ID G0VDX4_NAUCC Unreviewed; 511 AA.
AC G0VDX4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_03106};
DE EC=2.7.7.4 {ECO:0000256|HAMAP-Rule:MF_03106};
DE AltName: Full=ATP-sulfurylase {ECO:0000256|HAMAP-Rule:MF_03106};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000256|HAMAP-Rule:MF_03106};
DE Short=SAT {ECO:0000256|HAMAP-Rule:MF_03106};
GN Name=NCAS0D01830 {ECO:0000313|EMBL:CCC69764.1};
GN Synonyms=MET3 {ECO:0000256|HAMAP-Rule:MF_03106};
GN OrderedLocusNames=NCAS_0D01830 {ECO:0000313|EMBL:CCC69764.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC69764.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC69764.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate
CC assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic
CC sulfate and ATP. Plays an important role in sulfate activation as a
CC component of the biosynthesis pathway of sulfur-containing amino acids.
CC {ECO:0000256|HAMAP-Rule:MF_03106}.
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:0000256|HAMAP-
CC Rule:MF_03106};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000256|HAMAP-
CC Rule:MF_03106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106}.
CC -!- DOMAIN: The oligomerization domain is distantly related to APS kinases,
CC but it is not functional and does not bind APS. It is required for
CC oligomerization of the enzyme, although the oligomerization state has
CC no effect on the catalytic activity of the enzyme. {ECO:0000256|HAMAP-
CC Rule:MF_03106}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_03106}.
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DR EMBL; HE576755; CCC69764.1; -; Genomic_DNA.
DR RefSeq; XP_003676126.1; XM_003676078.1.
DR AlphaFoldDB; G0VDX4; -.
DR STRING; 1064592.G0VDX4; -.
DR GeneID; 11528238; -.
DR KEGG; ncs:NCAS_0D01830; -.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_022950_1_0_1; -.
DR InParanoid; G0VDX4; -.
DR OMA; EWFSFPE; -.
DR OrthoDB; 159at2759; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000001640; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1.
DR HAMAP; MF_03106; Sulf_adenylyltr_euk; 1.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR027535; Sulf_adenylyltr_euk.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03106}; Cysteine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03106};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03106};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03106};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_03106}; Reference proteome {ECO:0000313|Proteomes:UP000001640};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03106}.
FT DOMAIN 3..162
FT /note="ATP-sulfurylase PUA-like"
FT /evidence="ECO:0000259|Pfam:PF14306"
FT DOMAIN 172..386
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 1..167
FT /note="N-terminal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT REGION 168..393
FT /note="Catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT REGION 394..511
FT /note="Required for oligomerization; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT ACT_SITE 196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT ACT_SITE 197
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT ACT_SITE 198
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 195..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 195
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 197
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 289..292
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 293
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 201
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 204
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 328
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
SQ SEQUENCE 511 AA; 57167 MW; FEF18000B955C6D1 CRC64;
MPAPHGGILQ DLVARDASKK AALSQEAQSG SLAQWTLTAR QICDIELILN GGFSPLTGFL
TEKDYLSVVK NSRLADGTLW TMPITLDVDE TFAKSVAPNS RITLLQDGEI PIAILTVTDV
YRPDKALEAK EVFRGDPEHP AIRYLNNIAG EYYIGGSLEA IQLPQHYDYP GLRKAPAQLR
LEFQSRQWDR IVAFQTRNPM HRAHRELTVR AAREANAKVL IHPVVGLTKP GDIDHHTRVR
VYQEIIKRYP NGIAFLSLLP LAMRMGGDRE AVWHAIIRKN YGATHFIVGR DHAGPGSNSK
GVDFYGPYDA QELVESYKNE LDIQVVPFRM VTYLPDEDRY APIDQIDTSK TRTLNISGTE
LRKRLRVGGE IPEWFSYPEV VKILRESNPP RPKQGFAIVL EDSLNAPSGQ LAIALLSTFL
QFGGGRHYKV FEHENNDKLL ELIPDFIQAG SGLIVPNQWT SKNVSFGADQ NVYTLGASAN
SDIKLDSVDE TIFHIVQKVV LFLEDNGYLV F
//
