ID A0A177E1R8_ALTAL Unreviewed; 575 AA.
AC A0A177E1R8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=AA0117_g1816 {ECO:0000313|EMBL:RYN81993.1}, CC77DRAFT_951586
GN {ECO:0000313|EMBL:OAG25678.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG25678.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG25678.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25678.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000291422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FERA 1177 {ECO:0000313|Proteomes:UP000291422};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL bioRxiv 0:0-0(2019).
RN [3] {ECO:0000313|EMBL:RYN81993.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FERA 1177 {ECO:0000313|EMBL:RYN81993.1};
RA Armitage A.D., Cockerton H.M., Sreenivasaprasad S., Woodhall J., Lane C.,
RA Harrison R.J., Clarkson J.P.;
RT "Genomics, evolutionary history and diagnostics of the Alternaria alternata
RT species group including apple and Asian pear pathotypes.";
RL J. ISSAAS 0:0-0(2019).
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; KV441469; OAG25678.1; -; Genomic_DNA.
DR EMBL; PDXD01000002; RYN81993.1; -; Genomic_DNA.
DR RefSeq; XP_018391099.1; XM_018535390.1.
DR STRING; 5599.A0A177E1R8; -.
DR GeneID; 29120984; -.
DR KEGG; aalt:CC77DRAFT_951586; -.
DR VEuPathDB; FungiDB:CC77DRAFT_951586; -.
DR OMA; MEMRYAG; -.
DR OrthoDB; 159at2759; -.
DR UniPathway; UPA00097; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR Proteomes; UP000291422; 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}; Reference proteome {ECO:0000313|Proteomes:UP000077248};
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 176..389
FT /note="Sulphate adenylyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01747"
FT REGION 1..171
FT /note="N-terminal"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT REGION 397..575
FT /note="Allosteric regulation domain; adenylyl-sulfate
FT kinase-like"
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 ACT_SITE 202
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 199..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 199
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 201
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 293..296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 297
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT BINDING 436..439
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 517
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 205
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 208
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
FT SITE 332
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03106"
SQ SEQUENCE 575 AA; 64308 MW; 144E53F0EC166443 CRC64;
MANAPHGGVL KDLIARDAPR RKELFDEAEK LPAIVLSERQ LCDLELILNG GFSPLEGFMN
QKDYDGVVAE NRLADGNLFS IPITLDVSKQ TIDEVGVKQG ARIALRDFRD DRNLAIITVD
DVYQPDKEKE AREVFDKDGD VAHPAIKYLY ETVNEYYVGG KLEAIDRLEH YDYVGLRYTP
AELRLHFDKL GWSKVVAFQT RNPMHRAHRE LTVRAARARQ ANVLIHPVVG LTKPGDIDHF
TRVRVYQALM PRYPNGMAVL ALLPLAMRMA GPREAIWHAI IRKNHGATHF IVGRDHAGPG
KNSKGVDFYG PYDAQDAVEK YRDELGIEVV PFLQMTYLPD SDEYKPKNEV EQGIKTLDIS
GTELRKRLRT GQEIPEWFSY PEVVRVLRES HPPRSQQGFT VFLTGYQNSG KDAIARALNV
TLNQQGGRSV SLLLGDTIRS ELSSELGFSR SDRDKNIARI SFVAAELTKA GAAAIVAPIA
PFEDSRKAAR QTVERFGSFY LIHVSTPLEH AEKTDKRGVY AKARAGEIKG FTGVDDPYEV
PTNADLTVDL STTNVRTAVH QIVLLLESQG LLTQL
//
