SAT_PSYWF
ID SAT_PSYWF Reviewed; 419 AA.
AC A5WEH0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN OrderedLocusNames=PsycPRwf_1111;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-2007) 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; CP000713; ABQ94061.1; -; Genomic_DNA.
DR RefSeq; WP_011960370.1; NC_009524.1.
DR AlphaFoldDB; A5WEH0; -.
DR SMR; A5WEH0; -.
DR STRING; 349106.PsycPRwf_1111; -.
DR PRIDE; A5WEH0; -.
DR EnsemblBacteria; ABQ94061; ABQ94061; PsycPRwf_1111.
DR KEGG; prw:PsycPRwf_1111; -.
DR eggNOG; COG2046; Bacteria.
DR HOGENOM; CLU_022950_1_1_6; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 1574819at2; -.
DR UniPathway; UPA00140; UER00204.
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..419
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000340629"
SQ SEQUENCE 419 AA; 46569 MW; FC2337AA743FC7F8 CRC64;
MTSQKIVKRL GKTSIVPPHG SDELKPLLLE GEALSQALHN AKNLPKITLS SRERGDLIML
GIGGFTPLDG FMNQADWQGV VDEMTLKTGA NKGLFWPIPI TLSTSKEQAD SLAPGDEVAL
VAEDGEIMGV ITVEETYTID KAHECQQVFT TTEEEHPGVK QVMEQGEVNV AGAVKVFSQG
EFPTLYPEIY KTPAETRKLF EEKNWQTIAA FQTRNPMHRS HEYLAKIAIE ICDGVMIHSL
LGALKPGDIP AEVRQEAIKT LIDNYFKKDT VIQAGYPLDM RYAGPREALL HALFRQNYGC
SHLIVGRDHA GVGDYYGPFD AQAIFDEIDK DAMLTQPLKI DWTFWCNACQ AMASTKTCPH
DAEHHVKVSG TKLRKALSED QEVPENFSRP EVLQILRNYY ESIAKEDRAE VKLVGASAQ
