ID A0A091HM04_CALAN Unreviewed; 587 AA.
AC A0A091HM04;
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=N300_12372 {ECO:0000313|EMBL:KFO96871.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO96871.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO96871.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO96871.1};
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; KL217603; KFO96871.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HM04; -.
DR STRING; 9244.A0A091HM04; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000054308; 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 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:UP000054308};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..141
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFO96871.1"
FT NON_TER 587
FT /evidence="ECO:0000313|EMBL:KFO96871.1"
SQ SEQUENCE 587 AA; 63635 MW; 7CEE6F9A23CC7982 CRC64;
LALLSVSDKT NLVDFAKSLN ALGLGLIASG GTANSLRDAG LPVRDVSDLT GFPEMLGGRV
KTLHPAVHAG ILARNIPEDN ADMNKQDFSL VRVVVCNLYP FVKTVSSPGV TVPEAVEKID
IGGVALLRAA AKNHARVTVV CDPGDYSAVA KEMAASGDKD TSMETRRLLA LKAFTHTAQY
DAAISDYFRK EYSKGVSQLP LRYGMNPHQS PAQLYTIRSK LPLTVLNGSP GFINLCDALN
AWQLVKELKQ ALGIPAAASF KHVSPAGAAV GIPLSEEEAK VCMVHDFHKT LTPLASAYAR
SRGADRMSSF GDFIALSDIC DVATAKIISR EVSDGVVAPG YEEEALKILS KKKNGGYCIL
QMDPHYEPDD TEIRTLYGLH LMQKRNDAVI NPSLFKNIVT KNKNLPESAV RDLIVASIAV
KYTQSNSVCY AKDGQVIGIG AGQQSRIHCT RLAGDKANNW WLRHHPHVLS MKFKAGVKRA
EISNAIDQYV TGTIGEGEDL VKWQAMFEEV PAQLTEAEKK QWIAKMTAVS LSSDAFFPFR
DNVDRAKRSG VQFIAAPSGS AADDIVIKAC DELGITLIHT NLRLFHH
//
