PURA2_CHICK
ID PURA2_CHICK Reviewed; 451 AA.
AC Q5ZJL5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Adenylosuccinate synthetase isozyme 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AMPSase 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=AdSS 2 {ECO:0000255|HAMAP-Rule:MF_03127};
DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, acidic isozyme {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=Adenylosuccinate synthetase, liver isozyme {ECO:0000255|HAMAP-Rule:MF_03127};
DE Short=L-type adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_03127};
DE AltName: Full=IMP--aspartate ligase 2 {ECO:0000255|HAMAP-Rule:MF_03127};
GN Name=ADSS2 {ECO:0000255|HAMAP-Rule:MF_03127};
GN Synonyms=ADSS {ECO:0000255|HAMAP-Rule:MF_03127}; ORFNames=RCJMB04_17e23;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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:0000250|UniProtKB:P46664}.
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:0000255|HAMAP-
CC Rule:MF_03127};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03127};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03127};
CC -!- ACTIVITY REGULATION: Inhibited competitively by AMP and IMP and non-
CC competitively by fructose 1,6-bisphosphate.
CC {ECO:0000250|UniProtKB:P46664}.
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_03127}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03127}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03127}.
CC Mitochondrion {ECO:0000250|UniProtKB:A4Z6H1}.
CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_03127}.
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DR EMBL; AJ720419; CAG32078.1; -; mRNA.
DR RefSeq; NP_001026692.1; NM_001031521.1.
DR AlphaFoldDB; Q5ZJL5; -.
DR SMR; Q5ZJL5; -.
DR STRING; 9031.ENSGALP00000017386; -.
DR GeneID; 428579; -.
DR KEGG; gga:428579; -.
DR CTD; 159; -.
DR VEuPathDB; HostDB:geneid_428579; -.
DR eggNOG; KOG1355; Eukaryota.
DR HOGENOM; CLU_029848_3_0_1; -.
DR InParanoid; Q5ZJL5; -.
DR OrthoDB; 1276527at2759; -.
DR PhylomeDB; Q5ZJL5; -.
DR Reactome; R-GGA-421203; De novo synthesis of AMP.
DR UniPathway; UPA00075; UER00335.
DR PRO; PR:Q5ZJL5; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central.
DR CDD; cd03108; AdSS; 1.
DR Gene3D; 1.10.300.10; -; 1.
DR Gene3D; 3.40.440.10; -; 1.
DR Gene3D; 3.90.170.10; -; 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 PANTHER; PTHR11846; PTHR11846; 1.
DR Pfam; PF00709; Adenylsucc_synt; 1.
DR SMART; SM00788; Adenylsucc_synt; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00184; purA; 1.
DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..451
FT /note="Adenylosuccinate synthetase isozyme 2"
FT /id="PRO_0000398882"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT ACT_SITE 63
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 34..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 35..38
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 60..63
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 62..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 62
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 157
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 171
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 250
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 265
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 325..331
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 329
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 331
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 357..359
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
FT BINDING 439..442
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03127"
SQ SEQUENCE 451 AA; 49455 MW; 7FA047778EE32606 CRC64;
MAEHGAPAPA IPNGGCAARL PGNKVTVVLG AQWGDEGKGK VVDLLAQDAD IVCRCQGGNN
AGHTVVVDSV EYDFHLLPSG IINPKVTAFI GNGVVIHLPG LFEETEKNLK KGKGLEGWEK
RLVISDRAHI VFDFHQAADG IQEQQRQEQA GKNLGTTKKG IGPVYSSKAA RSGLRMCDLV
SDFDEFSERF KVLANQYKAI YPTLEIDIEG ELKKLKAYME KVKPMVKDGV YFMYEALHGP
PKKILVEGAN AALLDIDFGT YPFVTSSNCT VGGVCTGLGM PPQNVGEVYG VVKAYTTRVG
IGAFPTEQDN EIGELLQMRG KEFGVTTGRK RRCGWLDLVQ LRYAYMINGF TALALTKLDI
LDVFPEIKVG VAYKLDGEVI PHFPANHEVL SKVEVKYETL PGWDTDISNA RTFDELPVNA
QNYVRFIEME LGVPVKWIGV GKSRESMIQL F
