PUR5_ARATH
ID PUR5_ARATH Reviewed; 389 AA.
AC Q05728; Q9M2W5; Q9SV49;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic;
DE EC=6.3.3.1;
DE AltName: Full=AIR synthase;
DE Short=AIRS;
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
DE Flags: Precursor;
GN Name=PUR5; OrderedLocusNames=At3g55010; ORFNames=F28P10.10, T15C9.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Columbia; TISSUE=Leaf, and Stem;
RX PubMed=8108507; DOI=10.1104/pp.102.2.387;
RA Senecoff J.F., Meagher R.B.;
RT "Isolating the Arabidopsis thaliana genes for de novo purine synthesis by
RT suppression of Escherichia coli mutants. I. 5'-Phosphoribosyl-5-
RT aminoimidazole synthetase.";
RL Plant Physiol. 102:387-399(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC37341.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L12457; AAC37341.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; AL049655; CAB41083.1; -; Genomic_DNA.
DR EMBL; AL132970; CAB82696.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79327.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79328.1; -; Genomic_DNA.
DR EMBL; AY060585; AAL31210.1; -; mRNA.
DR EMBL; AY142054; AAM98318.1; -; mRNA.
DR PIR; JQ2256; JQ2256.
DR PIR; T47640; T47640.
DR RefSeq; NP_191061.1; NM_115359.3.
DR RefSeq; NP_974437.1; NM_202708.2.
DR AlphaFoldDB; Q05728; -.
DR SMR; Q05728; -.
DR BioGRID; 9983; 2.
DR IntAct; Q05728; 1.
DR STRING; 3702.AT3G55010.2; -.
DR PaxDb; Q05728; -.
DR PRIDE; Q05728; -.
DR ProteomicsDB; 226000; -.
DR EnsemblPlants; AT3G55010.1; AT3G55010.1; AT3G55010.
DR EnsemblPlants; AT3G55010.2; AT3G55010.2; AT3G55010.
DR GeneID; 824667; -.
DR Gramene; AT3G55010.1; AT3G55010.1; AT3G55010.
DR Gramene; AT3G55010.2; AT3G55010.2; AT3G55010.
DR KEGG; ath:AT3G55010; -.
DR Araport; AT3G55010; -.
DR TAIR; locus:2097203; AT3G55010.
DR eggNOG; KOG0237; Eukaryota.
DR HOGENOM; CLU_047116_0_0_1; -.
DR InParanoid; Q05728; -.
DR OMA; EPLFMTD; -.
DR OrthoDB; 1281175at2759; -.
DR PhylomeDB; Q05728; -.
DR BioCyc; ARA:AT3G55010-MON; -.
DR UniPathway; UPA00074; UER00129.
DR PRO; PR:Q05728; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q05728; baseline and differential.
DR Genevisible; Q05728; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IBA:GO_Central.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IBA:GO_Central.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_00741; AIRS; 1.
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 PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Ligase; Nucleotide-binding; Plastid;
KW Purine biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..389
FT /note="Phosphoribosylformylglycinamidine cyclo-ligase,
FT chloroplastic"
FT /id="PRO_0000029881"
FT REGION 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 389 AA; 41504 MW; F341E9D21E9286F0 CRC64;
MEARILQSSS SCYSSLYAVN RSRFSSVSSP KPFSVSFAQT TRTRTRVLSM SKKDGRTDKD
DDTDSLNYKD SGVDIDAGAE LVKRIAKMAP GIGGFGGLFP LGDSYLVAGT DGVGTKLKLA
FETGIHDTIG IDLVAMSVND IITSGAKPLF FLDYFATSRL DVDLAEKVIK GIVEGCRQSE
CALLGGETAE MPDFYAEGEY DLSGFAVGIV KKTSVINGKN IVAGDVLIGL PSSGVHSNGF
SLVRRVLARS NLSLKDALPG GSSTLGDALM APTVIYVKQV LDMIEKGGVK GLAHITGGGF
TDNIPRVFPD GLGAVIHTDA WELPPLFKWI QQTGRIEDSE MRRTFNLGIG MVMVVSPEAA
SRILEEVKNG DYVAYRVGEV VNGEGVSYQ
