KEGG   ENZYME: 4.1.2.57
Entry
EC 4.1.2.57                 Enzyme                                 

Name
sulfofructosephosphate aldolase;
yihT (gene name)
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
Sysname
6-deoxy-6-sulfofructose-1-phosphate 2-hydroxy-3-oxopropane-1-sulfonate-lyase (glycerone-phosphate-forming)
Reaction(IUBMB)
6-deoxy-6-sulfo-D-fructose 1-phosphate = glycerone phosphate + 2-hydroxy-3-oxopropane-1-sulfonate [RN:R10760]
Reaction(KEGG)
R10760
Substrate
6-deoxy-6-sulfo-D-fructose 1-phosphate [CPD:C20831]
Product
glycerone phosphate [CPD:C00111];
2-hydroxy-3-oxopropane-1-sulfonate [CPD:C20798]
Comment
The enzyme, characterized from the bacterium Escherichia coli, is involved in the degradation pathway of sulfoquinovose, the polar headgroup of sulfolipids found in the photosynthetic membranes of all higher plants, mosses, ferns, algae, and most photosynthetic bacteria, as well as the surface layer of some archaea.
History
EC 4.1.2.57 created 2014
Orthology
K01671  sulfofructosephosphate aldolase
Genes
ECO: b3881(yihT)
ECJ: JW3852(yihT)
ECD: ECDH10B_4071(yihT)
EBW: BWG_3551(yihT)
ECOK: ECMDS42_3320(yihT)
ECE: Z5418(yihT)
ECS: ECs4804
ECF: ECH74115_5328
ETW: ECSP_4937(yihT)
ELX: CDCO157_4543
EOI: ECO111_4701(yihT)
EOJ: ECO26_4709(yihT)
EOH: ECO103_4290(yihT)
ESL: O3K_24490
ESO: O3O_00845
ESM: O3M_24410
EOK: G2583_4682(yihT)
ELH: ETEC_4151
ECP: ECP_4089
ENA: ECNA114_3976(yihT)
ECOS: EC958_4355(yihT)
ECY: ECSE_4164
ECR: ECIAI1_4081(yihT)
ECQ: ECED1_4581(yihT)
EUM: ECUMN_4408(yihT)
ECT: ECIAI39_3119(yihT)
EOC: CE10_4545(yihT)
EBR: ECB_03766(yihT)
EBL: ECD_03766(yihT)
EBE: B21_03715(yihT)
EBD: ECBD_4146
ECI: UTI89_C4464(yihT)
ECC: c4827(yihT)
ESE: ECSF_3732
EKF: KO11_03200(yihT)
EDJ: ECDH1ME8569_3752(yihT)
ELW: ECW_m4185(yihT)
ELL: WFL_20390(yihT)
ELC: i14_4421(yihT)
ELD: i02_4421(yihT)
ELF: LF82_611
ECOI: ECOPMV1_04238(yihT)
ECOJ: P423_21515
STY: STY3856(yihT)
STT: t3599(yihT)
STM: STM4022(yihT)
SEO: STM14_4835(yihT)
SEY: SL1344_3968(yihT)
SEJ: STMUK_4005(yihT)
SEB: STM474_4199(yihT)
SEF: UMN798_4359(yihT)
SENR: STMDT2_38821(yihT)
SEND: DT104_40291(yihT)
SENI: CY43_21020
SPT: SPA3863(yihT)
SEK: SSPA3593
SEI: SPC_4125(yihT)
SEC: SCH_3912(yihT)
SHB: SU5_0118
SENS: Q786_19715
SED: SeD_A4410
SEL: SPUL_3650(yihT)
SEGA: SPUCDC_3636(yihT)
SET: SEN3810(yihT)
SENA: AU38_19690
SENO: AU37_19705
SENV: AU39_19725
SENQ: AU40_22015
SENL: IY59_20185
SEEP: I137_17530
SENE: IA1_19545
SBG: SBG_3539(yihT)
SBZ: A464_4063
SFL: SF3953(yihT)
SFX: S3793(yihT)
SFV: SFV_3618(yihT)
SFE: SFxv_4307(yihT)
SFN: SFy_5648
SFS: SFyv_5711
SFT: NCTC1_04279(yihT)
SSN: SSON_4049(yihT)
SBO: SBO_3888(yihT)
ENC: ECL_05104
ECLX: LI66_22515
ECLY: LI62_24600
ECLZ: LI64_21630
ECLO: ENC_00290
EEC: EcWSU1_04481(yihT)
ESA: ESA_04057
CSK: ES15_0036
CTU: CTU_41750(yihT)
RTG: NCTC13098_02411(yihT)
CRO: ROD_38801
CKO: CKO_03132
CAMA: F384_20995
AHN: NCTC12129_04954(yihT)
RAA: Q7S_20715
RACE: JHW33_14715(yihT)
PATR: EV46_11350
PATO: GZ59_22000
PCT: PC1_1950
PEC: W5S_2187
EBI: EbC_37890(lacD)
PAM: PANA_3496(yihT)
PLF: PANA5342_0555(yihT)
PAJ: PAJ_2725(yihT)
PSTW: DSJ_21390
MTHI: C7M52_01007(yihT)
ARA: Arad_9621
AVI: Avi_5337
RPC: RPC_1043
PLEO: OHA_1_03129(yihT)
RSP: RSP_4030(yihT)
RHB: NY08_111
RFA: A3L23_03501(lacD2)
RHS: A3Q41_04729(lacD2)
MLV: CVS47_02956(yihT)
ART: Arth_1948
ARM: ART_3392
ACIJ: JS278_00498(yihT)
MPH: MLP_21510
TLA: TLA_TLA_01114(yihT)
KFL: Kfla_0658
NML: Namu_3974
PSEE: FRP1_05055
PAUT: Pdca_49500(yihT)
MSAG: GCM10017556_58640(yihT)
PFLA: Pflav_052130(yihT)
 » show all
Reference
1  [PMID:24463506]
  Authors
Denger K, Weiss M, Felux AK, Schneider A, Mayer C, Spiteller D, Huhn T, Cook AM, Schleheck D
  Title
Sulphoglycolysis in Escherichia coli K-12 closes a gap in the biogeochemical sulphur cycle.
  Journal
Nature 507:114-7 (2014)
DOI:10.1038/nature12947
  Sequence
[eco:b3881]
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.57
IUBMB Enzyme Nomenclature: 4.1.2.57
ExPASy - ENZYME nomenclature database: 4.1.2.57
BRENDA, the Enzyme Database: 4.1.2.57

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