; A1AVC7; -.
DR SMR; A1AVC7; -.
DR STRING; 413404.Rmag_0085; -.
DR PRIDE; A1AVC7; -.
DR EnsemblBacteria; ABL01884; ABL01884; Rmag_0085.
DR KEGG; rma:Rmag_0085; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_6; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002587; 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..402
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340631"
SQ SEQUENCE 402 AA; 44508 MW; 60C5B1B2EC503BD9 CRC64;
MTKLVPPHGS DTLKSLALEG NALTVELERA KLLPKINCSS REEGDIIMMG VGGFTPLEGF
MGKADWQSVC DNMTIESGLF WPIPITLSTD NEGVNQGDEV ALVNGETDEI IATMVISEKY
SIDKTHECNT VYKTTEIEHP GVVMVMAQGK YNLAGSIKVL SDGGFPEKYS SLYMTPMETR
AYFDDKGWKT VAAFQTRNPM HRSHEYLVKI AVEVCDGVMI HSVLGNLKAG DIPANVRSEA
ISVLIENYFV DNTILQSGYP LDMRYAGPRE ALLHALFRQN YGCSHLIVGR DHAGIDDYYG
PFDAHNIFDE IADDALMTKA LKIDWTFWCH KCGGMSSMKT CPHSAEDRAL LSGTKVRKML
SDSEDLPETF SRPEVAKVLQ AYYAGIKDED KVEIKLNGHS AK
