MET3_ASPCL
ID MET3_ASPCL Reviewed; 574 AA.
AC A1CJC1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=ACLA_034480;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027056; EAW09245.1; -; Genomic_DNA.
DR RefSeq; XP_001270671.1; XM_001270670.1.
DR AlphaFoldDB; A1CJC1; -.
DR SMR; A1CJC1; -.
DR STRING; 5057.CADACLAP00003141; -.
DR PRIDE; A1CJC1; -.
DR EnsemblFungi; EAW09245; EAW09245; ACLA_034480.
DR GeneID; 4702828; -.
DR KEGG; act:ACLA_034480; -.
DR VEuPathDB; FungiDB:ACLA_034480; -.
DR eggNOG; KOG0636; Eukaryota.
DR HOGENOM; CLU_022950_0_0_1; -.
DR OMA; LQHMIIR; -.
DR OrthoDB; 528280at2759; -.
DR UniPathway; UPA00140; UER00204.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Amino-acid biosynthesis; ATP-binding;
KW Cysteine biosynthesis; Cytoplasm; Methionine biosynthesis;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..574
FT /note="Sulfate adenylyltransferase"
FT /id="PRO_0000283676"
FT REGION 1..169
FT /note="N-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 170..394
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT REGION 395..574
FT /note="Allosteric regulation domain; adenylyl-sulfate
FT kinase-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 198
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 199
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT ACT_SITE 200
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 197..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 197
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 199
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 291..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 295
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT BINDING 434..437
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 451
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 477..478
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 516
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 203
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 206
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
FT SITE 330
FT /note="Induces change in substrate recognition on ATP
FT binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106"
SQ SEQUENCE 574 AA; 64189 MW; 7AF57F796B954C07 CRC64;
MSNPPHGGVL KDLLARDAPR HDQLETEAEQ LPAIVLTERQ LCDLELIMNG GFSPLEGFMN
QKDYDNVCEN VRLADGNLFS MPITLDVSKA VIDESQLKAG SRVTLRDFRD DRNLAILTID
DIYRPDKARE AKLVFGGDKE HPAIKFLNNT VQEFYIGGKV EAINKLNHYD YVALRYTPAE
LRVHFDKLGW SRVVAFQTRN PMHRAHRELT VRAARARQAN VLIHPVVGLT KPGDIDHFTR
VRAYQALLPR YPNGMAVLGL LGLAMRMGGP REAIWHAIIR KNHGATHFIV GRDHAGPGKN
SKGEEFYGPY DAQHAVEKYR EELGIEVVEF QQVTYLPDTD EYKPKDEVPA GVKTLDISGT
ELRNRLRTGA PIPEWFSYPE VVKILRESSR PRSTQGFTIF LTGYMNSGKD AIARALQVTL
NQQGGRSVSL LLGDTVRHEL SSELGFSRED RHTNVQRIAF VAGELTRAGA AVIAAPIAPY
EESRNAARDA VTQGGGNFFL VHVATPLEYC EKTDKRGIYA KARRGEIKGF TGVDDPYETP
SNAHLTVDVS KQTVRSIVHE IILMLETEGF FDRA
