| Entry |
|
| Name |
salicylate 1-monooxygenase;
salicylate hydroxylase;
salicylate 1-hydroxylase;
salicylate monooxygenase;
salicylate hydroxylase (decarboxylating) |
| Class |
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With NADH or NADPH as one donor, and incorporation of one atom of
oxygen into the other donor
 |
| Sysname |
salicylate,NADH:oxygen oxidoreductase (1-hydroxylating,
decarboxylating) |
| Reaction(IUBMB) |
salicylate + NADH + 2 H+ + O2 = catechol + NAD+ + H2O + CO2
[RN:R00818] |
| Reaction(KEGG) |
R00818;
(other) R05632 R06915 R06936 R06939
 |
| Substrate |
salicylate [CPD:C00805];
NADH [CPD:C00004];
H+ [CPD:C00080];
O2 [CPD:C00007] |
| Product |
catechol [CPD:C00090];
NAD+ [CPD:C00003];
H2O [CPD:C00001];
CO2 [CPD:C00011] |
| Cofactor |
FAD [CPD:C00016] |
| Comment |
A flavoprotein (FAD). |
| Pathway |
PATH: ec00120 Primary bile acid biosynthesis
PATH: ec00624 1- and 2-Methylnaphthalene degradation
PATH: ec00626 Naphthalene and anthracene degradation
PATH: ec00628 Fluorene degradation
PATH: ec01100 Metabolic pathways |
| Orthology |
KO: K00480 salicylate hydroxylase |
| Genes |
PIC: PICST_31033(NHG3) PICST_56402(NHG1.2)
MGR: MGG_03764 MGG_04166 MGG_04240 MGG_06552 MGG_10012 MGG_10014
MGG_10216
ANI: AN2114.2 AN3382.2 AN4576.2 AN7382.2 AN7902.2
AFM: AFUA_1G02970 AFUA_1G12410 AFUA_1G17670 AFUA_2G00770
AFUA_2G01680 AFUA_2G01950 AFUA_2G04330 AFUA_2G05260
AFUA_3G01460 AFUA_3G01600 AFUA_4G01530 AFUA_6G07340
AFUA_6G13970 AFUA_6G14510 AFUA_7G00590 AFUA_8G02380
AFUA_8G06050 AFUA_8G07020
AOR: AO090003000349 AO090010000109 AO090011000262 AO090011000462
AO090020000356
ANG: An03g02130 An07g00550 An07g01440 An07g05650 An09g01840
An09g04390 An11g05130 An12g02000 An18g01030
CNE: CNA08200
UMA: UM03408.1 UM05967.1
LMA: LmjF26.2610
ECE: Z3390
ECS: ECs3027
ECF: ECH74115_3267
ETW: ECSP_3013
STY: STY2405
STT: t0680
SPT: SPA0676
SEK: SSPA0635
SPQ: SPAB_00841
SEI: SPC_1527
SEC: SC2192(nhg)
SEH: SeHA_C2410
SEE: SNSL254_A2365
SEW: SeSA_A2414
SEA: SeAg_B2321
SED: SeD_A2522
SEG: SG2211
SET: SEN2168
STM: STM2175
SGL: SG0076
CKO: CKO_00654
SPE: Spro_2311
PPU: PP_3944(nahG)
PPF: Pput_1893
PEN: PSEEN2596(mhbM)
ACI: ACIAD0984 ACIAD1424(salA)
MMW: Mmwyl1_0991
REU: Reut_A2515 Reut_B3601 Reut_B5805 Reut_B5861
REH: H16_A0578 H16_A0922 H16_A1785 H16_B0750 H16_B0876
BUR: Bcep18194_A4962 Bcep18194_B0481 Bcep18194_B1231 Bcep18194_B1886
Bcep18194_C6859
BCN: Bcen_4218 Bcen_4324
BCH: Bcen2424_4042 Bcen2424_4148
BCM: Bcenmc03_3371
BCJ: BCAM1274(mhbM)
BAM: Bamb_1082 Bamb_4040
BMU: Bmul_4439
BMJ: BMULJ_04070(nahG)
