KEGG ENZYME: 1.14.13.1

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

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

DBGET integrated database retrieval system