ID A0A1G1K341_9BACT Unreviewed; 395 AA.
AC A0A1G1K341;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=A3C35_04435 {ECO:0000313|EMBL:OGW87294.1};
OS Omnitrophica bacterium RIFCSPHIGHO2_02_FULL_46_11.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801820 {ECO:0000313|EMBL:OGW87294.1, ECO:0000313|Proteomes:UP000176909};
RN [1] {ECO:0000313|EMBL:OGW87294.1, ECO:0000313|Proteomes:UP000176909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGW87294.1}.
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DR EMBL; MHFF01000012; OGW87294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1K341; -.
DR STRING; 1801820.A3C35_04435; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000176909; 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 4..160
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 169..383
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 395 AA; 44626 MW; 6D76227DA62264B7 CRC64;
MSLKPHGGIL INRELEGKPR DDAKERAKKL TVLTLSEREV CDLEMIATGA MSPLEGFMTK
SDYDSVLEKK RLVNKLPWTI PVTKSISAEE RSRISKESQV VLQDGRGRQL AILEVAGIFP
LDKKKEALAV YGTDEEAHPG VQQILKMGDF LVGGRISLFD RPAHTDFLEY RLDPKQTREL
FQKKNWKRVV AFQTRNPIHR AHEYLTKCAL ETVDGLMIHP LVGETKGDDV PARVRMECYK
VLIDKYYPKD HVLLSVFPAA MRYAGPREAV WHAICRKNYG CTHFIVGRDH AGCSKPDGKP
YYGSYDAQLI FDEFTPEEIG IEIYKFEHSF YDKKTGGIVS FKTAPADADQ FSVSGTKLRE
MLRAGQIPPP EITRPEVAQV LIEAMREKAA VSDKS
//
