MET3_CRYNH
ID MET3_CRYNH Reviewed; 581 AA.
AC Q8TG24; J9VR79; Q96UP1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
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}; ORFNames=CNAG_04215;
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=12177356; DOI=10.1099/00221287-148-8-2617;
RA Yang Z., Pascon R.C., Alspaugh A., Cox G.M., McCusker J.H.;
RT "Molecular and genetic analysis of the Cryptococcus neoformans MET3 gene
RT and a met3 mutant.";
RL Microbiology 148:2617-2625(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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 -!- ACTIVITY REGULATION: Allosterically inhibited by 3'-phosphoadenosine
CC 5'-phosphosulfate (PAPS). {ECO:0000255|HAMAP-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 adenylyl-sulfate kinase (APS kinase) is non-functional. It
CC is involved in allosteric regulation by PAPS. PAPS binding induces a
CC large rotational rearrangement of domains lowering the substrate
CC affinity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000255|HAMAP-Rule:MF_03106}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC family. {ECO:0000255|HAMAP-Rule:MF_03106}.
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DR EMBL; AF489498; AAL92174.1; -; Genomic_DNA.
DR EMBL; AY035556; AAK61369.1; -; mRNA.
DR EMBL; CP003828; AFR96947.1; -; Genomic_DNA.
DR RefSeq; XP_012051668.1; XM_012196278.1.
DR AlphaFoldDB; Q8TG24; -.
DR SMR; Q8TG24; -.
DR SwissPalm; Q8TG24; -.
DR EnsemblFungi; AFR96947; AFR96947; CNAG_04215.
DR GeneID; 23887653; -.
DR VEuPathDB; FungiDB:CNAG_04215; -.
DR HOGENOM; CLU_022950_0_0_1; -.
DR UniPathway; UPA00140; UER00204.
DR PHI-base; PHI:265; -.
DR Proteomes; UP000010091; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:InterPro.
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; cd02027; APSK; 1.
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; IPR002891; APS_kinase.
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 2: Evidence at transcript level;
KW Allosteric enzyme; Amino-acid biosynthesis; ATP-binding;
KW Cysteine biosynthesis; Cytoplasm; Methionine biosynthesis;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..581
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000283684"
FT REGION 1..176
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 177..401
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 402..581
FT /note="Allosteric regulation domain; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 205
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 206
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 204..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 204
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 206
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 298..301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 302
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 441..444
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 486..487
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 526
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 210
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 213
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 337
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT CONFLICT 293
FT /note="T -> N (in Ref. 1; AAK61369)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="T -> N (in Ref. 1; AAK61369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 64515 MW; A40A82DE0FA5580D CRC64;
MANAPHGGVL KDLLVRDAAL HDSLLEEARS LNDIFLTERQ LCDLELILNG GFSPLEGFMD
EQDYTSVVET LRLAPFNGHK YGHVFPIPIT LDVSQEDINT LGLKQGARVA LRDPRDDAAL
AILTVSDIYR PNKATEAEKV MGADDIAHPS VAYLRNNVKE FYVGGKVQAI QAPTHFDYVP
LRYTPAELRA HFHKLAWRKV VAFQTRNPMH RAHRELTVRA ARQRRANVLI HPVVGLTKPG
DVDHYTRVRA YQALMPSYPE GMAHLALLPL AMRMAGPREA VWHAVIRKNF GATHFIVGRD
HAGPGKNSQG KDFYGPYDAQ ELVTQFKDEL QIEMVPFQAM TYLPGSDEYQ PVDEVPKGTP
TADISGTELR KRLRTGASIP DWFSYTGVVK VLRESYPPRP QQGFTILLTG LHNSGKDTIA
RALQVTLQQQ GSRSVSLLLG EELRSDLDPQ IGRAITPEQK HINLERIGFV AAELTKAGAA
VIAAPTAPYE RSRQAFKKQV VGSGGGNYFL VHVATPLEWC EKVDRRGLYK AARAGEIKNL
TGVDDVYEAP ENADLVCDLR IDTVPEIVHS IIMILESQNL V