BXE: Bxe_B2392 Bxe_B2526 Bxe_C0213 Bxe_C1022
BPE: BP1954
BPA: BPP2327
BBR: BB1778
BPT: Bpet0509
BAV: BAV1787
RFR: Rfer_3311
POL: Bpro_2128 Bpro_3591
PNA: Pnap_3023 Pnap_3144
AAV: Aave_1154 Aave_3927
AJS: Ajs_1146
VEI: Veis_1345
DIA: Dtpsy_1067
EBA: ebA1378(s5h)
AZO: azo2422(nahG)
PUB: SAR11_0110(nah)
MLO: mll8158
MES: Meso_0052 Meso_0813 Meso_1117
SME: SMc02116
ATU: Atu1574(nah)
ATC: AGR_C_2901
RET: RHE_CH01900(nah)
RLE: RL2206
BME: BMEI1017 BMEI1207
BMF: BAB1_0770
BMB: BruAb1_0763
BMS: BR0746
BOV: BOV_0740
BJA: blr4977 blr5591(nah)
BRA: BRADO2323 BRADO2935
BBT: BBta_2684 BBta_5237
RPA: RPA3433
RPB: RPB_2131
RPC: RPC_3149
RPD: RPD_3292
RPE: RPE_2307
NWI: Nwi_2182
NHA: Nham_2584
BHE: BH09840
BQU: BQ07610
BBK: BARBAKC583_0871
BTR: Btr_1363
MEX: Mext_2203
MDI: METDI2976
MRD: Mrad2831_0588
MET: M446_6758
MPO: Mpop_2160
MCH: Mchl_2480
SIL: SPO2510(nahG) SPO3692
SIT: TM1040_0896
RSP: RSP_2656(nahG)
RSQ: Rsph17025_1193
JAN: Jann_2908
RDE: RD1_2791
DSH: Dshi_1885
MAB: MAB_0288 MAB_3330
CGL: NCgl2923(cgl3026)
CGB: cg3354
CGT: cgR_2913
CEF: CE0117 CE2863
RHA: RHA1_ro01869
SCO: SCO3245(SCE29.14c)
ART: Arth_2055
AAU: AAur_0334
FRA: Francci3_2068 Francci3_4207
SEN: SACE_1995
 |
Reference Authors Title
Journal
|
1 [PMID:4390441]
Uzuki K, Takemori S, Katagiri M.
Mechanism of the salicylate hydroxylase reaction. IV. Fluorometric
analysis of the complex formation.
Biochim. Biophys. Acta. 191 (1969) 77-85. |
Reference Authors Title
Journal Organism
|
2 [PMID:4898626]
Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M.
Mechanism of the salicylate hydroxylase reaction. II. The
enzyme-substrate complex.
Biochim. Biophys. Acta. 191 (1969) 58-68.
Pseudomonas putida |
Reference Authors Title
Journal Organism
|
3 [PMID:4309912]
Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M.
Mechanism of the salicylate hydroxylase reaction. 3.
Characterization and reactivity of chemically or photochemically
reduced enzyme-flavin.
Biochim. Biophys. Acta. 191 (1969) 69-76.
Pseudomonas putida |
Reference Authors Title
Journal Organism
|
4 [PMID:14321380]
YAMAMOTO S, KATAGIRI M, MAENO H, HAYAISHI O.
SALICYLATE HYDROXYLASE, A MONOOXYGENASE REQUIRING FLAVIN ADENINE
DINUCLEOTIDE. I. PURIFICATION AND GENERAL PROPERTIES.
J. Biol. Chem. 240 (1965) 3408-13.
Pseudomonas sp. |
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.13.1
IUBMB Enzyme Nomenclature: 1.14.13.1
ExPASy - ENZYME nomenclature database: 1.14.13.1
UM-BBD (Biocatalysis/Biodegradation Database): 1.14.13.1
BRENDA, the Enzyme Database: 1.14.13.1
CAS: 9059-28-3 |