PUR2_PICAN
ID PUR2_PICAN Reviewed; 789 AA.
AC G8EWC8;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Bifunctional purine biosynthetic protein PUR2,5 {ECO:0000303|PubMed:24135445};
DE AltName: Full=OpPUR2,5 {ECO:0000303|PubMed:24135445};
DE Includes:
DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000305};
DE EC=6.3.4.13 {ECO:0000305|PubMed:24135445};
DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000305};
DE Short=GAR synthetase {ECO:0000250|UniProtKB:P20772};
DE Short=GARS {ECO:0000305};
DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000305};
DE Includes:
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000305};
DE EC=6.3.3.1 {ECO:0000250|UniProtKB:P20772};
DE AltName: Full=AIR synthase {ECO:0000305};
DE Short=AIR synthetase {ECO:0000250|UniProtKB:P20772};
DE Short=AIRS {ECO:0000305};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000305};
GN Name=PUR25 {ECO:0000303|PubMed:24135445};
GN Synonyms=PUR2,5 {ECO:0000303|PubMed:24135445};
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730 {ECO:0000312|EMBL:AEQ61912.1};
RN [1] {ECO:0000312|EMBL:AEQ61912.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24135445; DOI=10.1016/j.micres.2013.08.008;
RA Stoyanov A., Petrova P., Lyutskanova D., Lahtchev K.;
RT "Structural and functional analysis of PUR2,5 gene encoding bifunctional
RT enzyme of de novo purine biosynthesis in Ogataea (Hansenula) polymorpha CBS
RT 4732T.";
RL Microbiol. Res. 169:378-387(2014).
CC -!- FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine
CC biosynthesis pathway; contains phosphoribosylamine--glycine ligase
CC (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS)
CC activities. {ECO:0000305|PubMed:24135445}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000250|UniProtKB:P20772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC Evidence={ECO:0000250|UniProtKB:P20772};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 2/2. {ECO:0000305}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 2/2. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P20772}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR synthase
CC family. {ECO:0000305}.
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DR EMBL; JF967633; AEQ61912.1; -; Genomic_DNA.
DR PhylomeDB; G8EWC8; -.
DR BRENDA; 6.3.4.13; 2587.
DR UniPathway; UPA00074; UER00125.
DR UniPathway; UPA00074; UER00129.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IGI:UniProtKB.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IGI:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_00741; AIRS; 1.
DR HAMAP; MF_00138; GARS; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR InterPro; IPR000115; PRibGlycinamide_synth.
DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR InterPro; IPR020562; PRibGlycinamide_synth_N.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Purine biosynthesis.
FT CHAIN 1..789
FT /note="Bifunctional purine biosynthetic protein PUR2,5"
FT /id="PRO_0000454644"
FT DOMAIN 114..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 1..428
FT /note="GARS"
FT /evidence="ECO:0000255"
FT REGION 438..773
FT /note="AIRS"
FT /evidence="ECO:0000255"
FT BINDING 140..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 789 AA; 84886 MW; 12B8E4B3D6C50EA1 CRC64;
MEKINVLVVG NGGREHALVW KLAQSPWAKH IFVAPGNGGF SKLENVTSVP IGSSPSDFGS
LVDFATKHNV GLVIPGPEQP LVDGITTWFQ KAGIPVFGPS AKAARMEGSK TFSKDFMKKH
NIPTARYENF TDYEAAKQYI ANSSHNLVIK ASGIAAGKGV LIPANKQEAY EAIKEIMVNK
QFGSAGDEVV IEEFLEGDEL SILCISDGYS FVDLPPAQDH KRIGDGDTGL NTGGMGAYSP
APIGTPSLLE KIRKNILKPT IDGMRKDGYP MVGCLFVGVM VTPDGDPKVL EYNVRFGDPE
TQTVLPLLKS DLLELMLATV EHRLDSVDFQ VHADKYSTTV VVAAGGYPES YRKGDEITVK
EPLPENTFIF HAGTKEENGK VVTAGGRVIA ATAIADTLEE AVKKAYVGVD HISFKDKYNR
TDIAHRAFKE KPKNKVSLTY EDAGVSVDAG NQLVEKIKKS VKSTKRPGAD SEIGGFGGLF
DLQRAGYTDI NNTLLVAATD GVGTKLRVAQ IMDIHNTVGI DLVAMNVNDL VVQGAEPLMF
LDYFATAHLD IKVAADFVEG VADGCKLSGC ALVGGETSEM PGMYAPGHYD TNGTAVGAVL
KENILPKKDK MNAGDVLLGI ASDGVHSNGF SLIRKIIETT DYSYTDPAPW NPKSTIGEEV
LIPTRIYVKQ LLPATRRGLI LGLAHITGGG LVENIPRAIP DNLSAEVDMT TWNVPEIFKW
LGKTGGVPIN DILKTLNMGI GMVAIVKPEN VEEVIKVLKE AGETVYTIGK LVERKDLPGC
TIKNSEDLY
