SAT_THIDA
ID SAT_THIDA Reviewed; 402 AA.
AC Q3SEZ6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=Tbd_0874;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ96827.1; -; Genomic_DNA.
DR RefSeq; WP_011311386.1; NC_007404.1.
DR AlphaFoldDB; Q3SEZ6; -.
DR SMR; Q3SEZ6; -.
DR STRING; 292415.Tbd_0874; -.
DR PRIDE; Q3SEZ6; -.
DR EnsemblBacteria; AAZ96827; AAZ96827; Tbd_0874.
DR KEGG; tbd:Tbd_0874; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_4; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR BRENDA; 2.7.7.4; 11660.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000008291; 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_0000340638"
SQ SEQUENCE 402 AA; 44316 MW; 83A23B4DD742859A CRC64;
MSKLVRPHGG GELKPLLLTG DALSAEKARA ASLPQLKMSS RETGDLIMMG IGGFTPLDGF
MTKSDWQGVC DGYKMTNGLF WPIPITLSTD DESIKDGDEL ALVDAETGEI MGTMKVTDKY
TIDKAHECMQ VYKTTDMEHP GVKMVMAQGK YNLAGPVKVL STGNFKEEYG EQFMTPAETR
AKFEQMGWSR VAAFQTRNPM HRSHEYLAKI AIETMDGVLV HSLLGALKPG DIPAEVRSEA
IATLIDNYFA PNTVIQAGYP LDMRYAGPRE ALLHALFRQN YGCSHLIVGR DHAGVGDYYG
PFDAQKIFDE IPKGSLETVN MNIDWTFWCK KCGGMASQRT CPHTKDDRIL LSGTKVRAML
SEGQDLPVEF SRPEVAKVLQ KYYAGLSAEQ NVKVELKGHS AA