MET3_CANGA
ID MET3_CANGA Reviewed; 507 AA.
AC Q6FXQ8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03106};
DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_03106};
DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_03106};
DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_03106};
DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_03106};
GN Name=MET3 {ECO:0000255|HAMAP-Rule:MF_03106};
GN OrderedLocusNames=CAGL0B03839g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_03106};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000255|HAMAP-
CC Rule:MF_03106}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_03106}.
CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03106}.
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DR EMBL; CR380948; CAG58037.1; -; Genomic_DNA.
DR RefSeq; XP_445137.1; XM_445137.1.
DR AlphaFoldDB; Q6FXQ8; -.
DR SMR; Q6FXQ8; -.
DR STRING; 5478.XP_445137.1; -.
DR EnsemblFungi; CAG58037; CAG58037; CAGL0B03839g.
DR GeneID; 2886500; -.
DR KEGG; cgr:CAGL0B03839g; -.
DR CGD; CAL0127678; MET3.
DR VEuPathDB; FungiDB:CAGL0B03839g; -.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_022950_1_0_1; -.
DR InParanoid; Q6FXQ8; -.
DR OMA; LQHMIIR; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000002428; Chromosome B.
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:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IEA:EnsemblFungi.
DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:EnsemblFungi.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cysteine biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..507
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000283680"
FT REGION 1..165
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 166..391
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 392..507
FT /note="Required for oligomerization; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 194
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 195
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 193..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 193
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 195
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 287..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 291
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 199
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 202
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 326
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
SQ SEQUENCE 507 AA; 57228 MW; 55C803FF7693F9EB CRC64;
MPAPHGGVLQ DLVARDASKR DSLLSESQQL SQWTLTARQI CDIELILNGG FSPLTGFLAQ
EDYNGVVHNS RLSDGTLWTM PITLDVPEQF ANSVKPNQRI ALLQDGTIPV AILTVKDIYK
PDKSVEAEKV FRGDPEHPAI NYLFNTAGDY YIGGALDAIQ LPQHYDYPGL RKTPAQLRLE
FQSRQWDRVV AFQTRNPMHR AHRELTVRAA RETNAKVLIH PVVGLTKPGD IDHHTRVRVY
QEIIKRYPNG IAFLSLLPLA MRMGGDREAV WHAIIRKNYG ASHFIVGRDH AGPGSNSKGV
DFYGPYDAQE LVESYKNELD IDVVPFRMVT YLPDEDRYAP IDEIDTSKTR TLNISGTELR
KRLRDGGEIP EWFSYPEVVK ILRESNPPRP KQGFALVFND DIKVDRDQLS IALLSTFLQF
GGGRHYKIYD HNDKPEFLEL ISDFVQAGSG LIIPSTWSAS NKVNSANVYT IGHAKDADIK
LASTEETIFH IVQKVVLFLE DNHFIQF
