ID A0A0M3HVK1_ASCLU Unreviewed; 426 AA.
AC A0A0M3HVK1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=AIRC domain-containing protein {ECO:0000313|WBParaSite:ALUE_0000700101-mRNA-1};
OS Ascaris lumbricoides (Giant roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0000700101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ALUE_0000700101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004672}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004747}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000256|ARBA:ARBA00011020}.
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DR AlphaFoldDB; A0A0M3HVK1; -.
DR WBParaSite; ALUE_0000700101-mRNA-1; ALUE_0000700101-mRNA-1; ALUE_0000700101.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000036681; Unplaced.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01416; SAICAR_synt_Ade5; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR PANTHER; PTHR43599:SF3; BIFUNCTIONAL PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE_PHOSPHORIBOSYLAMINOIMIDAZOLE SUCCINOCARBOXAMIDE SYNTHETASE; 1.
DR PANTHER; PTHR43599; MULTIFUNCTIONAL PROTEIN ADE2; 1.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF52255; N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE); 1.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000256|ARBA:ARBA00022793};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 266..413
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
SQ SEQUENCE 426 AA; 47382 MW; 477DCBD74C4582B0 CRC64;
MVPIIAYTEN DIKKVAEGKT KEIFTISNHD EYVLIRSKNR ITAFNAQRSN QIEGKGAIAN
DTTCNVFEYL NALGLKTHYV ERGAENEFVA LSCKMIPLEW VARRIATGSF LKRNPGVKEG
YRFNPPKLEV FFKDDANNDP QWSEEQILEH RFEFNGLKIG KREINSMKRQ TDVIFRVLEK
AWNAEGCTLI DLKVEFGVTK NGELVLADVI DNDSWRVWPA GDRRLQLDKQ FYRDLKQVDD
AALSKLKENY QTVAHITKNF IKPTCGRVVV LMGSTNDMEY ASRICDGCKT LGIAAIKRVS
SAHKTTENVL EIIAEYEGDS IPTVFVATAG RSNGLGLVIA GNSALPVINA PPLDADWAAK
DIWSSVHTPS GLGCSTVLGA DEAALAAAKT LAINDYMIFG RLLVKQFDNF AAISVSIQFS
VSEFQK
//
