ID F2U073_SALR5 Unreviewed; 416 AA.
AC F2U073;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 ORFNames=PTSG_11717 {ECO:0000313|EMBL:EGD80801.1};
OS Salpingoeca rosetta (strain ATCC 50818 / BSB-021).
OC Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Salpingoeca.
OX NCBI_TaxID=946362 {ECO:0000313|Proteomes:UP000007799};
RN [1] {ECO:0000313|Proteomes:UP000007799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50818 {ECO:0000313|Proteomes:UP000007799};
RA Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA Birren B.;
RT "Annotation of Salpingoeca rosetta.";
RL Submitted (AUG-2009) 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 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03125}.
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DR EMBL; GL832958; EGD80801.1; -; Genomic_DNA.
DR RefSeq; XP_004997362.1; XM_004997305.1.
DR AlphaFoldDB; F2U073; -.
DR STRING; 946362.F2U073; -.
DR EnsemblProtists; EGD80801; EGD80801; PTSG_11717.
DR GeneID; 16077959; -.
DR KEGG; sre:PTSG_11717; -.
DR eggNOG; KOG1355; Eukaryota.
DR InParanoid; F2U073; -.
DR OMA; FHHAKPI; -.
DR OrthoDB; 122722at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000007799; 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 PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF0; ADENYLOSUCCINATE SYNTHETASE; 1.
DR Pfam; PF00709; Adenylsucc_synt; 2.
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:UP000007799}.
FT ACT_SITE 17
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT ACT_SITE 45
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT ACT_SITE 147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134"
FT BINDING 16..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 17..20
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 42..45
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 44..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 136
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 150
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 289..295
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 293
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 321..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
FT BINDING 404..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03125"
SQ SEQUENCE 416 AA; 44846 MW; 727ACEA7590702FC CRC64;
MSSKSNVTAV IGLQWGDEGK GKLVDILAPG FGVVARFAGG NNAGHTVVID GTSYAFHLLP
SGIAHKSCTS VIGNGVVVHL PGLMKEIKAN TEKGPHLAGW ESRLKISNRA HVVLDIHQVV
DGLTETERGV SKIGTTKRGI GPTYSCKATR NGLRMCDLLG DEDHLRAKVA AVCGMYQRLF
PSITVDVEAE LAAIQQYLDT IRPLICDTFA EIHTALDSGV PILLEGLCVC VCVCVCVCVR
VCARDCVCVL LLCICPQRSS SIPSSLSIAT SLDQETGRYL QEKGHEYGTT TARPRRCGWL
DLVVINYACK LNGVTAICLT KLDVLDDLAE VKIGVSYTSP SNTYTCSMPA SQEEMAQCTV
EYITLPGWQQ SIEAVRKFEE LPANAKAYIA KIEELVGVPV RWIGVGKERE ATIHIA
//
