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
NCRNCU11363
NTENEUTE1DRAFT120622(NEUTE1DRAFT_120622)
SMPSMAC_07304
PANPODANSg276
PBELQC761_300080 QC761_507200
PPSDQC762_300080 QC762_507200
PPSPQC763_300080 QC763_404510 QC763_507200 QC763_600780
PPSAQC764_300080 QC764_404510 QC764_507200 QC764_600780
TTTTHITE_2076116
MTMMYCTH_2305618
CTHRCTHT_0064630
MGRMGG_08293
PPEIPpBr36_02133
PGRIPgNI_07877
TMNUCRPA7_4723
SSCKSPSK_07531 SPSK_07555
FGRFGSG_03657 FGSG_10330
FPUFPSE_01878 FPSE_09034
FPOAFPOAC1_006054 FPOAC1_007682
FVNFVRRES_06653
FVRFVEG_08763 FVEG_13802
FOXFOXG_09708 FOXG_16417 FOXG_16999
NHENECHADRAFT_42151 NECHADRAFT_90493
FFCNCS54_00173900 NCS54_00976200
FKRNCS57_00170900 NCS57_00499000
FMUJ7337_012571
TRETRIREDRAFT_39535 TRIREDRAFT_73623
TRRM419DRAFT_139626 M419DRAFT_91038
PCHMVFPPC_05612
CMTCCM_06214
AMUSLMH87_005088
PLJVFPFJ_07465
PTKZJDV02_010293 JDV02_010400
CFJCFIO01_04593 CFIO01_07911 CFIO01_07931
CLUPCLUP02_01804 CLUP02_14238
CHIGCH63R_06149 CH63R_10727
SAPOSAPIO_CDS1150
ELAUCREL1_664
PFYPFICI_06004 PFICI_07209
SSLSS1G_02963 SS1G_12062
BFUBCIN_05g08190 BCIN_06g05670
MBEMBM_02468
PSCOLY89DRAFT_644170 LY89DRAFT_690792 LY89DRAFT_777397
GLZGLAREA_00796 GLAREA_12217 GLAREA_12986
ANIANIA_02114 ANIA_07382
AFMAFUA_2G05260 AFUA_3G01460
ACTACLA_062980 ACLA_089370
NFINFIA_002410 NFIA_082020
AORAO090003000349 AO090020000356
ANGAn07g00550 An11g05130 An16g01280
AFVAFLA_001339 AFLA_010304
ALUCAKAW2_12072S AKAW2_70093A AKAW2_80463A
ACHEACHE_70030S ACHE_80368S
APUUAPUU_20104S APUU_20944A
PCSN7525_006987 N7525_010030
PDPPDIP_10380
POUPOX_b03321
TMFEYB26_005332
TRGTRUGW13939_10602
PNOSNOG_15763(AY587541)
PTEPTT_01263 PTT_18951
BZECOCCADRAFT_10188 COCCADRAFT_80694
BSCCOCSADRAFT_166665 COCSADRAFT_80807
BORCOCMIDRAFT_111355 COCMIDRAFT_87469
AALTCC77DRAFT_1028223 CC77DRAFT_642952 CC77DRAFT_942942
ARABEKO05_0004884 EKO05_0009558
ZTRMYCGRDRAFT_38199
PFJMYCFIDRAFT_72425
FFUCLAFUR5_07705 CLAFUR5_10284 CLAFUR5_11539 CLAFUR5_12856
CBETCB0940_06262 CB0940_07349 CB0940_12107
BCOMBAUCODRAFT_266173 BAUCODRAFT_343349
NPAUCRNP2_1128 UCRNP2_4358 UCRNP2_7602
TASAA1Q1_05812
CCACCcaHIS019_0300570(CcaverHIS019_0300570)
PPLPOSPLDRAFT_105326 POSPLDRAFT_23052 POSPLDRAFT_32625 POSPLDRAFT_32934 POSPLDRAFT_87724
TVSTRAVEDRAFT_16216 TRAVEDRAFT_32834 TRAVEDRAFT_41389 TRAVEDRAFT_43869 TRAVEDRAFT_58559
DSQDICSQDRAFT_145027 DICSQDRAFT_166290 DICSQDRAFT_45577 DICSQDRAFT_97807
