KEGG   ENZYME: 2.7.2.15Help
Entry
EC 2.7.2.15                 Enzyme                                 

Name
propionate kinase;
PduW;
TdcD;
propionate/acetate kinase
Class
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with a carboxy group as acceptor
BRITE hierarchy
Sysname
ATP:propanoate phosphotransferase
Reaction(IUBMB)
ATP + propanoate = ADP + propanoyl phosphate [RN:R01353]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
propanoate [CPD:C00163]
Product
ADP [CPD:C00008];
propanoyl phosphate [CPD:C02876]
Comment
Requires Mg2+. Acetate can also act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [1]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate [1].
History
EC 2.7.2.15 created 2005
Pathway
ec00640  Propanoate metabolism
ec01100  Metabolic pathways
Orthology
K00932  propionate kinase
K19697  propionate kinase
Genes
ECO: b3115(tdcD)
ECJ: JW5806(tdcD)
ECD: ECDH10B_3289(tdcD)
EBW: BWG_2823(tdcD)
ECOK: ECMDS42_2583(tdcD)
ECE: Z4467(tdcD)
ECS: ECs3995
ECF: ECH74115_4428(tdcD)
ETW: ECSP_4087(tdcD)
ELX: CDCO157_3736
EOJ: ECO26_4220(tdcD)
EOI: ECO111_3939(tdcD)
EOH: ECO103_3862(tdcD)
ECOO: ECRM13514_4076(tdcD)
ECOH: ECRM13516_3879(tdcD)
ECG: E2348C_3405(tdcD)
EOK: G2583_3837(tdcD)
ESO: O3O_22280
ESM: O3M_03405
ESL: O3K_03365
ECW: EcE24377A_3589(tdcD)
ELH: ETEC_3383
EUN: UMNK88_3870(ackA)
ECC: c3873 c4530(tdcD)
ECP: ECP_3208
ECI: UTI89_C3550(tdcD)
ECX: EcHS_A3303(tdcD)
ECM: EcSMS35_3411(tdcD)
ECY: ECSE_3399
ECR: ECIAI1_3264(tdcD)
ECK: EC55989_3532(tdcD)
ECT: ECIAI39_3616(tdcD)
EOC: CE10_3647(tdcD)
EUM: ECUMN_3599(tdcD)
ELO: EC042_3407(tdcD)
ESE: ECSF_2955
EBR: ECB_02982(tdcD)
EBD: ECBD_0625
EKF: KO11_07110(tdcD)
EAB: ECABU_c35320(tdcD)
EDJ: ECDH1ME8569_3008(tdcD)
EIH: ECOK1_3542(tdcD)
ENA: ECNA114_4344(tdcD)
ELW: ECW_m3384(tdcD)
ELL: WFL_16540(tdcD)
ELC: i14_3561(tdcD)
ELD: i02_3561(tdcD)
ELP: P12B_c3231(tdcD)
EBL: ECD_02982(tdcD)
EBE: B21_02933(tdcD)
ELF: LF82_2233(tdcD)
ECOI: ECOPMV1_03429(tdcD)
ECOJ: P423_17570
ECOS: EC958_3518(tdcD)
EFE: EFER_2027
EAL: EAKF1_ch2818(tdcD)
STY: STY2262 STY3424(tdcD)
STT: t0817 t3162(tdcD)
STM: STM2057(pduW) STM3242(tdcD)
SEO: STM14_2546(pduW) STM14_3924(tdcD)
SEY: SL1344_2033(pduW) SL1344_3214(tdcD)
SEJ: STMUK_2087(pduW) STMUK_3231(tdcD)
SEB: STM474_2142(pduW) STM474_3396(tdcD)
SEF: UMN798_2223(pduW) UMN798_3526(tdcD)
SENR: STMDT2_20301(pduW) STMDT2_31341(tdcD)
SEND: DT104_21141(pduW) DT104_32371(tdcD)
SPT: SPA0814(pduW) SPA3111(tdcD)
SEI: SPC_1657(pduW) SPC_3318(tdcD)
SEC: SCH_2066(pduW) SCH_3188(tdcD)
SEH: SeHA_C2280(ackA) SeHA_C3537(ackA)
SEE: SNSL254_A2234(ackA) SNSL254_A3504(ackA)
SEW: SeSA_A2227(ackA) SeSA_A3433(ackA)
SEA: SeAg_B2180(ackA) SeAg_B3430(ackA)
SED: SeD_A2393(ackA) SeD_A3600(ackA)
SEG: SG2086(pduW) SG3139(tdcD)
SEL: SPUL_0843(pduW) SPUL_3255(tdcD)
