Entry
Name
L-rhamnose isomerase;
rhamnose isomerase;
L-rhamnose ketol-isomerase
Class
Isomerases;
Intramolecular oxidoreductases;
Interconverting aldoses and ketoses, and related compounds
BRITE hierarchy
Sysname
L-rhamnose aldose-ketose-isomerase
Reaction(IUBMB)
L-rhamnopyranose = L-rhamnulose [RN:
R02437 ]
Reaction(KEGG)
Substrate
Product
Comment
Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose [2].
History
EC 5.3.1.14 created 1965
Pathway
ec00051 Fructose and mannose metabolism
ec01120 Microbial metabolism in diverse environments
Orthology
K01820 L-rhamnose isomerase / sugar isomerase
Genes
ECOO : ECRM13514_4971(rhaA)
ECOH : ECRM13516_4751(rhaA)
ECW : EcE24377A_4434(rhaA)
EDJ : ECDH1ME8569_3773(rhaA)
ECOI : ECOPMV1_04263(rhaA)
RTG : NCTC13098_07122(rhaA)
KIE : NCTC12125_03699(rhaA)
AHN : NCTC12129_00079(rhaA)
METY : MRY16398_55510(rhaA)
MPHG : MPHASIOC01_000207(rhaA)
YPG : YpAngola_A0744(rhaA)
YPI : YpsIP31758_3756(rhaA)
SFJ : SAMEA4384070_2468(rhaA)
SOF : NCTC11214_05018(rhaA)
PARL : PEC302110_35160(rhaA)
SLIG : GTU79_04185 GTU79_26610
PHEI : NCTC12003_02667(rhaA)
VIB : VspSTUT11_23690(rhaA_1) VspSTUT11_45700(rhaA_2)
CATE : C2869_03860(rhaI) C2869_06305(rhaA)
AEL : NCTC12917_03314(rhaA)
SOK : D0B54_18775(rhaI) D0B54_22420
CDIZ : CEDIAZO_01240(rhaA)
RGU : A4W93_00190 A4W93_06470
MESU : LHFGNBLO_000180(rhaI)
SMEL : SM2011_c02321(rhaI)
ALF : CFBP5473_13775(rhaI)
ASAL : CFBP5507_21540(rhaI)
RIR : BN877_II0501 BN877_p0480
RPUS : CFBP5875_16375(rhaI)
ALEG : CFBP4996_17050(rhaI)
RTR : RTCIAT899_PC02900(rhaI)
RLW : RlegWSM1455_30620(rhaI)
RBW : RLCC275e_29460(rhaI)
NEN : NCHU2750_49910(rhaA)
BIO : BR141012304_20015 BR141012304_21203
RLI : RLO149_c023140(rhaI)
LVS : LOKVESSMR4R_01195(rhaA)
NOV : TQ38_019065 TQ38_027605
OBG : Verru16b_01319(rhaA)
OBT : OPIT5_04955 OPIT5_30100
PUO : RZN69_01430 RZN69_06560
PND : Pla175_49130(xylA_2)
CCOP : Mal65_00640(rhaA_1) Mal65_14880(rhaA_2)
MCAD : Pan265_04640(xylA_1)
VBC : C5Q97_03920 C5Q97_11855
ABAC : LuPra_01985(xylA_1)
BTHO : Btheta7330_04524(rhaA)
BCEL : BcellWH2_02086(rhaA)
DDB : E7747_00880 E7747_05720
COPR : Cop2CBH44_09450(rhaA)
PHER : prwr041_07150(rhaA)
POC : NCTC13071_01985(rhaA_1) NCTC13071_02368(rhaA_2)
ACOU : A5CBH24_07170(rhaA)
EST : DN752_13835 DN752_23370
AHAO : OM944_02905 OM944_18675
PSEZ : HME7025_01891(rhaA)
FGL : EM308_11965 EM308_15735
FPLU : NLG42_18755 NLG42_19700
SPON : HME9304_00210(rhaA) HME9304_00701
BSON : S101395_01707(rhaA)
BLEN : NCTC4824_04267(yulE)
LMOC : LMOSLCC5850_2857(rhaA)
LMW : LMOSLCC2755_2868(rhaA)
LMX : LMOSLCC2372_2927(rhaA)
LMZ : LMOSLCC2482_2865(rhaA)
LMON : LMOSLCC2376_2746(rhaA)
LMOS : LMOSLCC7179_2817(rhaA)
LMOO : LMOSLCC2378_2865(rhaA)
LMOY : LMOSLCC2479_2926(rhaA)
LMOT : LMOSLCC2540_2898(rhaA)
LMOA : LMOATCC19117_2859(rhaA)
LGZ : NCTC10812_00423(rhaA)
PPM : PPSC2_11285(xylA1) PPSC2_24735(rhaA)
PPO : PPM_2160(xylA1) PPM_4915(rhaA)
PPOL : X809_11610 X809_41290
