ID A7T273_NEMVE Unreviewed; 421 AA.
AC A7T273;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=PurE domain-containing protein {ECO:0000259|SMART:SM01001};
GN ORFNames=NEMVEDRAFT_v1g142804 {ECO:0000313|EMBL:EDO29941.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO29941.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO29941.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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 C-terminal section; belongs to the AIR carboxylase
CC family. Class II subfamily. {ECO:0000256|ARBA:ARBA00010478}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000256|ARBA:ARBA00011020}.
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DR EMBL; DS470211; EDO29941.1; -; Genomic_DNA.
DR RefSeq; XP_001622041.1; XM_001621991.1.
DR AlphaFoldDB; A7T273; -.
DR STRING; 45351.A7T273; -.
DR EnsemblMetazoa; EDO29941; EDO29941; NEMVEDRAFT_v1g142804.
DR GeneID; 5500615; -.
DR KEGG; nve:5500615; -.
DR eggNOG; KOG2835; Eukaryota.
DR HOGENOM; CLU_061495_1_0_1; -.
DR InParanoid; A7T273; -.
DR OMA; WSDEQII; -.
DR OrthoDB; 2898120at2759; -.
DR PhylomeDB; A7T273; -.
DR UniPathway; UPA00074; UER00130.
DR Proteomes; UP000001593; Unassembled WGS sequence.
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; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central.
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_02045; PurE_classII; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR033626; PurE_classII.
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.
DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 263..410
FT /note="PurE"
FT /evidence="ECO:0000259|SMART:SM01001"
SQ SEQUENCE 421 AA; 46126 MW; 00B156D20A8386CB CRC64;
MKIGEKIIEG KTKIVYALPD SPDGNHVLLK SKDKITAFDA TRKDEMSGKA AQSTATTCAI
FEMLKACGLK THFVKRCESD PEAFIGIACE MIPLEVVCRR IATGSFLKRY PGVKEGYRFT
PPKQEFFLKD DAQHDPFWTY EQCVEAAFEI GGKKIGKHEL DIMSESAIAI FEIIERAWAT
VDVALVDMKI EFGVNRKTGE LMLADVVDND SWRIWPSGDK RLMRDKQVYR NLPEVTPEAL
EQVKKNYAWV AGESQKLNKH NPGHVVVFMG SASDIDHCKK IEAALKSFNV PCDLRVSSAH
KGSEDTLKVL RVYEGQGVPI VIIAVAGRSN GLGPVLSGNT SFPVINCPPV SSGWGAEDVW
SSLRLPSGLG CTTALNPDGA AAAAAQILGL HDHIIWGSLR AKRLNMAVGL READDKLVSG
K
//
