KEGG   ENZYME: 2.3.1.242Help
Entry
EC 2.3.1.242                Enzyme                                 

Name
Kdo2-lipid IVA palmitoleoyltransferase;
LpxP;
palmitoleoyl-acyl carrier protein-dependent acyltransferase;
cold-induced palmitoleoyl transferase;
palmitoleoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase;
(Kdo)2-lipid IVA palmitoleoyltransferase;
alpha-Kdo-(2->4)-alpha-(2->6)-lipid IVA palmitoleoyltransferase
Class
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
BRITE hierarchy
Sysname
(9Z)-hexadec-9-enoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-palmitoleoyltransferase
Reaction(IUBMB)
a (9Z)-hexadec-9-enoyl-[acyl-carrier protein] + Kdo2-lipid IVA = (9Z)-hexadec-9-enoyl-Kdo2-lipid IVA + an [acyl-carrier protein] [RN:R10906]
Reaction(KEGG)
Substrate
(9Z)-hexadec-9-enoyl-[acyl-carrier protein] [CPD:C16520];
Kdo2-lipid IV(A) [CPD:C06025]
Product
(9Z)-hexadec-9-enoyl-Kdo2-lipid IV(A) [CPD:C20933];
[acyl-carrier protein] [CPD:C00229]
Comment
The enzyme, characterized from the bacterium Escherichia coli, is induced upon cold shock and is involved in the formation of a cold-adapted variant of the outer membrane glycolipid lipid A.
History
EC 2.3.1.242 created 2014
Orthology
K12974  KDO2-lipid IV(A) palmitoleoyltransferase
Genes
ECO: b2378(lpxP)
ECJ: JW2375(ddg)
ECD: ECDH10B_2543(lpxP)
EBW: BWG_2146(lpxP)
ECOK: ECMDS42_1935(ddg)
ECE: Z3643(ddg)
ECS: ECs3258
ECF: ECH74115_3609
ETW: ECSP_3327(lpxP)
ELX: CDCO157_3022
EOJ: ECO26_3438(ddg)
EOI: ECO111_3114(ddg)
EOH: ECO103_2903(ddg)
ECG: E2348C_2571(lpxP)
EOK: G2583_2911(lpxP)
ECC: c2915(ddg)
ECP: ECP_2404
ECI: UTI89_C2710(ddg)
ECV: APECO1_4159(ddg)
ECY: ECSE_2675
ECR: ECIAI1_2444(ddg)
ECQ: ECED1_2825(ddg)
ECK: EC55989_2674(ddg)
ECT: ECIAI39_2522(ddg)
EOC: CE10_2755(lpxP)
EUM: ECUMN_2708(ddg)
ECZ: ECS88_2573(ddg)
ELO: EC042_2597(lpxP)
ELH: ETEC_2497
ESE: ECSF_2248
ESO: O3O_18155
ESM: O3M_07530
ESL: O3K_07480
EBR: ECB_02288(ddg)
EBD: ECBD_1294
EKF: KO11_10870(lpxP)
EDJ: ECDH1ME8569_2317(ddg)
ENA: ECNA114_2459(ddg)
ELW: ECW_m2611(lpxP)
ELL: WFL_12810(lpxP)
ELC: i14_2712(ddg)
ELD: i02_2712(ddg)
EBL: ECD_02288(lpxP)
EBE: B21_02249(lpxP)
ELF: LF82_1232(lpxP)
ECOI: ECOPMV1_02582(htrB_2)
ECOJ: P423_13220
ECOO: ECRM13514_3202(ddg)
ECOH: ECRM13516_3064(ddg)
ECOS: EC958_4999
EFE: EFER_0790(ddg)
STY: STY2639
STT: t0457
STM: STM2401(ddg)
SEO: STM14_2953(ddg)
SEY: SL1344_2369(lpxP)
SEJ: STMUK_2432(ddg)
SEB: STM474_2501(ddg)
SENI: CY43_12850
SPT: SPA0459(ddg)
SEK: SSPA0426
SEI: SPC_1256(ddg)
SEC: SCH_2402(ddg)
SENS: Q786_11860
SEG: SG2437(ddg)
SEL: SPUL_0478(ddg)
SEGA: SPUCDC_0478(ddg)
SET: SEN2387(ddg)
SENA: AU38_12080
SENO: AU37_12095
SENV: AU39_12095
SENQ: AU40_13540
SENL: IY59_12415
SEEP: I137_02185
SENE: IA1_11985
SBG: SBG_2203
SBZ: A464_2528
SFL: SF2444(ddg)
SFX: S2582(ddg)
SFV: SFV_2436(ddg)
