ID A0A0A5GRX9_9BACI Unreviewed; 388 AA.
AC A0A0A5GRX9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_00066};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_00066};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_00066};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_00066};
GN Name=sat {ECO:0000256|HAMAP-Rule:MF_00066,
GN ECO:0000313|EMBL:KGX93920.1};
GN ORFNames=N781_01680 {ECO:0000313|EMBL:KGX93920.1};
OS Pontibacillus halophilus JSM 076056 = DSM 19796.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385510 {ECO:0000313|EMBL:KGX93920.1, ECO:0000313|Proteomes:UP000030528};
RN [1] {ECO:0000313|EMBL:KGX93920.1, ECO:0000313|Proteomes:UP000030528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 076056 {ECO:0000313|EMBL:KGX93920.1,
RC ECO:0000313|Proteomes:UP000030528};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000262, ECO:0000256|HAMAP-
CC Rule:MF_00066};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|ARBA:ARBA00005048, ECO:0000256|HAMAP-
CC Rule:MF_00066}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000256|ARBA:ARBA00037980, ECO:0000256|HAMAP-Rule:MF_00066}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGX93920.1}.
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DR EMBL; AVPE01000001; KGX93920.1; -; Genomic_DNA.
DR RefSeq; WP_036768834.1; NZ_AVPE01000001.1.
DR AlphaFoldDB; A0A0A5GRX9; -.
DR STRING; 1385510.GCA_000425205_00144; -.
DR eggNOG; COG2046; Bacteria.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000030528; Unassembled WGS sequence.
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; HUPs; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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 NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR43509; PTHR43509; 1.
DR PANTHER; PTHR43509:SF1; SULFATE ADENYLYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00066};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00066}; Reference proteome {ECO:0000313|Proteomes:UP000030528};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00066}.
FT DOMAIN 11..165
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 173..383
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 388 AA; 44137 MW; 8D226EDC8D08A65E CRC64;
MNSIQVGEQV APHGGRLVQR VDESKETRDR ASQLPKLRVS KWTVSDLELI GIGGFSPLTG
FMKQKDYESV VEQMRLADGT VWSIPITLPV YEKEAERFQI GDEVALEGED GVLYGILSLE
DVFTYDEAKE AQNVYGTTDQ NHPGVQKVYE KGNVYFGGPI TLIQRPDHGE FDEFYLDPSE
TRKLFKDLGW KTVVGFQTRN PVHRAHEYIQ KIALEAVDGL LLNPLVGETK SDDIPASIRM
ESYQEILKHY YPEQRTRLVI YPAAMRYAGP REAILHALVR KNYGCTHFIV GRDHAGIGDY
YGTYDAQEIF NAFTHEELGI SIFKFEHAFY CQKCENMATA KTCPHGKEDH VHLSGTKVRE
MLRKGEMPPK EFSRPEVVNV LIKGMKDR
//