PURCE_DICDI
ID PURCE_DICDI Reviewed; 997 AA.
AC Q54QE4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Bifunctional purine synthesis protein purC/E;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase;
DE EC=6.3.2.6;
DE AltName: Full=SAICAR synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase;
DE EC=4.1.1.21;
DE AltName: Full=AIR carboxylase;
DE Short=AIRC;
GN Name=purC/E; Synonyms=purC, purE; ORFNames=DDB_G0283987;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 76-98; 161-169; 643-654; 676-689; 712-720; 761-768 AND
RP 823-837, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Sumpton D., Ura S., Insall R.H.;
RL Submitted (OCT-2008) to UniProtKB.
CC -!- FUNCTION: Bifunctional enzyme involved in de novo IMP synthesis, an
CC essential step for de nove purine synthesis. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP +
CC L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-
CC 4-carboxamido]succinate + ADP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:22628, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58443,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:456216; EC=6.3.2.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SAICAR synthetase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR carboxylase
CC family. Class I subfamily. {ECO:0000305}.
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DR EMBL; AAFI02000058; EAL65481.1; -; Genomic_DNA.
DR RefSeq; XP_638800.1; XM_633708.1.
DR AlphaFoldDB; Q54QE4; -.
DR SMR; Q54QE4; -.
DR STRING; 44689.DDB0230088; -.
DR PaxDb; Q54QE4; -.
DR PRIDE; Q54QE4; -.
DR EnsemblProtists; EAL65481; EAL65481; DDB_G0283987.
DR GeneID; 8624324; -.
DR KEGG; ddi:DDB_G0283987; -.
DR dictyBase; DDB_G0283987; purC/E.
DR eggNOG; KOG2835; Eukaryota.
DR HOGENOM; CLU_300436_0_0_1; -.
DR InParanoid; Q54QE4; -.
DR OMA; WTIEGCV; -.
DR UniPathway; UPA00074; UER00130.
DR UniPathway; UPA00074; UER00131.
DR PRO; PR:Q54QE4; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; ISS:dictyBase.
DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; ISS:dictyBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006144; P:purine nucleobase metabolic process; ISS:dictyBase.
DR Gene3D; 3.30.1490.20; -; 1.
DR HAMAP; MF_01929; PurE_classI; 1.
DR HAMAP; MF_01928; PurK; 1.
DR HAMAP; MF_00137; SAICAR_synth; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR033747; PurE_ClassI.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR005875; PurK.
DR InterPro; IPR040686; PurK_C.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR028923; SAICAR_synt/ADE2_N.
DR InterPro; IPR018236; SAICAR_synthetase_CS.
DR Pfam; PF00731; AIRC; 1.
DR Pfam; PF02222; ATP-grasp; 1.
DR Pfam; PF17769; PurK_C; 1.
DR Pfam; PF01259; SAICAR_synt; 1.
DR SMART; SM01001; AIRC; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01162; purE; 1.
DR TIGRFAMs; TIGR01161; purK; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Decarboxylase; Direct protein sequencing; Ligase; Lyase;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..997
FT /note="Bifunctional purine synthesis protein purC/E"
FT /id="PRO_0000388376"
FT DOMAIN 732..927
FT /note="ATP-grasp"
FT REGION 1..?305
FT /note="SAICAR synthetase"
FT REGION 294..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION ?305..997
FT /note="AIR carboxylase"
FT REGION 518..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 768
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 779
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 807..810
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 815
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 880
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 897..898
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 898
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 997 AA; 108939 MW; 09B1DA8B64E07D00 CRC64;
MTTAINNNIV NKEFDLKDKT FLASGKTKTI YQLNKEDQYV LIESNSAITA GDGAKKDILP
NKDIYSTTTT VNNFKVLQLS GINTHFVKQV EPNAFIAKKC SMIPLEVIVR RLATGSYLKR
NTHVTEGTKF NPPLIEFTFK DDVQHDPLVT EQDILEMNLK IGGVPITSKL LSQTRHIATL
SFEALERAWQ SLDVTLVDFK VEFGITSQGE LILADVIDND SWRIWPKGDK TLMKDKQVYR
NLPSALNTPG ATPTTQSGPL LNTLSDQQLK MIEDNYAWVA TSTEKLVEFT AANLNNNNNN
NNNNSNNNNN NTSSTSRSNS LPNVPSITTT PTLHHHHHHH QQQQSGVGNN NNVNSGFQVQ
LNQPLVGIIM GSQSDWETMK LAANTLTTLG VPFETRIVSA HRTPDRLFEY AKTAKSRGLK
IVIAGAGGAA HLPGMVAALT PLPVFGVPVQ SKALSGVDSL LSIVQMPAGI PVGTVAIGAA
GATNAALLSA AVLAPYYPSI ELSLDLYRKK QTDAVAEIPV DNPTSTSTTT TTTTTSNATS
ILSAIHTSTI NSNTSSHNNN QQQQQQQQTI LPTQPTIINT PTPVRSSVSR SQSPLPSGNG
SSIISQEKTP LSTFVLSTCR PSALVLPPGS TIGILGGGQL ARMMAIAAAQ LGYKTHIFCP
ENDPSASHVA TYTTKSNYNN YSALDIFARQ VDVVTYEFEN IMVEPVEYLT KQVAVFPDPK
ILRTCQDRVL EKTFIQSLDI PTAQFQSVES FNDLKSAIEK IGYPAILKSN TMGYDGKGQV
KLTDQVDLEQ AWKKVTSETC ATKAILEQYI EFESEASVIV ARALDGTELT FPLVTNKHRN
HILRQTIAPA QLPEYIHKQA NEIGLKIARS NGLVGIIAVE LFVVKNNETG QYSLMVNELA
PRPHNSGHWT IEGCVTSQFE QLIRCVCGLP LGSVDFTKRI SEAEFIQQQI PPIVMTNLLG
QEVNGWEKIL QTKGSHLHIY AKGDAKEGRK MGHVTQQ
