GenomeNet

Database: UniProt
Entry: G3SQM2_LOXAF
LinkDB: G3SQM2_LOXAF
Original site: G3SQM2_LOXAF 
ID   G3SQM2_LOXAF            Unreviewed;       592 AA.
AC   G3SQM2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Bifunctional purine biosynthesis protein ATIC {ECO:0000256|ARBA:ARBA00017905};
DE            EC=2.1.2.3 {ECO:0000256|ARBA:ARBA00012253};
DE            EC=3.5.4.10 {ECO:0000256|ARBA:ARBA00012712};
DE   AltName: Full=AICAR transformylase/inosine monophosphate cyclohydrolase {ECO:0000256|ARBA:ARBA00032307};
GN   Name=ATIC {ECO:0000313|Ensembl:ENSLAFP00000002107.3};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002107.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000002107.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002107.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000002107.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002107.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00035778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193;
CC         Evidence={ECO:0000256|ARBA:ARBA00035778};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-
CC         ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate;
CC         Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452,
CC         ChEBI:CHEBI:58467, ChEBI:CHEBI:58475;
CC         Evidence={ECO:0000256|ARBA:ARBA00000945};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145;
CC         Evidence={ECO:0000256|ARBA:ARBA00000945};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001252};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447;
CC         Evidence={ECO:0000256|ARBA:ARBA00001252};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC       1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004954}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC       from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004844}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the PurH family.
CC       {ECO:0000256|ARBA:ARBA00007667}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; G3SQM2; -.
DR   STRING; 9785.ENSLAFP00000002107; -.
DR   Ensembl; ENSLAFT00000002520.3; ENSLAFP00000002107.3; ENSLAFG00000002520.3.
DR   eggNOG; KOG2555; Eukaryota.
DR   GeneTree; ENSGT00390000004553; -.
DR   HOGENOM; CLU_016316_3_2_1; -.
DR   InParanoid; G3SQM2; -.
DR   OMA; WRVAKFV; -.
DR   TreeFam; TF105642; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0097294; P:'de novo' XMP biosynthetic process; IEA:Ensembl.
DR   GO; GO:0098761; P:cellular response to interleukin-7; IEA:Ensembl.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:Ensembl.
DR   CDD; cd01421; IMPCH; 1.
DR   Gene3D; 1.10.287.440; -; 1.
DR   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00139; PurH; 1.
DR   InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR   InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR002695; PurH-like.
DR   NCBIfam; TIGR00355; purH; 1.
DR   PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR   PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..146
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   592 AA;  64622 MW;  6D2DF52A34912DD6 CRC64;
     MAPASLALFS VSDKTGLVEF ARNLTSVGLN LVASGGTAKA LRDAGLTVRD VSELTGFPEM
     LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFDLIRVVV CNLYPFVKTV ASPDVTVEAA
     VEQIDIGGVT LLRAAAKNHA RVTVVCDPED YAAVSAEMQS SNSRDTSLEA RRQLALKAFT
     HTAQYDEAIS DYFRKQYSKG VSQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL
     CDALNAWQLV KELKEALGVP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS
     AAYARARGAD RMSSFGDFIA LSDVCDVPTA KIISREVSDG IVAPGYEEEA LKILSKKKNE
     NYCVLQMDQT YKPDENEVRT LFGLRLSQKR NNGVIDRSLF SNVVTKNKEL PESALRDLIV
     ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS RIHCTRLAGD KANYWWLRHH PRVLSMKFKT
     GVKRAEISNA IDQYVTGTIG EDEDLVKWKA LFEEVPELLT EAEKKDWIGK LSEVSVSSDA
     FFPFRDNVDR AKRSGVAYIA APSGSAADQV VIEACDELGI ILVHTSLRLF HH
//
DBGET integrated database retrieval system