KEGG   ENZYME: 4.1.1.21Help
Entry
EC 4.1.1.21                 Enzyme                                 
Name
phosphoribosylaminoimidazole carboxylase;
5-phosphoribosyl-5-aminoimidazole carboxylase;
5-amino-1-ribosylimidazole 5-phosphate carboxylase;
AIR carboxylase;
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase;
ADE2;
class II PurE;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
BRITE hierarchy
Sysname
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase [5-amino-1-(5-phospho-D-ribosyl)imidazole-forming]
Reaction(IUBMB)
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2 [RN:R04209]
Reaction(KEGG)
Substrate
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate [CPD:C04751]
Product
5-amino-1-(5-phospho-D-ribosyl)imidazole [CPD:C03373];
CO2 [CPD:C00011]
Comment
While this is the reaction that occurs in vertebrates during purine biosynthesis, two enzymes are required to carry out the same reaction in Escherichia coli, namely EC 6.3.4.18, 5-(carboxyamino)imidazole ribonucleotide synthase and EC 5.4.99.18, 5-(carboxyamino)imidazole ribonucleotide mutase [3]. 5-Carboxyamino-1-(5-phospho-D-ribosyl)imidazole is not a substrate.
Pathway
Purine metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K01587  
phosphoribosylaminoimidazole carboxylase / phosphoribosylaminoimidazole-succinocarboxamide synthase
K11808  
phosphoribosylaminoimidazole carboxylase
Genes
HSA: 
10606(PAICS)
PTR: 
471236(PAICS)
PPS: 
100993147(PAICS)
GGO: 
101132763(PAICS)
PON: 
100190835(PAICS)
MMU: 
67054(Paics)
RNO: 
140946(Paics)
CFA: 
AML: 
100482672(PAICS)
FCA: 
101084705(PAICS)
BTA: 
404170(PAICS)
SSC: 
100521281(PAICS)
ECB: 
100058501(PAICS)
MDO: 
100012535(PAICS)
SHR: 
100923019(PAICS)
OAA: 
100086365
GGA: 
396534(PAICS)
MGP: 
100539860
TGU: 
100225152(PAICS)
ACS: 
100566555
XLA: 
379855(paics) 444677(paics.1)
XTR: 
100036662(paics.2) 100488155
DRE: 
321193(paics)
TRU: 
101073764
OLA: 
101171736
BFO: 
BRAFLDRAFT_117612
CIN: 
100177417
SPU: 
575874
DME: 
Dmel_CG3989(ade5)
DPO: 
Dpse_GA17827
DAN: 
Dana_GF20891
DER: 
Dere_GG19541
DPE: 
Dper_GL15026
DSE: 
Dsec_GM11535
DSI: 
Dsim_GD15919
DWI: 
Dwil_GK16398
DYA: 
Dyak_GE16201(Dyak_ade5)
DGR: 
Dgri_GH12574
DMO: 
Dmoj_GI14693
DVI: 
Dvir_GJ16601
AGA: 
AgaP_AGAP000180
AAG: 
AaeL_AAEL003606
CQU: 
CpipJ_CPIJ009002
AME: 
551966(ade5)
NVI: 
100122105(NV11180)
TCA: 
656066
API: 
100169501
PHU: 
Phum_PHUM430820
ISC: 
IscW_ISCW015611
CEL: 
CELE_B0286.3
CBR: 
CBG03675
TSP: 
Tsp_02239
NVE: 
NEMVE_v1g142804
HMG: 
100210246
TAD: 
TRIADDRAFT_56870
ATH: 
AT2G37690
ALY: 
ARALYDRAFT_321477
GMX: 
100787182 100812377
MTR: 
MTR_1g080500
CSV: 
101220975
RCU: 
RCOM_0607690
POP: 
POPTR_586808 POPTR_834540
VVI: 
100250122
OSA: 
4327345
DOSA: 
Os01t0199900-01(Os01g0199900)
