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Information on EC 1.14.13.172 - salicylate 5-hydroxylase for references in articles please use BRENDA:EC1.14.13.172
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EC Tree
IUBMB Comments This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7, ferredoxin---NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
The enzyme appears in viruses and cellular organisms
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SALD
enzyme complex component
nagG
-
-
gene name
-
nagG
gene name; oxygenase component
NagGH
-
nagH
-
-
gene name
-
S5H
-
S5H
a three-component system consisting of NagGH (the oxygenase components), NagAa (ferredoxin reductase), and NagAb (ferredoxin)
S5H
; a three-component system consisting of NagGH (the oxygenase components), NagAa (ferredoxin reductase), and NagAb (ferredoxin)
-
SAL5H
-
-
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salicylate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
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salicylate,NADH:oxygen oxidoreductase (5-hydroxylating)
This enzyme, which was characterized from the bacterium Ralstonia sp. U2, comprises a multicomponent system, containing a reductase that is an iron-sulfur flavoprotein (FAD; EC 1.18.1.7, ferredoxin---NAD(P)+ reductase), an iron-sulfur oxygenase, and ferredoxin.
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2,4-dihydroxybenzoate + NADH + H+ + O2
?
2,6-dihydroxybenzoate + NADH + H+ + O2
?
2-nitrophenol + NADH + H+ + O2
?
anthranilate + NADH + H+ + O2
5-hydroxyanthranilate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
additional information
?
-
2,4-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2,4-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2,6-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2,6-dihydroxybenzoate + NADH + H+ + O2
?
-
-
-
?
2-nitrophenol + NADH + H+ + O2
?
-
-
-
?
2-nitrophenol + NADH + H+ + O2
?
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
-
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
-
-
-
-
?
additional information
?
-
2-aminobenzoate might be a substrate for the enzyme
-
-
-
additional information
?
-
-
no activity is detected against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate, and 2-hydroxyacetophenone
-
-
-
additional information
?
-
-
no activity is detected against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate, and 2-hydroxyacetophenone
-
-
-
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salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
Q0KB56
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADH + H+ + O2
2,5-dihydroxybenzoate + NAD+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
O52379 and O52380
-
-
-
?
salicylate + NADPH + H+ + O2
2,5-dihydroxybenzoate + NADP+ + H2O
O52379 and O52380
-
-
-
?
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additional information
SalABCD requires NAD(P)H as the cofactor instead of BH4
-
NADH
-
-
NADPH
-
-
[2Fe-2S]-center
-
-
[2Fe-2S]-center
contains a Rieske-type iron-sulfur center
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Iron
-
the enzyme contains one Rieske-type [2Fe-2S] cluster and 7.5 g iron per mol enzyme
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0.9398
2,6-dihydroxybenzoate
-
in 50 mM MES buffer (pH 6.4), at 22°C
0.3284
2-Nitrophenol
-
in 50 mM MES buffer (pH 6.4), at 22°C
0.05976
NADH
-
in 50 mM MES buffer (pH 6.4), at 22°C
0.05641
NADPH
-
in 50 mM MES buffer (pH 6.4), at 22°C
0.1071
salicylate
-
in 50 mM MES buffer (pH 6.4), at 22°C
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0.051
-
in 50 mM MES buffer, pH 6.4, at 30°C
107.1
-
after 124fold purification, in 50 mM MES buffer (pH 6.4), at 22°C
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-
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
large oxygenase component and small oxagenase component
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
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physiological function
enzyme S5H hydroxylates salicylate into gentisate and is involved in the degradation of aromatic compounds. SalD is an essential component of the S5H complex
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NAGG_RALSP
Ralstonia sp
423
0
48795
Swiss-Prot
NAGH_RALSP
Ralstonia sp
161
0
18813
Swiss-Prot
A0A1Y5TZI0_9PROT
390
0
43446
TrEMBL
A0A1A8T883_9GAMM
73
0
8355
TrEMBL
A0A222C6W5_9BURK
Achromobacter sp
280
0
31717
TrEMBL
A0A2S6TEP4_9PROT
148
0
16933
TrEMBL
A0A2S6TEC1_9PROT
161
0
19024
TrEMBL
A0A1E7WQZ8_9BURK
366
0
42361
TrEMBL
A0A2S6Q8V4_9PROT
164
0
18991
TrEMBL
A0A0P0M7T9_9BURK
375
0
42848
TrEMBL
A0A2J7VWZ0_9BURK
157
0
18264
TrEMBL
A0A2C9D914_9RHIZ
378
1
42866
TrEMBL
A0A375D7G9_9BURK
429
0
49048
TrEMBL
A0A375CMC1_9BURK
429
0
49064
TrEMBL
A0A222C6V3_9SPHI
Sphingobacterium sp
299
0
34106
TrEMBL
A0A1Y0EGE6_9RHOB
934
0
102253
TrEMBL
A0A375I518_9BURK
429
0
48908
TrEMBL
A0A395L9J8_9RHIZ
428
0
48059
TrEMBL
A0A3P4B6X7_9BURK
160
0
18921
TrEMBL
A0A1A9GNE8_9ACTN
