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Entry: E6ZYJ1_SPORE
LinkDB: E6ZYJ1_SPORE
Original site: E6ZYJ1_SPORE 
ID   E6ZYJ1_SPORE            Unreviewed;       574 AA.
AC   E6ZYJ1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=MET3 {ECO:0000256|HAMAP-Rule:MF_03106};
GN   ORFNames=sr13006 {ECO:0000313|EMBL:CBQ72298.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72298.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ72298.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
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   -!- ACTIVITY REGULATION: Allosterically inhibited by 3'-phosphoadenosine
CC       5'-phosphosulfate (PAPS). {ECO:0000256|HAMAP-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 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:0000256|HAMAP-Rule:MF_03106}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the APS kinase
CC       family. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the sulfate
CC       adenylyltransferase family. {ECO:0000256|HAMAP-Rule:MF_03106}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03106}.
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DR   EMBL; FQ311463; CBQ72298.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZYJ1; -.
DR   EnsemblFungi; CBQ72298; CBQ72298; sr13006.
DR   VEuPathDB; FungiDB:sr13006; -.
DR   eggNOG; KOG0636; Eukaryota.
DR   HOGENOM; CLU_022950_0_0_1; -.
DR   OrthoDB; 159at2759; -.
DR   UniPathway; UPA00097; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000008867; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004020; F:adenylylsulfate kinase activity; IEA:UniProtKB-EC.
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; 3.40.50.620; 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; 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   NCBIfam; TIGR00455; apsK; 1.
DR   NCBIfam; TIGR00339; sopT; 1.
DR   PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01583; APS_kinase; 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   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW   Rule:MF_03106}; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03106}.
FT   DOMAIN          4..165
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          174..388
FT                   /note="Sulphate adenylyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01747"
FT   REGION          1..170
FT                   /note="N-terminal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   REGION          396..574
FT                   /note="Allosteric regulation domain; adenylyl-sulfate
FT                   kinase-like"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   ACT_SITE        199
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   ACT_SITE        200
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   ACT_SITE        201
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         198..201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         198
FT                   /ligand="sulfate"
FT                   /ligand_id="ChEBI:CHEBI:16189"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         200
FT                   /ligand="sulfate"
FT                   /ligand_id="ChEBI:CHEBI:16189"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         292..295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         296
FT                   /ligand="sulfate"
FT                   /ligand_id="ChEBI:CHEBI:16189"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         435..438
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /ligand_note="allosteric inhibitor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   BINDING         519
FT                   /ligand="3'-phosphoadenylyl sulfate"
FT                   /ligand_id="ChEBI:CHEBI:58339"
FT                   /ligand_note="allosteric inhibitor"
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            207
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT   SITE            331
FT                   /note="Induces change in substrate recognition on ATP
FT                   binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
SQ   SEQUENCE   574 AA;  63661 MW;  5FCB87C1DCF7EA30 CRC64;
     MANAPHGGVL KDLLVRDAPI AAQLRQEADT LPELVLTERQ LCDLELIING GFSPLQGFMN
     QADYNGCLDS MRLTDGNLFP MPITLDVDQQ QIQTLNIQQG ARIALRDPRD DNAIAIITVT
     DVYAVDKVRE AKAVFGSDDL AHPAITYLHK SVKEFYVGGE VQAISKPNYY DYAELRYTPA
     ELRQHFAKIA WRKVVAFQTR NPMHRAHREL TVRAARQRQA NVLIHPVVGM TKPGDVDHYT
     RVRVYQSLMP RYPNGMATLA LLPLAMRMGG PREALWHAII RKNFGVTHFI VGRDHAGPGK
     DSSGKDFYGP YDAQTLVTKY TDELGIEMVP FQQMTYIPST DEYQPVDEIT PGTQTMDISG
     TELRRRLRTG AAIPDWFSYE SVVKTLRESY PPKAKQGFTL FLTGLHNSGK DQIARALQVK
     LNEQGGRSVS LLLGETVRSE LSSELGFSPE DRAKNIQRIS FVAAELTRAG AAVIAAPIAP
     YEKARAAARD TITKTGGAGN FFLIHVATPL EFCEKTDRKG NYAKARAGHI KGFTGVDDVY
     EEPTDADLVV DISRQSVAEI THSIILLLEA QSLI
//
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