ID A0A1I4G4X3_9ACTN Unreviewed; 398 AA.
AC A0A1I4G4X3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=sulfate adenylyltransferase {ECO:0000256|ARBA:ARBA00012391};
DE EC=2.7.7.4 {ECO:0000256|ARBA:ARBA00012391};
GN ORFNames=SAMN04488085_108155 {ECO:0000313|EMBL:SFL25095.1};
OS Geodermatophilus ruber.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=504800 {ECO:0000313|EMBL:SFL25095.1, ECO:0000313|Proteomes:UP000199152};
RN [1] {ECO:0000313|EMBL:SFL25095.1, ECO:0000313|Proteomes:UP000199152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45317 {ECO:0000313|EMBL:SFL25095.1,
RC ECO:0000313|Proteomes:UP000199152};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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};
CC -!- PATHWAY: Sulfur metabolism. {ECO:0000256|ARBA:ARBA00004678}.
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DR EMBL; FOSW01000008; SFL25095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4G4X3; -.
DR STRING; 504800.SAMN04488085_108155; -.
DR InParanoid; A0A1I4G4X3; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000199152; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 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; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR NCBIfam; TIGR00339; sopT; 1.
DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR PANTHER; PTHR42700: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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:SFL25095.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199152};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFL25095.1}.
FT DOMAIN 7..160
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 170..384
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
SQ SEQUENCE 398 AA; 43804 MW; B1FAE60AC8563551 CRC64;
MAIPGPPPHG GALVDLRVED GRAVAAAAQE LPRWELTRRQ RCDLELLATG GFSPLRTFLG
RADHASVCTA MRLTTGELWP IPVTLDLPEC VVAAASSAGG LTLCARGADL AVLWLREAWR
PDRVAEAAAV FGTTDPAHPG VHTLLHETHP WYVSGPLAVL ALPTHHDFRS LRHTPAELRR
ELADRGWDTV VAFQTRNPMH RAHQELTIRA ARELGAHVLL HPVVGITKPG DVDPSVRVRC
YRALLPTYPP GTVLLSVLPL AMRMAGPREA LWHAIVRKNH GATHFIVGRD HAGPGPDSQG
RPFYEPSEAQ DLLRRHEDEL GIGVVPFRQM VFVRELQRHV PEDEVPPGHH CLRISGTEQR
RRLAQGEELP EWFTPPEVAA ELRRAFPGRT GEAVALLS
//
