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Database: UniProt
Entry: A0A077ZCJ9_TRITR
LinkDB: A0A077ZCJ9_TRITR
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ID   A0A077ZCJ9_TRITR        Unreviewed;       429 AA.
AC   A0A077ZCJ9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Multifunctional protein ADE2 {ECO:0000313|EMBL:CDW57574.1};
GN   ORFNames=TTRE_0000586601 {ECO:0000313|EMBL:CDW57574.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW57574.1};
RN   [1] {ECO:0000313|EMBL:CDW57574.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW57574.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; HG806181; CDW57574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077ZCJ9; -.
DR   STRING; 36087.A0A077ZCJ9; -.
DR   UniPathway; UPA00074; UER00130.
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.
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          258..405
FT                   /note="PurE"
FT                   /evidence="ECO:0000259|SMART:SM01001"
SQ   SEQUENCE   429 AA;  48005 MW;  47EDD9D9FF540750 CRC64;
     MENCSKIADG KTKTILTIPD SDYVLVQSKD RITAFNAERQ HDLEGKAHLS NVTTSLVFQY
     LNSLGLKTHF VKMHSNTEFI ALRCVMIPIE WVARRLATGS FLKRNPNVSD GYRFSPPKVE
     LFYKDDSLGD PEWSRETLIE SGLVVSGVTI HAKEVDFMIE VTRTVFEILE RAWDSVGCTL
     VDMKVEFGVH AITGNIILAD VIDSDSWRLW PGGDKSLQVD KQFYRDLPIV TEEDLSTLIK
     KFSWVVEQLK NFTPPARSRV VVFMGSDKDS ECGEMIRSYL QKLGIHCDLR VASAHKGTVE
     TLKILAEYEG DLVPTVFIAV AGRSNGLGPI LSGNTSYPVI NCPPVEDASS MQDVWSSLRM
     PSGIGCVTVL NYEAAALHAA NVLALHDHYV WSRLRVNRLL NYISLMKADS KSHRDNDVKR
     DLVSRHSIG
//
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