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   27-MAR-2024, entry version 169.
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.Q05728; -.
DR   PaxDb; 3702-AT3G55010-2; -.
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; AT3G55010; PUR5.
DR   eggNOG; KOG0237; Eukaryota.
DR   HOGENOM; CLU_047116_0_0_1; -.
DR   InParanoid; Q05728; -.
DR   OMA; MTDYICV; -.
DR   OrthoDB; 729at2759; -.
DR   PhylomeDB; Q05728; -.
DR   BioCyc; ARA:AT3G55010-MONOMER; -.
DR   UniPathway; UPA00074; UER00129.
DR   PRO; PR:Q05728; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q05728; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd02196; PurM; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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   NCBIfam; TIGR00878; purM; 1.
DR   PANTHER; PTHR10520:SF12; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3; 1.
DR   PANTHER; PTHR10520; TRIFUNCTIONAL PURINE BIOSYNTHETIC PROTEIN ADENOSINE-3-RELATED; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
DR   Genevisible; Q05728; AT.
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
//