KEGG   ENZYME: 1.14.14.54
Entry
EC 1.14.14.54               Enzyme                                 
Name
phenylacetate 2-hydroxylase;
CYP504;
phaA (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
phenylacetate,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (2-hydroxylating)
Reaction(IUBMB)
phenylacetate + [reduced NADPH---hemoprotein reductase] + O2 = (2-hydroxyphenyl)acetate + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R05487]
Reaction(KEGG)
R05487
Substrate
phenylacetate [CPD:C07086];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
2-hydroxyphenylacetate [CPD:C05852];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
This cytochrome P-450 (heme-thiolate) enzyme, found in Aspergillus nidulans, is involved in the degradation of phenylacetate.
History
EC 1.14.14.54 created 2017
Pathway
ec00360  Phenylalanine metabolism
ec00643  Styrene degradation
ec01100  Metabolic pathways
ec01120  Microbial metabolism in diverse environments
Orthology
K10437  phenylacetate 2-hydroxylase
Genes
PPAPAS_chr3_0864
DHADEHA2D03168g
PICPICST_49761
PGUPGUG_01534
SPAASPAPADRAFT_48604
CALCAALFM_C404360WA(CaO19.1411)
CTPCTRG_03930
COTCORT_0E04490
CDUCD36_44030
CTENCANTEDRAFT_117516
YLIYALI0F03663g
CLUCLUG_05046
CLUSA9F13_03g01892
CAURCJI96_0001268
SLBAWJ20_2948
BNNFOA43_001054
BBRXBRETT_003642
OPAHPODL_00882 HPODL_02307
MGRMGG_04684
PPEIPpBr36_05425
PGRIPgNI_02910
FGRFGSG_03741
FPUFPSE_08438
FPOAFPOAC1_006144
FVNFVRRES_06746
FVRFVEG_08703
FOXFOXG_09779
NHENECHADRAFT_102133 NECHADRAFT_54339
FFCNCS54_00875600 NCS54_01417700
FKRNCS57_01399500 NCS57_01448200
FMUJ7337_012635
TRETRIREDRAFT_4726
MAWMAC_08608
MAJMAA_10366
PCHMVFPPC_06705
CMTCCM_02553
AMUSLMH87_008733
PLJVFPFJ_10353 VFPFJ_11202
PTKZJDV02_003477 JDV02_008082
CFJCFIO01_05930
SAPOSAPIO_CDS6228 SAPIO_CDS6571
ELAUCREL1_9178
PFYPFICI_13076 PFICI_15387
SSLSS1G_06874
BFUBCIN_11g01060
MBEMBM_06099
PSCOLY89DRAFT_640579 LY89DRAFT_698231
GLZGLAREA_00187 GLAREA_06077
ANIANIA_08078
AFMAFUA_5G01710
ACTACLA_003600
NFINFIA_040380
AORAO090003001361
ANGAn12g04210 An16g01030
AFVAFLA_000316
ALUCAKAW2_60307S AKAW2_60829S AKAW2_70076A
APUUAPUU_21170S APUU_41450A APUU_41480A
PCSN7525_005978 N7525_007972
PDPPDIP_47610
POUPOX_a00016
TMFEYB26_004635 EYB26_004836 EYB26_006692
TRGTRUGW13939_03396 TRUGW13939_07699 TRUGW13939_10129
CIMCIMG_07017
CPWCPC735_033760
UREUREG_05848
PBLPAAG_08664
PBNPADG_07269
ABEARB_03198
TVETRV_03913
BGHBDBG_00176
PNOSNOG_06873 SNOG_07254
PTEPTT_06566 PTT_19143
BZECOCCADRAFT_96181 COCCADRAFT_97535
BSCCOCSADRAFT_148288 COCSADRAFT_148767
BORCOCMIDRAFT_40411 COCMIDRAFT_4778 COCMIDRAFT_7585
AALTCC77DRAFT_1030168 CC77DRAFT_779096
ARABEKO05_0001612
ZTRMYCGRDRAFT_32609(CYP-22) MYCGRDRAFT_83782(CYP-33)
PFJMYCFIDRAFT_185117 MYCFIDRAFT_201503
FFUCLAFUR5_00972 CLAFUR5_01627
CBETCB0940_00379 CB0940_00725
BCOMBAUCODRAFT_188720
NPAUCRNP2_1360 UCRNP2_5654
TASAA1Q1_06336
CCACCcaHIS019_0108630(CcaverHIS019_0108630)
SLASERLADRAFT_414563
UMAUMAG_01424
PFPPFL1_00039
SGRAEX895_001904
 » show all
Reference
1  [PMID:10329644]
  Authors
Mingot JM, Penalva MA, Fernandez-Canon JM
  Title
Disruption of phacA, an Aspergillus nidulans gene encoding a novel cytochrome P450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction.
  Journal
J Biol Chem 274:14545-50 (1999)
DOI:10.1074/jbc.274.21.14545
  Sequence
Reference
2  [PMID:11544206]
  Authors
Rodriguez-Saiz M, Barredo JL, Moreno MA, Fernandez-Canon JM, Penalva MA, Diez B.
  Title
Reduced function of a phenylacetate-oxidizing cytochrome p450 caused strong genetic improvement in early phylogeny of penicillin-producing strains.
  Journal
J Bacteriol 183:5465-71 (2001)
DOI:10.1128/JB.183.19.5465-5471.2001
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.54
IUBMB Enzyme Nomenclature: 1.14.14.54
ExPASy - ENZYME nomenclature database: 1.14.14.54
BRENDA, the Enzyme Database: 1.14.14.54

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