ID A0A3P8YBA7_ESOLU Unreviewed; 474 AA.
AC A0A3P8YBA7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Adenylosuccinate synthetase isozyme 2 {ECO:0000256|HAMAP-Rule:MF_03127};
DE Short=AMPSase 2 {ECO:0000256|HAMAP-Rule:MF_03127};
DE Short=AdSS 2 {ECO:0000256|HAMAP-Rule:MF_03127};
DE EC=6.3.4.4 {ECO:0000256|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, acidic isozyme {ECO:0000256|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, liver isozyme {ECO:0000256|HAMAP-Rule:MF_03127};
DE Short=L-type adenylosuccinate synthetase {ECO:0000256|HAMAP-Rule:MF_03127};
DE AltName: Full=IMP--aspartate ligase 2 {ECO:0000256|HAMAP-Rule:MF_03127};
GN Name=ADSS {ECO:0000256|HAMAP-Rule:MF_03127};
GN Synonyms=ADSS2 {ECO:0000256|HAMAP-Rule:MF_03127};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000013366.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000013366.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000013366.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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_03127}.
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_03127, ECO:0000256|RuleBase:RU000520};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03127};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03127};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000256|HAMAP-Rule:MF_03127,
CC ECO:0000256|RuleBase:RU000520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_03127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03127}.
CC Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000256|HAMAP-Rule:MF_03127, ECO:0000256|RuleBase:RU000520}.
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DR AlphaFoldDB; A0A3P8YBA7; -.
DR STRING; 8010.ENSELUP00000013366; -.
DR Ensembl; ENSELUT00000038483.2; ENSELUP00000013366.2; ENSELUG00000013493.2.
DR GeneTree; ENSGT00390000015553; -.
DR InParanoid; A0A3P8YBA7; -.
DR OMA; FHHAKPI; -.
DR OrthoDB; 122722at2759; -.
DR UniPathway; UPA00075; UER00335.
DR Proteomes; UP000265140; LG05.
DR Bgee; ENSELUG00000013493; Expressed in ovary and 14 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; 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 HAMAP; MF_03127; Adenylosucc_synth_vert_acid; 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; IPR027529; AdSS_2_vert.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00184; purA; 1.
DR PANTHER; PTHR11846; ADENYLOSUCCINATE SYNTHETASE; 1.
DR PANTHER; PTHR11846:SF13; ADENYLOSUCCINATE SYNTHETASE ISOZYME 2; 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_03127};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_03127};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_03127};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03127};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03127}; Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03127};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_03127}; Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10134"
FT BINDING 57..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 58..61
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 83..86
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 85..87
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 180
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 194
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 273
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 288
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 348..354
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 352
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 354
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 380..382
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
FT BINDING 462..465
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03127"
SQ SEQUENCE 474 AA; 51870 MW; 934D8FB2D8732D38 CRC64;
LAHGSQAAAG RRTQTVMSES RSKDAPQNGA AHSTIEPHVA KPKVGNRVTV VLGAQWGDEG
KGKVVDLLAQ DADIVCRCQG GNNAGHTVVV DSVEYDFHLL PSGIINPKVT AFIGNGVVIH
LPGLFEEAEK NVRKGKSLEG WDKRLIISDR AHIVFDFHQA VDGVQEQQRQ EQAGKNLGTT
KKGIGPVYSA KAARSGLRIC DLMSDFTQFS ERFKVLASQY QSMYPSLKID VDGELTRLKV
SYSSLKPMVR DGVFYMYEAL HGPPKNILVE GANAALLDID FGTYPFVTSS NCTVGGVCTG
LGMPPQNVGE VYGVVKAYTT RVGIGAFPSE QFNDIGDLLQ TRGKEVGVTT GRKRRCGWLD
LVLIKYAHMI NGFTALALTK LDILDVFPEI KVGVSYSVDG ENIPHFPANQ EVLQKVEVQY
DTLPGWKSDT SATRTFDELP ENAQKYIRYI EDHLGVPVKW IGVGKSRESM IRIF
//
