KEGG   ENZYME: 1.14.13.1
Entry
EC 1.14.13.1                Enzyme                                 
Name
salicylate 1-monooxygenase;
salicylate hydroxylase;
salicylate 1-hydroxylase;
salicylate monooxygenase;
salicylate hydroxylase (decarboxylating)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
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]
Comment
A flavoprotein (FAD).
History
EC 1.14.13.1 created 1972
Pathway
ec00621  Dioxin degradation
ec00624  Polycyclic aromatic hydrocarbon degradation
ec00626  Naphthalene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K00480  salicylate hydroxylase
Genes
NCR: NCU11363
NTE: NEUTE1DRAFT120622(NEUTE1DRAFT_120622)
SMP: SMAC_07304
PAN: PODANSg276
TTT: THITE_2076116
MTM: MYCTH_2305618
CTHR: CTHT_0064630
MGR: MGG_08293
PPEI: PpBr36_02133
TMN: UCRPA7_4723
SSCK: SPSK_07531 SPSK_07555
FGR: FGSG_03657 FGSG_10330
FPU: FPSE_01878 FPSE_09034
FVR: FVEG_08763 FVEG_13802
FOX: FOXG_09708 FOXG_16417 FOXG_16999
NHE: NECHADRAFT_42151 NECHADRAFT_90493
FFC: NCS54_00173900 NCS54_00976200
TRE: TRIREDRAFT_39535 TRIREDRAFT_73623
TRR: M419DRAFT_139626 M419DRAFT_91038
CMT: CCM_06214
PLJ: VFPFJ_07465
PTKZ: JDV02_010293 JDV02_010400
CFJ: CFIO01_04593 CFIO01_07911 CFIO01_07931
CLUP: CLUP02_01804 CLUP02_14238
CHIG: CH63R_06149 CH63R_10727
SAPO: SAPIO_CDS1150
ELA: UCREL1_664
PFY: PFICI_06004 PFICI_07209
SSL: SS1G_02963 SS1G_12062
BFU: BCIN_05g08190 BCIN_06g05670
MBE: MBM_02468
PSCO: LY89DRAFT_644170 LY89DRAFT_690792 LY89DRAFT_777397
GLZ: GLAREA_00796 GLAREA_12217 GLAREA_12986
ANI: AN2114.2 AN7382.2
AFM: AFUA_2G05260 AFUA_3G01460
ACT: ACLA_062980 ACLA_089370
NFI: NFIA_002410 NFIA_082020
AOR: AO090003000349 AO090020000356
ANG: ANI_1_1410064(An07g00550) ANI_1_1448144(An16g01280) ANI_1_688094(An11g05130)
AFV: AFLA_001339 AFLA_010304
ALUC: AKAW2_12072S AKAW2_70093A AKAW2_80463A
ACHE: ACHE_70030S ACHE_80368S
APUU: APUU_11094S APUU_20104S APUU_20944A
PCS: Pc15g00910 Pc21g05060
PDP: PDIP_10380
TMF: EYB26_005332
TRG: TRUGW13939_10602
PNO: SNOG_15763(AY587541)
PTE: PTT_01263 PTT_18951
BZE: COCCADRAFT_10188 COCCADRAFT_80694
BSC: COCSADRAFT_166665 COCSADRAFT_80807
BOR: COCMIDRAFT_111355 COCMIDRAFT_87469
AALT: CC77DRAFT_1028223 CC77DRAFT_642952 CC77DRAFT_942942
ZTR: MYCGRDRAFT_38199
PFJ: MYCFIDRAFT_72425
FFU: CLAFUR5_07705 CLAFUR5_10284 CLAFUR5_11539 CLAFUR5_12856
BCOM: BAUCODRAFT_266173 BAUCODRAFT_343349
NPA: UCRNP2_1128 UCRNP2_4358 UCRNP2_7602
TASA: A1Q1_05812
PPL: POSPLDRAFT_105326 POSPLDRAFT_23052 POSPLDRAFT_32625 POSPLDRAFT_32934 POSPLDRAFT_87724
TVS: TRAVEDRAFT_16216 TRAVEDRAFT_32834 TRAVEDRAFT_41389 TRAVEDRAFT_43869 TRAVEDRAFT_58559
DSQ: DICSQDRAFT_145027 DICSQDRAFT_166290 DICSQDRAFT_45577 DICSQDRAFT_97807
PCO: PHACADRAFT_146035 PHACADRAFT_172966 PHACADRAFT_191006 PHACADRAFT_209510 PHACADRAFT_248683 PHACADRAFT_24951 PHACADRAFT_257104 PHACADRAFT_257977 PHACADRAFT_260263 PHACADRAFT_264550 PHACADRAFT_83218
SHS: STEHIDRAFT_135813 STEHIDRAFT_164296 STEHIDRAFT_168688 STEHIDRAFT_79346 STEHIDRAFT_87533
HIR: HETIRDRAFT_442771 HETIRDRAFT_452336 HETIRDRAFT_453182
PSQ: PUNSTDRAFT_123020 PUNSTDRAFT_138973 PUNSTDRAFT_145991 PUNSTDRAFT_63080