SBI: 
SORBI_03g002690(SORBIDRAFT_03g002690)
ZMA: 
100501865
SMO: 
SELMODRAFT_121407
PPP: 
PHYPADRAFT_189585
CRE: 
CHLREDRAFT_196726
VCN: 
VOLCADRAFT_88132
OLU: 
OSTLU_33376
OTA: 
Ot09g00850
SCE: 
YOR128C(ADE2)
AGO: 
AGOS_ACR210C
ERC: 
Ecym_4634
KLA: 
KLLA0E02685g
LTH: 
KLTH0F15532g
PPA: 
PAS_chr3_0085
VPO: 
Kpol_440p3
ZRO: 
ZYRO0G04400g
CGR: 
CAGL0K10340g
NCS: 
NCAS_0H02150(NCAS0H02150)
NDI: 
NDAI_0C01500(NDAI0C01500)
TPF: 
TPHA_0J02670(TPHA0J02670)
TBL: 
TBLA_0A02680(TBLA0A02680)
TDL: 
TDEL_0D02460(TDEL0D02460)
KAF: 
KAFR_0D05120(KAFR0D05120)
DHA: 
DEHA2G13772g
PIC: 
PICST_81265(ADE2)
PGU: 
PGUG_04377
LEL: 
LELG_02667
CAL: 
CaO19.13327(ADE2) CaO19.5906(ADE2)
CTP: 
CTRG_02291
CDU: 
CD36_84460
COT: 
CORT_0C03210
YLI: 
YALI0B23188g
CLU: 
CLUG_04693
NCR: 
NCU03194
SMP: 
SMAC_02914
PAN: 
PODANSg5612
TTT: 
THITE_2122013
MTM: 
MYCTH_2106437
MGR: 
MGG_01256
FGR: 
FG10669.1
NHE: 
NECHADRAFT_57703
VAL: 
VDBG_04892
SSL: 
SS1G_09902
BFU: 
BC1G_15666
ANI: 
AN3626.2
NFI: 
NFIA_103710
AFM: 
AFUA_4G12600
AOR: 
AOR_1_552184(AO090009000333)
ANG: 
ANI_1_1076014(An01g08090)
AFV: 
AFLA_051370
ACT: 
ACLA_051590
PCS: 
Pc22g04460
CIM: 
CIMG_00790
CPW: 
CPC735_055130
PBL: 
PAAG_06211
URE: 
UREG_00756
ABE: 
ARB_04901
TVE: 
TRV_05910
AJE: 
HCAG_03809
PNO: 
SNOG_09661
PTE: 
PTT_18788
ZTR: 
MYCGRDRAFT_73277
TML: 
GSTUM_00003827001
SPO: 
SPCC1322.13(ade6)
CNE: 
CNE02500
CNB: 
CNBE2520
CGI: 
CGB_E3300W
PPL: 
POSPLDRAFT_90700
LBC: 
LACBIDRAFT_318305
MPR: 
MPER_11161
CCI: 
CC1G_11091
SCM: 
SCHCODRAFT_76354
UMA: 
UM00993.1
MGL: 
MGL_2675
PGR: 
PGTG_13944
MBR: 
MONBRDRAFT_34384 MONBRDRAFT_9068
PTI: 
PHATRDRAFT_56626
TPS: 
THAPSDRAFT_21670
PIF: 
PITG_09726
MPH: 
MLP_03890(purC)
 » show all
Taxonomy
Reference
1  [PMID:13672967]
  Authors
LUKENS LN, BUCHANAN JM.
  Title
Biosynthesis of the purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from 5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide.
  Journal
J. Biol. Chem. 234 (1959) 1799-805.
  Organism
Gallus gallus [GN:gga]
Reference
2  [PMID:7918411]
  Authors
Firestine SM, Poon SW, Mueller EJ, Stubbe J, Davisson VJ.
  Title
Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.
  Journal
Biochemistry. 33 (1994) 11927-34.
  Organism
Escherichia coli [GN:eco], Gallus gallus [GN:gga]
Reference
3  [PMID:9500840]
  Authors
Firestine SM, Misialek S, Toffaletti DL, Klem TJ, Perfect JR, Davisson VJ.
  Title
Biochemical role of the Cryptococcus neoformans ADE2 protein in fungal de novo purine biosynthesis.
  Journal
Arch. Biochem. Biophys. 351 (1998) 123-34.
  Organism
Escherichia coli [GN:eco], Gallus gallus [GN:gga], Cryptococcus neoformans
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9032-04-6
DBGET integrated database retrieval system