ID A0A194VLF9_9PEZI Unreviewed; 574 AA.
AC A0A194VLF9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=VM1G_00510 {ECO:0000313|EMBL:KUI65006.1};
OS Valsa mali.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=105487 {ECO:0000313|EMBL:KUI65006.1};
RN [1] {ECO:0000313|EMBL:KUI65006.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-8 {ECO:0000313|EMBL:KUI65006.1};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-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}.
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DR EMBL; CM003098; KUI65006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VLF9; -.
DR OrthoDB; 159at2759; -.
DR UniPathway; UPA00097; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000078559; Chromosome 1.
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 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; 64476 MW; 8E0370929DB735CA CRC64;
MANPPHGGSL KDLLARDAPR NAELAAEAET LTAVVLTERQ LCDLELILNG GFSPLEGFMN
QKDYDGVVKE NRLENGLLFS MPITLDVSKA EIDELDLKPG KRVTLRDLRD DRNLAILTID
DIYKPDKVRE AKEVFGSDDE AHPAVKYLFH TAGDYYVGGK LEAVSRLQHY DFVDLRYTPA
EIRQHFDKLG WTRVVAFQTR NPMHRAHREL TVRAARSHHA NVLIHPVVGL TKPGDIDHFT
RVRVYKALIA RYPNGMAVLG LLPLAMRMGG PREAIWHAII RKNHGATHFI VGRDHAGPGK
NSKGVDFYGP YDAQYAVEKY RDELGIEVVP FQMMTYLPDS DEYAPVDTIP KEVRTLNISG
TELRSRLRSG REIPEWFSYP EVVKVLRESH PPRHQQGFTV FLTGYMNSGK DQIARALQVT
LNQQGGRSVS MLLGETVRAE LSSELGFSKE DRNRNIGRIA FVASELTRSG AAVIAAPIAP
FESSRQHARE LVEKYGDFYL VHIATSLEYC EKTDKRGIYA RARKGEIKGF TGVDDPYETP
AKADLVVDAE KQSVRSIVHQ IVLMLESQGL LDRL
//