SEGA: SPUCDC_0843(pduW) SPUCDC_3241(tdcD)
SET: SEN2055(pduW) SEN3083(tdcD)
SBG: SBG_2879(tdcD)
SBZ: A464_3326
SFL: SF3155(tdcD)
SFX: S3367(tdcD)
SFV: SFV_3156(tdcD)
SFE: SFxv_3462(tdcD)
SFN: SFy_4506
SFS: SFyv_4580
SFT: NCTC1_03420(tdcD)
SSN: SSON_3272(tdcD)
SBO: SBO_2980(tdcD)
SBC: SbBS512_E3242(tdcD)
SDY: SDY_3307(tdcD)
ENC: ECL_04509
ECLO: ENC_33660
EEC: EcWSU1_03927(tdcD)
ECLX: LI66_19690
ECLY: LI62_21665
ECLZ: LI64_18805
KPN: KPN_02293(tdcD) KPN_03222(pduW)
KPU: KP1_3409(tdcD) KP1_4491(pduW)
KPT: VK055_0163(ackA) VK055_4303(ackA2)
KPE: KPK_0893(pduW) KPK_2016(tdcD)
KPR: KPR_1811(pduW) KPR_3203(tdcD)
KPX: PMK1_00703(pduW) PMK1_04654(tdcD)
KPNK: BN49_0886(pduW) BN49_3394(tdcD)
KOX: KOX_01540
KOE: A225_4773
EAE: EAE_22040
EAR: CCG29523
CRO: ROD_21431(pduW) ROD_47621(tdcD)
EBF: D782_0577
YEN: YE0338(tdcD) YE2747(pduW)
YEW: CH47_2096(ackA) CH47_3136(ackA)
YET: CH48_1252(ackA) CH48_3134(ackA)
YEE: YE5303_31801(pduW)
YAL: AT01_2860(ackA) AT01_4016(ackA)
YFR: AW19_702(ackA)
YIN: CH53_1391(ackA) CH53_3350(ackA)
YKR: CH54_960(ackA)
YRU: BD65_1333(ackA)
PEC: W5S_4257
SOD: Sant_2126(tdcD)
ETR: ETAE_0896(tdcD)
ETD: ETAF_0836
ETE: ETEE_2779(tdcD)
AVR: B565_1141
TAU: Tola_1703
FJG: BB050_04356(pduW)
 » show all
Taxonomy
Reference
1  [PMID:9484901]
  Authors
Hesslinger C, Fairhurst SA, Sawers G.
  Title
Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate.
  Journal
Mol Microbiol 27:477-92 (1998)
DOI:10.1046/j.1365-2958.1998.00696.x
  Sequence
[eco:b3115]
Reference
2  [PMID:12700259]
  Authors
Palacios S, Starai VJ, Escalante-Semerena JC.
  Title
Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol.
  Journal
J Bacteriol 185:2802-10 (2003)
DOI:10.1128/JB.185.9.2802-2810.2003
Reference
3  [PMID:10498722]
  Authors
Wei Y, Miller CG.
  Title
Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium.
  Journal
J Bacteriol 181:6092-7 (1999)
  Sequence
[stm:STM3242]
Reference
4  [PMID:15774882]
  Authors
Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG.
  Title
Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase.
  Journal
J Bacteriol 187:2386-94 (2005)
DOI:10.1128/JB.187.7.2386-2394.2005
Reference
5  [PMID:16508089]
  Authors
Simanshu DK, Murthy MR.
  Title
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 61:52-5 (2005)
DOI:10.1107/S1744309104026429
Reference
6  [PMID:16139298]
  Authors
Simanshu DK, Savithri HS, Murthy MR.
  Title
Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily.
  Journal
J Mol Biol 352:876-92 (2005)
DOI:10.1016/j.jmb.2005.07.069
  Sequence
[stm:STM3242]
Other DBs
ExplorEnz - The Enzyme Database: 2.7.2.15
IUBMB Enzyme Nomenclature: 2.7.2.15
ExPASy - ENZYME nomenclature database: 2.7.2.15
BRENDA, the Enzyme Database: 2.7.2.15
CAS: 39369-28-3

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