SFE: SFxv_2690(lpxP)
SFN: SFy_3466
SFS: SFyv_3541
SFT: NCTC1_02681(ddg)
SSN: SSON_2469(ddg)
SBO: SBO_2404(ddg)
SDY: SDY_2576(ddg)
ENC: ECL_03721
EEC: EcWSU1_03221(lpxP)
ECLX: LI66_15645
ECLY: LI62_17145
ECLZ: LI64_15075
ESA: ESA_02951
CSK: ES15_3030(lpxP)
CTU: CTU_09250(ddg)
KPN: KPN_01167
KPU: KP1_2185
KPP: A79E_3023
KPT: VK055_1295(lpxL)
KPE: KPK_3319 KPK_4958(lpxL)
KPJ: N559_3127
KPX: PMK1_03505(htrB_3)
KPNU: LI86_16245
KPNK: BN49_2301
KVA: Kvar_3191
KOE: A225_2433
EAR: CCG29572
CKO: CKO_00422
CRO: ROD_27921(lpxP)
CAMA: F384_13225
EBF: D782_1803
PSTS: E05_06240
YPE: YPO3632(ddg)
YPK: y0236(ddg)
YPA: YPA_3645
YPN: YPN_3538
YPM: YP_3915(ddg)
YPG: YpAngola_A1232(htrB2)
YPZ: YPZ3_3121
YPD: YPD4_3109
YPX: YPD8_3216
YPH: YPC_4380
YPW: CH59_2387(lpxL)
YPJ: CH55_2569(lpxL)
YPV: BZ15_4076(lpxL)
YPL: CH46_1427(lpxL)
YPS: YPTB3597(ddg)
YPO: BZ17_3003(lpxL)
YPI: YpsIP31758_0361(htrB2)
YPY: YPK_0430
YPB: YPTS_3787
YPQ: DJ40_2816(lpxL)
YPU: BZ21_2925(lpxL)
YPR: BZ20_2517(lpxL)
YPC: BZ23_3197(lpxL)
YPF: BZ19_3062(lpxL)
YEN: YE3829(ddg)
YEY: Y11_27341
YEW: CH47_3967(lpxL)
YET: CH48_2072(lpxL)
YEE: YE5303_01031(ddg)
YAL: AT01_2110(lpxL)
YFR: AW19_2837(lpxL)
YIN: CH53_2176(lpxL)
YKR: CH54_2951(lpxL)
YRO: CH64_2252(lpxL)
YRU: BD65_1562(lpxL)
SPE: Spro_4425
SRL: SOD_c42360(lpxP)
SPLY: Q5A_023075(lpxP)
SMAF: D781_4156
SMW: SMWW4_v1c43920(lpxP)
SMAR: SM39_3882(lpxP)
SMAC: SMDB11_3678(lpxP)
SERF: L085_06260
RAA: Q7S_20470
ECA: ECA0781(ddg)
PATR: EV46_03425
PATO: GZ59_06870(ddg)
PCT: PC1_0655
PEC: W5S_0778
SGL: SG0784
SOD: Sant_2836(lpxP)
PES: SOPEG_1130(lpxP)
DDD: Dda3937_02265(ddg)
DDQ: DDI_0536
ETA: ETA_02550(ddg)
EPY: EpC_02750(ddg)
EPR: EPYR_00286(ddg)
EAM: EAMY_0267(ddg)
EAY: EAM_3150(lpxP)
EBI: EbC_40850(ddg)
ERJ: EJP617_14400(ddg)
EGE: EM595_0412(lpxP)
PAM: PANA_3932(ddg)
PLF: PANA5342_0120(ddg)
PAJ: PAJ_3135(ddg)
PVA: Pvag_3205(ddg)
PMR: PMI0808(ddg)
PMIB: BB2000_0876(ddg)
PSI: S70_04395
PSX: DR96_55(lpxL)
PRG: RB151_026350(htrB_2)
ETR: ETAE_2920
ETD: ETAF_2652
ETE: ETEE_1146
AMIM: MIM_c02530
 » show all
Taxonomy
Reference
1  [PMID:10092655]
  Authors
Carty SM, Sreekumar KR, Raetz CR
  Title
Effect of cold shock on lipid A biosynthesis in Escherichia coli. Induction At 12 degrees C of an acyltransferase specific for palmitoleoyl-acyl carrier protein.
  Journal
J. Biol. Chem. 274 (1999) 9677-85.
  Sequence
[eco:b2378]
Reference
2  [PMID:11830594]
  Authors
Vorachek-Warren MK, Carty SM, Lin S, Cotter RJ, Raetz CR
  Title
An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C.
  Journal
J. Biol. Chem. 277 (2002) 14186-93.
  Sequence
[eco:b2378]
Other DBs
ExplorEnz - The Enzyme Database: 2.3.1.242
IUBMB Enzyme Nomenclature: 2.3.1.242
ExPASy - ENZYME nomenclature database: 2.3.1.242
BRENDA, the Enzyme Database: 2.3.1.242

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