ID A0A091LJH9_CATAU Unreviewed; 589 AA.
AC A0A091LJH9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
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};
DE Flags: Fragment;
GN ORFNames=N323_12195 {ECO:0000313|EMBL:KFP55422.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP55422.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP55422.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP55422.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KL323336; KFP55422.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LJH9; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000053745; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
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 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:UP000053745};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..139
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP55422.1"
FT NON_TER 589
FT /evidence="ECO:0000313|EMBL:KFP55422.1"
SQ SEQUENCE 589 AA; 64575 MW; 030D8598144F7315 CRC64;
LALLSVSDKT SLVEFAKSLN ALGLGLIASG GTAKSLRDAG FADVSDLTGF PEMLGGRVKT
LHPAVHAGIL ARNIPEDNAD MNKQDFSLVR VVVCNLYPFV KTVSSPDVTV QEAVEKIDIG
GVALLRAAAK NHARVTVVCD PADYSAVAKE MATSRDKDTS METRRHLALK AFTHTAQYDA
AISDYFRKEY SKGVSQLPLR YGMNPHQSPA QLYTMRSKLP LTVVNGSPGF INLCDALNAW
QLVKELKQAL GRTSKRFWFE CPGLYFPLGA AVGIPLSEEE AQVCMVHDFH KTLTPLASAY
ARSRGADRMS SFGDFIALSD ICDVATAKII SREVSDGVVA PGYEEEALKI LAKKKNGGYC
VLQMDPHYEP DDSEIRTLYG LHLMQKRNNA VIDRSLFKNI VTKNKNLPES AVRDLIVASI
AVKYTQSNSV CYAKDGQVIG IGAGQQSRIH CTRLAGDKAN NWWLRHHPRV LSMKFKAGVK
RAEISNAIDQ YVTGTIGEDE DLVKWQAMFE EVPAQLTEAE KKQWIAKLTA VSLSSDAFFP
FRDNVDRAKR SGVQFIAAPS GSAADEVVIE ACNELGITLI HTNLRLFHH
//
