ID A0A2X0MM58_9BASI Unreviewed; 431 AA.
AC A0A2X0MM58;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520};
DE Short=AMPSase {ECO:0000256|HAMAP-Rule:MF_03125};
DE Short=AdSS {ECO:0000256|HAMAP-Rule:MF_03125};
DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520};
DE AltName: Full=IMP--aspartate ligase {ECO:0000256|HAMAP-Rule:MF_03125};
GN Name=BQ5605_C012g06989 {ECO:0000313|EMBL:SGY16788.1};
GN ORFNames=BQ5605_C012G06989 {ECO:0000313|EMBL:SGY16788.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY16788.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY16788.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC commited step in the biosynthesis of AMP from IMP. {ECO:0000256|HAMAP-
CC Rule:MF_03125}.
CC -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC committed step in the biosynthesis of AMP from IMP.
CC {ECO:0000256|ARBA:ARBA00003779}.
CC -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC nucleotide biosynthesis. {ECO:0000256|RuleBase:RU000520}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC ChEBI:CHEBI:58189; EC=6.3.4.4; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03125, ECO:0000256|RuleBase:RU000520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03125};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03125};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03125,
CC ECO:0000256|RuleBase:RU000520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_03125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_03125, ECO:0000256|RuleBase:RU000520}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQNC01000014; SGY16788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0MM58; -.
DR STRING; 796604.A0A2X0MM58; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000249464; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 3.40.440.10; Adenylosuccinate Synthetase, subunit A, domain 1; 1.
DR Gene3D; 1.10.300.10; Adenylosuccinate Synthetase, subunit A, domain 2; 1.
DR Gene3D; 3.90.170.10; Adenylosuccinate Synthetase, subunit A, domain 3; 1.
DR HAMAP; MF_00011; Adenylosucc_synth; 1.
DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd.
DR InterPro; IPR033128; Adenylosuccin_syn_Lys_AS.
DR InterPro; IPR042109; Adenylosuccinate_synth_dom1.
DR InterPro; IPR042110; Adenylosuccinate_synth_dom2.
DR InterPro; IPR042111; Adenylosuccinate_synth_dom3.
DR InterPro; IPR001114; Adenylosuccinate_synthetase.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00184; purA; 1.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03125};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03125};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03125};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_03125}; Reference proteome {ECO:0000313|Proteomes:UP000249464}.
FT ACT_SITE 18
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT ACT_SITE 46
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134"
FT BINDING 17..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 18..21
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 43..46
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 45..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 45
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 138
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 152
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 229
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 244
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 304..310
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 308
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 310
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 336..338
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 419..421
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
SQ SEQUENCE 431 AA; 47200 MW; 95A55F1329670310 CRC64;
MVLQPDKVAV VLGSQWGDEG KGKLVDILAA EADICARCAG GNNAGHTIVA NVNGVKTHFD
FHLLPSGLVN PKCTAFIGNG VVVHVPAFFE ELDKLTKKGL NCDGRLLLSD RAHLVFDFHQ
IVDGLKEVEL GGSSIGTTKK GIGPAYSSKA SRSGLRVHHL FDEEAFATKF RKLVEGRFKR
YGHFEYDTEG EILRYKELAA RLKPYVVDGP TFLHKAMLEK KRILVEGANA LMLDMDFGTY
PFVTSSPTGI GGVCTGLGVP PRAIGEVVGV VKAYTTRVGA GPFPTEQLNS VGEHLQEVGA
EYGVTTGRRR RCGWLDLVVL KYSHLINGYT ALNLTKLDVL DQLPSLKVAT GYHLNGKPLE
AYFPADLDQL AQVEVQYVEL PGWQTSIANI TKFEDLPENC RKYIEFIEDF IGVKIGWIGT
GPARESMIRR L
//