PCOPHACADRAFT_146035 PHACADRAFT_172966 PHACADRAFT_191006 PHACADRAFT_209510 PHACADRAFT_248683 PHACADRAFT_24951 PHACADRAFT_257104 PHACADRAFT_257977 PHACADRAFT_260263 PHACADRAFT_264550 PHACADRAFT_83218
SHSSTEHIDRAFT_135813 STEHIDRAFT_164296 STEHIDRAFT_168688 STEHIDRAFT_79346 STEHIDRAFT_87533
HIRHETIRDRAFT_442771 HETIRDRAFT_452336 HETIRDRAFT_453182
PSQPUNSTDRAFT_123020 PUNSTDRAFT_138973 PUNSTDRAFT_145991 PUNSTDRAFT_63080
ADLAURDEDRAFT_112126 AURDEDRAFT_143542
FMEFOMMEDRAFT_104528 FOMMEDRAFT_156448 FOMMEDRAFT_171632
GTRGLOTRDRAFT_140449 GLOTRDRAFT_38668 GLOTRDRAFT_40080 GLOTRDRAFT_95824
RSXRhiXN_11181
LBCLACBIDRAFT_298461
CCICC1G_00517 CC1G_03949 CC1G_05817
ABPAGABI1DRAFT107807(AGABI1DRAFT_107807) AGABI1DRAFT51593(AGABI1DRAFT_51593) AGABI1DRAFT54356(AGABI1DRAFT_54356)
ABVAGABI2DRAFT177137(AGABI2DRAFT_177137) AGABI2DRAFT214062(AGABI2DRAFT_214062) AGABI2DRAFT222486(AGABI2DRAFT_222486)
MPRMPER_09678 MPER_12697
MRRMoror_13689 Moror_2514 Moror_4784 Moror_4785 Moror_5271
MOREE1B28_001559 E1B28_003297 E1B28_005868 E1B28_006091
SCMSCHCO_01138368(SCHCODRAFT_01138368) SCHCO_02703927(SCHCODRAFT_02703927)
CPUTCONPUDRAFT_101102 CONPUDRAFT_119489 CONPUDRAFT_126201 CONPUDRAFT_166647 CONPUDRAFT_46841
SLASERLADRAFT_414770 SERLADRAFT_447765 SERLADRAFT_453461 SERLADRAFT_466343
UMAUMAG_05230
PFPPFL1_03158
SGRAEX895_004627
PIFPITG_17117
PSOJPHYSODRAFT_560104
IZHFEM41_17505(salA)
XSASB85_10110
XARXB05_19230
PSDDSC_14905
PWIMWN52_14975(salA)
PREPCA10_41220(nahG)
PFUWKF707C_16120(salA) KF707C_29620
PPGPputGB1_3586
PPIND016(nahG) ND091(nahG)
PPXT1E_5510(nahG)
PMOSO165_009705
PFNHZ99_03455
PKRAYO71_16495
PFXA7318_13845
PSKU771_15980
PSESPSCI_4557(nahG)
PFKPFAS1_28805
PPSLBJP27_11255
PSILPMA3_14235
PALLUYA_07000
PAZEKSS91_14745(salA)
PKKQQ992_18065(salA)
PSCA458_06545
PSTUUIB01_22720
PBMCL52_14690
ACCBDGL_001688(salR)
ALCOTEC02_06330
ACALBUM88_12490
ACDAOLE_06150
ACIACIAD1424(salA)
ATTAMQ28_00970
AJORZ95_18845 RZ95_19670
ACWA0J50_06110
ASOLBEN76_06835
ADVDJ533_02040(salA)
AGUAS4_21780(salA)
ABERBSR55_10845
CCAGSR908_06585(salA)
HAKKO116_00227
HHHCLM76_07000(salA)
HPIZGYM47_16310(salA)
HSVHNO53_19235(salA)
HTXEKK97_21235(salA)
HPROLMS44_22970(salA)
HBHE4T21_16500(salA)
HASOB2G49_18175
HNPSR894_21570(salA)
 » 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
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