ID   Q1HQ66_BOMMO            Unreviewed;       425 AA.
AC   Q1HQ66;
DT   13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   SubName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000313|EMBL:ABF51275.1};
GN   Name=732910 {ECO:0000313|EnsemblMetazoa:NP_001040376.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000313|EMBL:ABF51275.1};
RN   [1] {ECO:0000313|EMBL:ABF51275.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Niu B.L., Meng Z.Q., Weng H.B., Shen W.F., He L.H., Zheng K.F., Ye S.T.,
RA   Lin T.B., Chen J.E.;
RT   "Blast silkworm EST database for functional genes.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [3] {ECO:0007829|PDB:4JA0}
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RX   PubMed=23553965; DOI=10.1002/prot.24296;
RA   Taschner M., Basquin J., Benda C., Lorentzen E.;
RT   "Crystal structure of the invertebrate bifunctional purine biosynthesis
RT   enzyme PAICS at 2.8 A resolution.";
RL   Proteins 81:1473-1478(2013).
RN   [4] {ECO:0000313|EnsemblMetazoa:NP_001040376.1}
RP   IDENTIFICATION.
RC   STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001040376.1};
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) 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 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; DQ443186; ABF51275.1; -; mRNA.
DR   RefSeq; NP_001040376.1; NM_001046911.1.
DR   PDB; 4JA0; X-ray; 2.80 A; A/B/C/D=1-425.
DR   PDBsum; 4JA0; -.
DR   AlphaFoldDB; Q1HQ66; -.
DR   SMR; Q1HQ66; -.
DR   STRING; 7091.Q1HQ66; -.
DR   PaxDb; 7091-BGIBMGA007935-TA; -.
DR   EnsemblMetazoa; NM_001046911.1; NP_001040376.1; LOC732910.
DR   GeneID; 732910; -.
DR   KEGG; bmor:732910; -.
DR   eggNOG; KOG2835; Eukaryota.
DR   HOGENOM; CLU_061495_1_0_1; -.
DR   InParanoid; Q1HQ66; -.
DR   OMA; WSDEQII; -.
DR   OrthoDB; 2898120at2759; -.
DR   BRENDA; 4.1.1.21; 890.
DR   UniPathway; UPA00074; UER00130.
DR   Proteomes; UP000005204; 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; 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_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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4JA0};
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:UP000005204}.
FT   DOMAIN          267..413
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
SQ   SEQUENCE   425 AA;  47344 MW;  245092F377D7EA1F CRC64;
     MSHPKQVGQY KLGKLLIEGK TKQVFDVPDQ PGYCLLLNKD RITAGDGVKA HDLEGKAAIS
     NQTNAKVFEI LKSAGIKTAF VKIASETAFL SKKCEMIPIE WVTRRLATGS FLKRNPGVPE
     GFRFTPPKQE TFFKDDANHD PQWSEEQIIS AKFNYNGLLI GRDEVDYMRK ATILIFEILE
     KAWALRDCAL IDMKIEFGVD TEGSIVLADV IDSDSWRLWP SGDKRLMVDK QVYRNLTTVT
     AADLDTVKRN FAWVKDQLDF LKPTIHHKVV VFMGSPADQE HCQKIAKAAR ELGLDVDLRV
     TSAHKATEET LRIMQQYEDT HGALVFIAVA GRSNGLGPVL SGNTSYPVIN CPPPSDKLVQ
     DIWSSLSVPS GLGCATVIYP DSAALMAAQI IGLQDYLVWG RLRSKQLDMA HSLRQADKKL
     RNQTA
//