ADL: AURDEDRAFT_112126 AURDEDRAFT_143542
FME: FOMMEDRAFT_104528 FOMMEDRAFT_156448 FOMMEDRAFT_171632
GTR: GLOTRDRAFT_140449 GLOTRDRAFT_38668 GLOTRDRAFT_40080 GLOTRDRAFT_95824
RSX: RhiXN_11181
LBC: LACBIDRAFT_298461
CCI: CC1G_00517 CC1G_03949 CC1G_05817
ABP: AGABI1DRAFT107807(AGABI1DRAFT_107807) AGABI1DRAFT51593(AGABI1DRAFT_51593) AGABI1DRAFT54356(AGABI1DRAFT_54356)
ABV: AGABI2DRAFT177137(AGABI2DRAFT_177137) AGABI2DRAFT214062(AGABI2DRAFT_214062) AGABI2DRAFT222486(AGABI2DRAFT_222486)
MPR: MPER_09678 MPER_12697
MRR: Moror_13689 Moror_2514 Moror_4784 Moror_4785 Moror_5271
MORE: E1B28_001559 E1B28_003297 E1B28_005868 E1B28_006091
SCM: SCHCO_01138368(SCHCODRAFT_01138368) SCHCO_02703927(SCHCODRAFT_02703927)
CPUT: CONPUDRAFT_101102 CONPUDRAFT_119489 CONPUDRAFT_126201 CONPUDRAFT_166647 CONPUDRAFT_46841
SLA: SERLADRAFT_414770 SERLADRAFT_447765 SERLADRAFT_453461 SERLADRAFT_466343
UMA: UMAG_05230
PFP: PFL1_03158
SGRA: EX895_004627
PIF: PITG_17117
PSOJ: PHYSODRAFT_560104
IZH: FEM41_17505(salA)
XSA: SB85_10110
XAR: XB05_19230
PSD: DSC_14905
PWI: MWN52_14975(salA)
PRE: PCA10_41220(nahG)
PFUW: KF707C_16120(salA) KF707C_29620
PPG: PputGB1_3586
PPI: ND016(nahG) ND091(nahG)
PPX: T1E_5510(nahG)
PMOS: O165_009705
PFN: HZ99_03455
PKR: AYO71_16495
PFX: A7318_13845
PSK: U771_15980
PSES: PSCI_4557(nahG)
PFK: PFAS1_28805
PPSL: BJP27_11255
PSIL: PMA3_14235
PALL: UYA_07000
PAZE: KSS91_14745(salA)
PKK: QQ992_18065(salA)
PSC: A458_06545
PSTU: UIB01_22720
PBM: CL52_14690
ACC: BDGL_001688(salR)
ALC: OTEC02_06330
ACAL: BUM88_12490
ACD: AOLE_06150
ACI: ACIAD1424(salA)
ATT: AMQ28_00970
AJO: RZ95_18845
ACW: A0J50_06110
ASOL: BEN76_06835
ADV: DJ533_02040(salA)
AGU: AS4_21780(salA)
ABER: BSR55_10845
HAK: KO116_00227
HHH: CLM76_07000(salA)
HPIZ: GYM47_16310(salA)
HSV: HNO53_19235(salA)
HTX: EKK97_21235(salA)
HPRO: LMS44_22970(salA)
HBH: E4T21_16500(salA)
HASO: B2G49_18175
 » show all
Reference
1  [PMID:4390441]
  Authors
Uzuki K, Takemori S, Katagiri M.
  Title
Mechanism of the salicylate hydroxylase reaction. IV. Fluorometric analysis of the complex formation.
  Journal
Biochim Biophys Acta 191:77-85 (1969)
DOI:10.1016/0005-2744(69)90316-7
Reference
2  [PMID:4898626]
  Authors
Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M.
  Title
Mechanism of the salicylate hydroxylase reaction. II. The enzyme-substrate complex.
  Journal
Biochim Biophys Acta 191:58-68 (1969)
DOI:10.1016/0005-2744(69)90314-3
Reference
3  [PMID:4309912]
  Authors
Takemori S, Yasuda H, Mihara K, Suzuki K, Katagiri M.
  Title
Mechanism of the salicylate hydroxylase reaction. 3. Characterization and reactivity of chemically or photochemically reduced enzyme-flavin.
  Journal
Biochim Biophys Acta 191:69-76 (1969)
DOI:10.1016/0005-2744(69)90315-5
Reference
4  [PMID:14321380]
  Authors
YAMAMOTO S, KATAGIRI M, MAENO H, HAYAISHI O.
  Title
SALICYLATE HYDROXYLASE, A MONOOXYGENASE REQUIRING FLAVIN ADENINE DINUCLEOTIDE. I. PURIFICATION AND GENERAL PROPERTIES.
  Journal
J Biol Chem 240:3408-13 (1965)
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
LinkDB

DBGET integrated database retrieval system