ID A0A0M9GUL8_9BACI Unreviewed; 383 AA.
AC A0A0M9GUL8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:KPB05889.1};
GN ORFNames=AAV98_02855 {ECO:0000313|EMBL:KPB05889.1};
OS Bacillus sp. CHD6a.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1643452 {ECO:0000313|EMBL:KPB05889.1, ECO:0000313|Proteomes:UP000037908};
RN [1] {ECO:0000313|EMBL:KPB05889.1, ECO:0000313|Proteomes:UP000037908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHD6a {ECO:0000313|EMBL:KPB05889.1,
RC ECO:0000313|Proteomes:UP000037908};
RA Lin W., Liu Y., Zheng Q., Jiao N.;
RT "Genome sequence of Bacillus sp. CHD6a isolated from the shallow-sea
RT hydrothermal environment.";
RL Submitted (APR-2015) 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:KPB05889.1}.
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DR EMBL; LBMD01000002; KPB05889.1; -; Genomic_DNA.
DR RefSeq; WP_060664053.1; NZ_LBMD01000002.1.
DR AlphaFoldDB; A0A0M9GUL8; -.
DR STRING; 1643452.AAV98_02855; -.
DR PATRIC; fig|1643452.3.peg.1818; -.
DR OrthoDB; 9804504at2; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000037908; 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; -; 1.
DR PANTHER; PTHR43509:SF1; SULFATE ADENYLYLTRANSFERASE; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00066}.
FT DOMAIN 5..154
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 163..372
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 383 AA; 43193 MW; 429DB9EA0FFA4471 CRC64;
MTLPKPHGGT LVQAYQPNYE TTKLTKEIEI DAIALSDLEL IGVGLFSPLT GFLTKTDYES
VVENLRLANG TVWSVPVTLP VTKEVASSLQ QGVTYKLTHQ QTTYGVMTVS EWYEPDLQKE
AREVYKTEEL AHPGVKRLFE RGEIYVAGEV TLIKKPNKGV AQDVWLEPKQ TRQLFEQKGW
KTVVGFQTRN PVHRAHEYIQ KAALETVDGL FLNPLVGETK SDDIPADVRL KSYRVLLENY
YPTDRVQLAV YPAAMRYAGP REAIFHAIAR KNFGCTHFIV GRDHAGVGDY YGTYDAQHIF
HQFTEEELGI KPLFFEHSFY CNKCEGMASD KTCPHPSKDR VILSGTKVRE LLRAGELPPS
TFSRKEVIEV LIDGLKQEKT AAV
//
