| Entry |
|
| Name |
threonine-phosphate decarboxylase;
L-threonine-O-3-phosphate decarboxylase;
CobD;
L-threonine-O-3-phosphate carboxy-lyase |
| Class |
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
 |
| Sysname |
L-threonine-O-3-phosphate carboxy-lyase
[(R)-1-aminopropan-2-yl-phosphate-forming] |
| Reaction(IUBMB) |
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2
[RN:R06530] |
| Reaction(KEGG) |
R06530
 |
| Substrate |
L-threonine O-3-phosphate [CPD:C12147] |
| Product |
(R)-1-aminopropan-2-yl phosphate [CPD:C04122];
CO2 [CPD:C00011] |
| Comment |
A pyridoxal-phosphate protein. This enzyme is unable to
decarboxylate the D-isomer of threonine O-3-phosphate. The product
of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate
of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which
converts adenosylcobyric acid into adenosylcobinamide phosphate in
the anaerobic cobalamin biosynthesis pathway. |
| Pathway |
PATH: ec00860 Porphyrin and chlorophyll metabolism |
| Orthology |
KO: K04720 threonine-phosphate decarboxylase |
| Genes |
STY: STY0695(cobD)
STT: t2223(cobD)
SPT: SPA2090(cobD)
SEK: SSPA1942
SPQ: SPAB_02906
SEI: SPC_0660
SEC: SC0674(cobD)
SEH: SeHA_C0760(cobD)
SEE: SNSL254_A0701
SEW: SeSA_A0804(cobD)
SEA: SeAg_B0687(cobD)
SED: SeD_A0747(cobD)
SET: SEN0613(cobD)
SES: SARI_02288
STM: STM0644(cobD)
YEN: YE2749(cobD)
PLU: plu2967(cobD)
PAY: PAU_01635(cobD)
KPN: KPN_03224(cobD)
KPE: KPK_0891(cobD)
KPU: KP1_4493(cobD)
CKO: CKO_02518
EIC: NT01EI_1848
TAU: Tola_1705
GSU: GSU2989
GME: Gmet_0487
GUR: Gura_0043
PPD: Ppro_0869
DDE: Dde_1401
SFU: Sfum_1737
GBE: GbCGDNIH1_0652
MGM: Mmc1_3126
BHA: BH1589(cobC)
GKA: GK2262
GTN: GTNG_2195
LMO: lmo1169(cobD)
LMF: LMOf2365_1177
LIN: lin1133
LWE: lwe1127(cobD)
LRE: Lreu_1723
CPE: CPE1040
CPF: CPF_1295
CNO: NT01CX_2083
CDF: CD3432(cobD)
CKL: CKL_0714(cobD1)
STH: STH1925
DRM: Dred_2701
PTH: PTH_1314(hisC)
MTA: Moth_1104
SYN: sll1713(hisC)
SYC: syc0440_c(hisC)
SYF: Synpcc7942_1109
SYD: Syncc9605_2464
SYE: Syncc9902_2148
SYG: sync_2715(cobD-2)
CYA: CYA_0941(cobD-2)
CYB: CYB_0897(cobD-1)
TEL: tll2266
CYT: cce_1744(cobD)
GVI: gvip468(hisC)
ANA: alr3936(hisC)
AVA: Ava_1766
PMN: PMN2A_1565
PMI: PMT9312_0200
PMB: A9601_02161
PMC: P9515_02271
PMG: P9301_02181
TER: Tery_1611
CCH: Cag_1011
CPH: Cpha266_1118
PVI: Cvib_0815
DEB: DehaBAV1_0625
MBA: Mbar_A3453
MBU: Mbur_0787 Mbur_2087 Mbur_2089
HWA: HQ1407A(cobD)
NPH: NP5302A(cobD)
RCI: RCIX2655(cobD)
 |
Reference Authors Title
Journal Organism Sequence
|
1 [PMID:11939774]
Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I.
Three-dimensional structure of the L-threonine-O-3-phosphate
decarboxylase (CobD) enzyme from Salmonella enterica.
Biochemistry. 41 (2002) 4798-808.
Salmonella enterica [GN:spq]
SPQ: SPAB_02906 |
Reference Authors Title
Journal
|
2 [PMID:9446573]
Brushaber KR, O'Toole GA, Escalante-Semerena JC
CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase
activity, is responsible for the synthesis of (R)-1-amino-2-propanol
O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis
in Salmonella typhimurium LT2.
J. Biol. Chem. 273 (1998) 2684-91. |
Reference Authors Title Journal Organism
|
3 [PMID:12195810]
Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC.
The biosynthesis of adenosylcobalamin (vitamin B12).
Nat. Prod. Rep. 19 (2002) 390-412.
Salmonella enterica, Pseudomonas denitrificans |
| Other DBs |
ExplorEnz - The Enzyme Database: 4.1.1.81
IUBMB Enzyme Nomenclature: 4.1.1.81
ExPASy - ENZYME nomenclature database: 4.1.1.81
BRENDA, the Enzyme Database: 4.1.1.81 |