Entry
Name
2-keto-3-deoxy-L-rhamnonate aldolase;
KDR aldolase;
2-dehydro-3-deoxyrhamnonate aldolase;
2-keto-3-deoxy acid sugar aldolase;
YfaU;
2-dehydro-3-deoxy-L-rhamnonate (S)-lactaldehyde lyase (pyruvate-forming);
2-dehydro-3-deoxy-L-rhamnonate (R)-lactaldehyde lyase (pyruvate-forming)
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
BRITE hierarchy
Sysname
2-dehydro-3-deoxy-L-rhamnonate (S)-lactaldehyde-lyase (pyruvate-forming)
Reaction(IUBMB)
2-dehydro-3-deoxy-L-rhamnonate = pyruvate + (S)-lactaldehyde [RN:
R02261 ]
Reaction(KEGG)
Substrate
2-dehydro-3-deoxy-L-rhamnonate [CPD:
C03979 ]
Product
Comment
Requires Mg2+ for activity. The enzyme can also use 2-oxo-3-deoxy-L-mannonate, 2-oxo-3-deoxy-L-lyxonate and 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) as substrates [2].
History
EC 4.1.2.53 created 2013
Pathway
ec00051 Fructose and mannose metabolism
ec01120 Microbial metabolism in diverse environments
Orthology
K12660 2-dehydro-3-deoxy-L-rhamnonate aldolase
K18339 2-keto-3-deoxy-L-rhamnonate aldolase
Genes
DHA : DEHA2C17688g DEHA2E00660g DEHA2E01056g DEHA2G19448g
PIC : PICST_57832 PICST_64442
PGU : PGUG_00213 PGUG_03287 PGUG_03590
CTEN : 18249052(PSN45_000412) 18249123(PSN45_000860) 18249645(PSN45_002893) 18249796(PSN45_004018) 18250726(PSN45_004012)
PPA : PAS_chr1-1_0356 PAS_chr4_0341 PAS_chr4_0577
BNN : FOA43_001684 FOA43_001969 FOA43_001972
OPA : HPODL_01988 HPODL_05174
YLI : 2906980(YALI2_C00616g)
NTE : NEUTE1DRAFT69855(NEUTE1DRAFT_69855)
SMP : 10805509(SMAC4_07611)
FPOA : FPOAC1_001913 FPOAC1_003306
FVN : FVRRES_02153 FVRRES_03650
FOX : FOXG_05126 FOXG_17406
FFC : NCS54_00716900 NCS54_01504200
FMU : J7337_005910 J7337_010252
TATV : 25775784(TrAtP1_012354)
TASP : 36617238(TrAFT101_010355)
MAW : 90962608(J3458_005824)
MBRN : 26241378(G6M90_00g077570)
PLJ : 28886674(PLICBS_002006)
VDA : VDAG_00197 VDAG_09650
CDET : 87948000(CDEST_11500)
PFY : PFICI_08543 PFICI_12530
SSL : SS1G_00980 SS1G_10069
BFU : BCIN_03g00250 BCIN_14g02460
PSCO : LY89DRAFT_47291 LY89DRAFT_706903
PTRR : 6349819(PtrM4_002100)
ADAC : 96083697(ACET3X_003375)
CCAC : CcaHIS019_0607320(CcaverHIS019_0607320)
ECOO : ECRM13514_3001(yfaU)
ECOH : ECRM13516_2945(yfaU)
EDJ : ECDH1ME8569_2181(yfaU)
ECOI : ECOPMV1_02406(rhmA)
KLW : DA718_08655 DA718_10630
RTG : NCTC13098_02025(rhmA)
CFAR : CI104_17360 CI104_21505
CTEL : GBC03_08335 GBC03_13105
METY : MRY16398_16460(rhmA)
AMOB : HG15A2_21150(garL_2)
SDYN : Mal52_00510(rhmA_1)
ABAC : LuPra_05015(rhmA_2)
PSEZ : HME7025_02113(rhmA)
AANR : KCTC52924_02763(rhmA)
PFAA : MM59RIKEN_19820(rhmA)
BPRO : PMF13cell1_02925(rhmA)
VRM : 44547418_01808(rhmA)
PAUS : NCTC13651_02073(rhmA)
BALA : DSM104299_03708(garL)
LMAJ : GKN94_06365 GKN94_07915
» show all
Taxonomy
Reference
Authors
Rakus JF, Fedorov AA, Fedorov EV, Glasner ME, Hubbard BK, Delli JD, Babbitt PC, Almo SC, Gerlt JA
Title
Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase.
Journal
Sequence
Reference
Authors
Rea D, Hovington R, Rakus JF, Gerlt JA, Fulop V, Bugg TD, Roper DI
Title
Crystal structure and functional assignment of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.53
ExPASy - ENZYME nomenclature database: 4.1.2.53
LinkDB
All DBs