SAT_ALKCK
ID SAT_ALKCK Reviewed; 372 AA.
AC Q5WKF4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, 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=ABC0612;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) 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; AP006627; BAD63151.1; -; Genomic_DNA.
DR RefSeq; WP_011245467.1; NC_006582.1.
DR AlphaFoldDB; Q5WKF4; -.
DR SMR; Q5WKF4; -.
DR STRING; 66692.ABC0612; -.
DR EnsemblBacteria; BAD63151; BAD63151; ABC0612.
DR KEGG; bcl:ABC0612; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_9; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001168; 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..372
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_1000075092"
SQ SEQUENCE 372 AA; 41893 MW; 3EA7F4DBF174CF7C CRC64;
MEAVKETELV HRYDPAYDTT GITNEIALDG FALSDLELLG IGGFTPLTGF LNEDDYHSVV
KSMRLANGAP WSIPISLPVS ADQASALRVG ERAKLVYKND IYGVIEIESI YTPDKKVEAQ
EVYRTTDEAH PGVAKMYARP PIYVGGPIVL TKRVNYERFA SYYIDPIDTR RIFAEKGWKT
VVGFQTRNPV HRAHEYIQKA ALETVDGLFL NPLVGETKAG DIPADVRMES YEVLLKNYYP
KNRVHLSVFP AAMRYAGPRE AIFHALVRKN YGCTHFIVGR DHAGVGNYYG TYDAQEIFKE
FEEGELGIKP LFFEHSFYCK ACGNMASQKT CPHDSEHHVI LSGTKVRQML KEGVLPPQEF
SRKEVVEVLM RG