421
0
46694
TrEMBL
A0A375JBS9_9BURK
429
0
49005
TrEMBL
A0A375C4T5_9BURK
429
0
48997
TrEMBL
A0A222C6X2_BURSP
Burkholderia sp
279
0
31665
TrEMBL
A0A1E7VM83_9BURK
366
0
42361
TrEMBL
A0A375GGX3_9BURK
417
0
47832
TrEMBL
A0A375FPI9_9BURK
429
0
49113
TrEMBL
A0A142XIH9_9BACT
369
0
41825
TrEMBL
A0A3P4AX35_9BURK
433
0
49527
TrEMBL
A0A149VR05_9PROT
367
0
42244
TrEMBL
A0A0H2M2V4_VARPD
421
0
48299
TrEMBL
A0A0H2MHW5_VARPD
156
0
18319
TrEMBL
A0A3P4AXY6_9BURK
160
0
17657
TrEMBL
A0A2R8AAM7_9RHOB
385
0
42726
TrEMBL
A0A375GDT1_9BURK
429
0
49075
TrEMBL
A0A0P0MEV8_9BURK
377
0
43039
TrEMBL
A0A1K0IH49_CUPNE
429
0
48959
TrEMBL
A0A1X7BUI1_9RHOB
386
0
43669
TrEMBL
A0A1E7W1V1_9BURK
366
0
42252
TrEMBL
A0A1W6THU0_VIBAL
395
0
44773
TrEMBL
A0A3P4B5X1_9BURK
420
0
48272
TrEMBL
A0A1X6ZKP7_9RHOB
363
0
41054
TrEMBL
A0A1X6YMU6_9RHOB
384
0
43299
TrEMBL
A0A1Y5RBW5_9PROT
412
0
46615
TrEMBL
A0A2J7VXR4_9BURK
436
0
49753
TrEMBL
A0A0P0MGR6_9BURK
417
0
47482
TrEMBL
A0A1N7RY79_9BURK
176
0
20116
TrEMBL
A0A2J7VWY2_9BURK
421
0
48365
TrEMBL
A0A1X7BQB8_9RHOB
388
0
44376
TrEMBL
A0A222C6V9_9GAMM
Stenotrophomonas sp
292
0
33140
TrEMBL
A0A0P0LHE4_9BURK
421
0
48410
TrEMBL
A0A0P0MB66_9BURK
162
0
18706
TrEMBL
A0A0H2M5X9_VARPD
436
0
49708
TrEMBL
A0A100J2Q5_9ACTN
413
0
45782
TrEMBL
A0A0B5FBJ0_9BURK
157
0
18268
TrEMBL
A0A375DSN7_9BURK
429
0
49060
TrEMBL
A0A0K1ZLS8_RALSL
418
0
47441
TrEMBL
A0A375FJ80_9BURK
156
0
18251
TrEMBL
A0A3P4B755_9BURK
419
0
48151
TrEMBL
A0A2J7VXB4_9BURK
378
0
43059
TrEMBL
A0A375FBD1_9BURK
429
0
49062
TrEMBL
Q0KB56_CUPNH
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
397
0
45709
TrEMBL
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20000
-
3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
45000
-
4 * 45000, SDS-PAGE
48799
x * 48799 + x * 18800, calculated from amino acid sequence
51000
-
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence
52000
-
3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
18800
-
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence
18800
x * 48799 + x * 18800, calculated from amino acid sequence
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?
x * 48799 + x * 18800, calculated from amino acid sequence
?
-
x * 48799 + x * 18800, calculated from amino acid sequence
-
heterohexamer
-
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence; 3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
heterohexamer
-
3 * 51000 + 3 * 18800, His6-tagged enzyme, calculated from amino acid sequence; 3 * 52000 + 3 * 20000, His6-tagged enzyme, SDS-PAGE
-
homotetramer
-
4 * 45000, SDS-PAGE
homotetramer
-
4 * 45000, SDS-PAGE
-
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additional information
precursor-directed biosynthesis of 5-hydroxytryptophan using metabolically engineered Escherichia coli and involving the salicylate 5-hydroxylase from Ralstonia eutropha strain H16
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the three-component Fe-S protein complex (NagAaGHAb) of the enzyme is purified by HisTrap column chromatography and Sephadex G-25 gel filtration
-
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enzyme S5H is encoded in the salABCD gene cluster, which locates on the chromosome rather than on a mobile plasmid, functional recombinant expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)/pLysS cells
-
expressed in Escherichia coli DH5alpha cells
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Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y.
Physicochemical and immunochemical characterization of salicylate 5-hydroxylase, m-hydroxybenzoate 6-hydroxylase and p-hydroxybenzoate 3-hydroxylase from Rhodococcus erythropolis
Biotechnol. Lett.
17
1063-1068
1995
Rhodococcus erythropolis, Rhodococcus erythropolis S1
-
brenda
Fang, T.; Zhou, N.Y.
Purification and characterization of salicylate 5-hydroxylase, a three-component monooxygenase from Ralstonia sp. strain U2
Appl. Microbiol. Biotechnol.
98
671-679
2014
Ralstonia sp. (O52379 and O52380), Ralstonia sp., Ralstonia sp. U2 (O52379 and O52380)
brenda
Fuenmayor, S.L.; Wild, M.; Boyes, A.L.; Williams, P.A.
A gene cluster encoding steps in conversion of naphthalene to gentisate in Pseudomonas sp. strain U2
J. Bacteriol.
180
2522-2530
1998
Pseudomonas sp. (O52379 and O52380), Pseudomonas sp., Pseudomonas sp. U2 (O52379 and O52380)
brenda
Zhou, N.Y.; Al-Dulayymi, J.; Baird, M.S.; Williams, P.A.
Salicylate 5-hydroxylase from Ralstonia sp. strain U2: a monooxygenase with close relationships to and shared electron transport proteins with naphthalene dioxygenase
J. Bacteriol.
184
1547-1555
2002
Ralstonia sp. (O52379 and O52380), Ralstonia sp., Ralstonia sp. U2 (O52379 and O52380)
brenda
Sun, X.; Lin, Y.; Yuan, Q.; Yan, Y.
Precursor-directed biosynthesis of 5-hydroxytryptophan using metabolically engineered E. coli
ACS Synth. Biol.
4
554-558
2015
Cupriavidus necator (Q0KB56)
brenda
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1.14.13.172 salicylate 5-hydroxylase
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