PPQ : PPSQR21_022400 PPSQR21_050080(rhaA)
PPOY : RE92_01070 RE92_12550
PTA : HPL003_06590 HPL003_19715
POD : PODO_11135 PODO_17305
PAEF : R50345_11600 R50345_17450
PAEJ : H70737_11050 H70737_17260
PPEO : ABE82_11420 ABE82_25035
PKB : B4V02_00300 B4V02_13940
PAIH : ASL14_12730 ASL14_24900
PLEN : EIM92_15935(rhaI) EIM92_17135(rhaA)
PBK : Back11_02640(rhaA) Back11_34790
PRZ : GZH47_09485(rhaI) GZH47_25670(rhaA)
PLYC : GXP70_06930(rhaI) GXP70_22020(rhaA)
PNK : AASFL403_09260(rhaI)
PLZH : C0638_08555(rhaA) C0638_21810(rhaI)
COHN : KCTCHS21_31280(rhaA)
CHEB : HH215_05035(rhaA) HH215_28970(rhaI)
COHL : J4772_08155(rhaI) J4772_12530(rhaA)
SCP : HMPREF0833_10564(rhaA)
SMEN : SAMEA4412692_2136(rhaA)
EFAU : EFAU085_00206(rhaA)
EFU : HMPREF0351_10213(rhaA)
BPRO : PMF13cell1_02019(rhaA)
ACEL : acsn021_21660(rhaA)
ACHT : bsdcttw_22120(rhaA)
QDO : H9Q78_04975 H9Q78_13755
WHJ : H9Q79_06765 H9Q79_11620
CMIU : B1H56_07205 B1H56_08610
MTHO : MOTHE_c20720(xylA2)
CDIA : CaldiYA01_17440(rhaA)
SCHI : SCHIN_v1c08040(rhaA)
NFR : ERS450000_00785(xylA)
RKO : JWS14_17385(rhaI) JWS14_22340(rhaI)
SCX : AS200_06745 AS200_06770
SLE : sle_05960(sle_05960)
SLS : SLINC_7639 SLINC_7643
SGD : ELQ87_03245(rhaI) ELQ87_03285(rhaI)
SPAD : DVK44_34670(rhaI) DVK44_34795(rhaI)
SCOA : QU709_01240(rhaI) QU709_01260(rhaI)
MSUW : GCM10025863_21390(rhaI)
FRP : AX769_00035 AX769_22320
FSB : GCM10025867_44080(rhaI)
AMAU : DSM26151_02320(xylA_1)
AMAV : GCM10025877_18390(rhaI)
LYH : FrondiHNR_01780(rhaI)
PSNI : NIBR502771_08805(rhaI)
TLA : TLA_TLA_00976(xylA_1)
RAIN : Rai3103_04420(rhaI)
NAQU : ENKNEFLB_00335(xylA_1)
ACTQ : OG417_21530(rhaI) OG417_38095(rhaI)
ABAR : AMYBAR_003403(rhaI) AMYBAR_003590(rhaI) AMYBAR_007106(rhaI)
SSYI : EKG83_27390(rhaI) EKG83_32160(rhaI)
ACTR : Asp14428_40490(rhaA)
ACTL : L3i22_026820 L3i22_079080(rhaA)
ACTE : ACTI_56060 ACTI_57780(rhaA)
ATIM : CYJ17_0002355(rhaI)
AIR : AIF0345_0416(xylA_1)
ABAM : B1s21122_02325(rhaI)
DEIN : DAAJ005_00945(rhaI)
LOKI : Lokiarch_17880(rhaA)
» show all
Taxonomy
Reference
Authors
DOMAGK GF, ZECH R.
Title
[ON THE DECOMPOSITION OF DESOXY SUGARS BY BACTERIAL ENZYMES. I. L-RHAMNOSE ISOMERASE FROM LACTOBACILLUS PLANTARUM.]
Journal
Biochem Z 339:145-53 (1963)
Reference
Authors
Leang K, Takada G, Ishimura A, Okita M, Izumori K
Title
Cloning, nucleotide sequence, and overexpression of the L-rhamnose isomerase gene from Pseudomonas stutzeri in Escherichia coli.
Journal
Sequence
Reference
Authors
Korndorfer IP, Fessner WD, Matthews BW
Title
The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution.
Journal
Sequence
Reference
Authors
Yoshida H, Yamada M, Ohyama Y, Takada G, Izumori K, Kamitori S
Title
The structures of L-rhamnose isomerase from Pseudomonas stutzeri in complexes with L-rhamnose and D-allose provide insights into broad substrate specificity.
Journal
Sequence
Other DBs
ExplorEnz - The Enzyme Database: 5.3.1.14
ExPASy - ENZYME nomenclature database: 5.3.1.14
LinkDB
All DBs