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Entry: A0A135T6S1_9PEZI
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Original site: A0A135T6S1_9PEZI 
ID   A0A135T6S1_9PEZI        Unreviewed;       574 AA.
AC   A0A135T6S1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=CSIM01_11998 {ECO:0000313|EMBL:KXH43842.1};
OS   Colletotrichum simmondsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=703756 {ECO:0000313|EMBL:KXH43842.1, ECO:0000313|Proteomes:UP000070328};
RN   [1] {ECO:0000313|EMBL:KXH43842.1, ECO:0000313|Proteomes:UP000070328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS122122 {ECO:0000313|EMBL:KXH43842.1,
RC   ECO:0000313|Proteomes:UP000070328};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum simmondsii CBS122122.";
RL   Submitted (FEB-2014) 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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXH43842.1}.
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DR   EMBL; JFBX01000265; KXH43842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135T6S1; -.
DR   OrthoDB; 159at2759; -.
DR   UniPathway; UPA00097; -.
DR   UniPathway; UPA00140; UER00204.
DR   Proteomes; UP000070328; Unassembled WGS sequence.
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..166
FT                   /note="ATP-sulfurylase PUA-like"
FT                   /evidence="ECO:0000259|Pfam:PF14306"
FT   DOMAIN          175..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         516
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;  63972 MW;  8D272064CFB3A551 CRC64;
     MANSPHGGVL KDLFARDAPR QSELFAEADK LPSLLLTERH LCDLELILNG GFSPLEGFMT
     EKDYNGVVKD NRLADGALFS MPITLDVSQQ QIDTLSIKPG ARITLRDLRD DRNLAILTVE
     DVYKPDRVKE AIEVFGSDDD THPGVKHLFN NTNDFYVGGK LEAIQRLAHY DFLDLRFTPA
     ELRQHFEKLG WNKVVAFQTR NPMHRAHREL TVRAARSQQA NVLIHPVVGM TKPGDIDHFT
     RVRVYKALLP RYPNGMAALA LLPLAMRMGG PREAIWHAII RKNHGATHFI VGRDHAGPGK
     NKNGKDHYGP YDAQVAVQKY SDELGITMVE FQEMIYIPDR DEYQPANEIA PGTHTANISG
     TELRNRLKTG KEIPAWFSYP EVVKVLREQN PLPAQKGFTI FLTGLLNSGK DQIAKALQVT
     LNQGGGRSVS LLLGETVRHE LSSELGFSRE DRDKNVGRIA FVASELTRAG AAVIAAPIAP
     FDEARQKARE LVEKAGPFFL VHVATPLEYA EKTDKRGIYQ KARNGDIKGF TGVDDPYEAP
     AKADLVVNLE QQTVRSIVHQ IVLLLESQGL LDRL
//
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