MET3_DEBHA
ID MET3_DEBHA Reviewed; 530 AA.
AC Q6BSU5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=DEHA2D06138g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG86869.1; -; Genomic_DNA.
DR RefSeq; XP_458725.1; XM_458725.2.
DR AlphaFoldDB; Q6BSU5; -.
DR SMR; Q6BSU5; -.
DR STRING; 4959.XP_458725.1; -.
DR PRIDE; Q6BSU5; -.
DR EnsemblFungi; CAG86869; CAG86869; DEHA2D06138g.
DR GeneID; 2901244; -.
DR KEGG; dha:DEHA2D06138g; -.
DR VEuPathDB; FungiDB:DEHA2D06138g; -.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_022950_0_0_1; -.
DR InParanoid; Q6BSU5; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 528280at2759; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000000599; Chromosome D.
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; 3.40.50.300; -; 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..530
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000283685"
FT REGION 1..178
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 179..410
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 411..530
FT /note="Required for oligomerization; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 209
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 210
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 211
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 208..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 208
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 210
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 304..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 308
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 214
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 217
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 345
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
SQ SEQUENCE 530 AA; 59449 MW; D17A98D832D08F71 CRC64;
MPIPAPHGGK LQDLVIRDSS IRSDLFKEIA DKKYKTLTLS PRQLCDLELI LNGGFSPLTG
FLNEEDYNSV VHDMRLSSVK NEKNGKGLLW SMPITLDVGQ EFAGKLSKGE KIVLKDLRDE
KPLALLTVET VYKPNKQTEA EKVFRGDPEH PAIKYLFETA QEFYVGGSIQ GLDYPTHYDY
IPFRKTPTEL REEFSKLGWD QQKVVAFQTR NPMHRAHREL TVRAANDLGS DGHILIHPVV
GLTKPGDIDH HTRVRVYQQI LKKYPDGLAT LSLLPLAMRM GGDREAMWHS LIRMNYGVDH
FIVGRDHAGP GSNSKGVDFY GPYDAQELLA KYKDELEPKI KVVPFRMVTY LPDEDRYAPI
DTIDTSKVNT ANISGTELRQ RLRDGTEIPG WFSYPEVVKV LRESNPPRSK QGFAIVIDSS
DSKQGEYLSF ALQSTLNQFS GERRITKLSS EQATPFIVNE LVKSGSGVIV PTKSNQSDII
KAVGSGNSII VNFNGEQNAD QGIFSLKEDL TSVIGEIVEY LVSQGFYQQS
