ID A0A058ZQS2_EUCGR Unreviewed; 397 AA.
AC A0A058ZQS2;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 28-JAN-2026, entry version 50.
DE RecName: Full=phosphoribosylformylglycinamidine cyclo-ligase {ECO:0000256|ARBA:ARBA00013047};
DE EC=6.3.3.1 {ECO:0000256|ARBA:ARBA00013047};
DE AltName: Full=AIR synthase {ECO:0000256|ARBA:ARBA00032931};
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase {ECO:0000256|ARBA:ARBA00031908};
GN ORFNames=EUGRSUZ_L02454 {ECO:0000313|EMBL:KCW44133.1};
OS Eucalyptus grandis (Flooded gum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW44133.1};
RN [1] {ECO:0000313|EMBL:KCW44133.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW44133.1};
RA Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT "The genome of Eucalyptus grandis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAK2631780.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2631780.1};
RX PubMed=24919147; DOI=10.1038/nature13308;
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA van der Merwe K., Singh P., van Jaarsveld I., Silva-Junior O.B.,
RA Togawa R.C., Pappas M.R., Faria D.A., Sansaloni C.P., Petroli C.D.,
RA Yang X., Ranjan P., Tschaplinski T.J., Ye C.Y., Li T., Sterck L.,
RA Vanneste K., Murat F., Soler M., Clemente H.S., Saidi N., Cassan-Wang H.,
RA Dunand C., Hefer C.A., Bornberg-Bauer E., Kersting A.R., Vining K.,
RA Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.E., Liston A.,
RA Spatafora J.W., Dharmwardhana P., Raja R., Sullivan C., Romanel E.,
RA Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van de Peer Y., Rokhsar D.S., Schmutz J.;
RT "The genome of Eucalyptus grandis.";
RL Nature 510:356-362(2014).
RN [3] {ECO:0000313|EMBL:KAK2631780.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2631780.1};
RA Myburg A., Grattapaglia D., Tuskan G., Hellsten U., Hayes R., Grimwood J.,
RA Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D., Dubchak I.,
RA Poliakov A., Mizrachi E., Kullan A., Hussey S., Pinard D., Van D.,
RA Singh P., Van J., Silva-Junior O., Togawa R., Pappas M., Faria D.,
RA Sansaloni C., Petroli C., Yang X., Ranjan P., Tschaplinski T., Ye C.,
RA Li T., Sterck L., Vanneste K., Murat F., Soler M., Clemente H., Saidi N.,
RA Cassan-Wang H., Dunand C., Hefer C., Bornberg-Bauer E., Kersting A.,
RA Vining K., Amarasinghe V., Ranik M., Naithani S., Elser J., Boyd A.,
RA Liston A., Spatafora J., Dharmwardhana P., Raja R., Sullivan C.,
RA Romanel E., Alves-Ferreira M., Kulheim C., Foley W., Carocha V., Paiva J.,
RA Kudrna D., Brommonschenkel S., Pasquali G., Byrne M., Rigault P.,
RA Tibbits J., Spokevicius A., Jones R., Steane D., Vaillancourt R., Potts B.,
RA Joubert F., Barry K., Pappas G., Strauss S., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van D., Rokhsar D., Schmutz J.;
RT "WGS assembly of Eucalyptus grandis.";
RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:KAK2631780.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KAK2631780.1};
RA Myburg A.A., Grattapaglia D., Tuskan G.A., Hellsten U., Hayes R.D.,
RA Grimwood J., Jenkins J., Lindquist E., Tice H., Bauer D., Goodstein D.M.,
RA Dubchak I., Poliakov A., Mizrachi E., Kullan A.R., Hussey S.G., Pinard D.,
RA Van D.M., Singh P., Van J.I., Silva-Junior O.B., Togawa R.C., Pappas M.R.,
RA Faria D.A., Sansaloni C.P., Petroli C.D., Yang X., Ranjan P.,
RA Tschaplinski T.J., Ye C.Y., Li T., Sterck L., Vanneste K., Murat F.,
RA Soler M., Clemente H.S., Saidi N., Cassan-Wang H., Dunand C., Hefer C.A.,
RA Bornberg-Bauer E., Kersting A.R., Vining K., Amarasinghe V., Ranik M.,
RA Naithani S., Elser J., Boyd A.E., Liston A., Spatafora J.W.,
RA Dharmwardhana P., Raja R., Sullivan C., Romanel E., Alves-Ferreira M.,
RA Kulheim C., Foley W., Carocha V., Paiva J., Kudrna D.,
RA Brommonschenkel S.H., Pasquali G., Byrne M., Rigault P., Tibbits J.,
RA Spokevicius A., Jones R.C., Steane D.A., Vaillancourt R.E., Potts B.M.,
RA Joubert F., Barry K., Pappas G.J., Strauss S.H., Jaiswal P.,
RA Grima-Pettenati J., Salse J., Van D.P., Rokhsar D.S., Schmutz J.;
RL Submitted (JUL-2023) to the EMBL/GenBank/DDBJ databases.
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 + phosphate +
CC H(+); Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:137981, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00049057};
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 {ECO:0000256|ARBA:ARBA00004686}.
CC -!- SIMILARITY: Belongs to the AIR synthase family.
CC {ECO:0000256|ARBA:ARBA00010280}.
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DR EMBL; MU849159; KAK2631780.1; -; Genomic_DNA.
DR EMBL; KK199678; KCW44133.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A058ZQS2; -.
DR FunCoup; A0A058ZQS2; 592.
DR STRING; 71139.A0A058ZQS2; -.
DR Gramene; KCW44133; KCW44133; EUGRSUZ_L02454.
DR KEGG; egr:104430688; -.
DR eggNOG; KOG0237; Eukaryota.
DR InParanoid; A0A058ZQS2; -.
DR OMA; MTDYICV; -.
DR OrthoDB; 2018833at2759; -.
DR UniPathway; UPA00074; UER00129.
DR Proteomes; UP000030711; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 FunFam; 3.30.1330.10:FF:000001; Phosphoribosylformylglycinamidine cyclo-ligase; 1.
DR FunFam; 3.90.650.10:FF:000001; Phosphoribosylformylglycinamidine cyclo-ligase; 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000030711}.
FT DOMAIN 113..221
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 234..394
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
SQ SEQUENCE 397 AA; 42058 MW; 7166E92A615661C1 CRC64;
MNPSIGTKTA LKSLVVPTGP CSWNPHTSGS YQCKIPLDLN SRKFLQLPLN YGGTQARACA
KNVFRKYSIS AKMAESLTYK DAGVDIDAGS ELVRRIAKMA PGIGGFGGLF PLGDSYLVAG
TDGVGTKLKL AFETGIHETI GIDLVAMSVN DIVTSGAKPL FFLDYFATSH LDVDLAEKVI
KGIVDGCRLA DCALLGGETA EMPDFYAEGE YDISGFAVGI VKKDSVIDGK EIVAGDVIIG
LPSSGVHSNG FSLVRRVLAR SDLSLTDKLP GEAVTVGEAL MAPTVIYVNQ VLNLISKGGI
KGIAHITGGG FTDNIPRVFP KGLGATIYGD SWVVPPLFKW IQKVGNIEDS EMKRTFNMGI
GMVLVVSPEA ALRILGDDET TAYRIGDVVN GEGVRYS
//
