KEGG ENZYME: 1.13.11.80

ENZYME: 1.13.11.80

Entry

EC 1.13.11.80               Enzyme

Name

(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase;
DpgC

Class

Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen

Sysname

(3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase

Reaction(IUBMB)

(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA [RN:R06624]

Reaction(KEGG)

R06624

Substrate

3,5-dihydroxyphenylacetyl-CoA [CPD:C12324];
O2 [CPD:C00007]

Product

2-(3,5-dihydroxyphenyl)-2-oxoacetate [CPD:C12325];
CoA [CPD:C00010]

Comment

The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin.

History

EC 1.13.11.80 created 2015

Pathway

ec01055

Biosynthesis of vancomycin group antibiotics

ec01110

Biosynthesis of secondary metabolites

Orthology

K16427

(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase

Genes

SMAF:

D781_2329

SERM:

CLM71_12090

SRHZ:

FO014_21620

RBAD:

H2866_19115

XAL:

XALC_1061

XTN:	FD63_09800

XPR:	MUG10_21490

NBR:	O3I_032810

NTP:	CRH09_30860 CRH09_31735

NAD:	NCTC11293_04863(caiD_11)

NIE:	KV110_15725

NGP:	LTT66_10455

SRC:	M271_00275 M271_09135

SMAL:

SMALA_7753

SSOI:

I1A49_42600

SVE:

SVEN_0495

SCW:	TU94_04895

STRC:

AA958_31875

SPRI:

SPRI_0192 SPRI_7161

STSI:

A4E84_04180

SKY:	D0C37_02220

SALW:

CP975_31990

SPHW:

NFX46_19245

SSIA:

A7J05_04080

SFK:	KY5_6275 KY5_7442

SGD:	ELQ87_39215

SKA:	CP970_02985 CP970_09660

SGZ:	C0216_32520

SNK:	CP967_00240

SGAL:

CP966_31760

SAQU:

EJC51_23005

SSEO:

D0Z67_21850

STSU:

B7R87_00845

SVD:	CP969_02980

SROI:

IAG44_40625

SXN:	IAG42_36465

KAU:	B6264_25040

STRH:

GXP74_22705

KFL:

Kfla_4130

NDA:

Ndas_1737

ACTW:

F7P10_10110

AGRA:

AGRA3207_002328

AMAZ:

LUW76_44615

NOA:	BKM31_54185

NCX:	Nocox_13285(noc6)

NGN:	LCN96_07950

FRA:	Francci3_2456

SACC:

EYD13_07730(paaF)

AOI:	AORI_1504 AORI_5328

AJA:	AJAP_31995

AMYB:

BKN51_41565

AAB:	A4R43_07890

AMYY:

YIM_22215(caiD5)

AORI:

SD37_33600

AROO:

NQK81_15365

PBRO:

HOP40_32680

SESP:

BN6_47880

KUT:	JJ691_30280 JJ691_70270(dpgC)

KBU:	Q4V64_04795

MSAG:

GCM10017556_56570

MFEU:

H1D33_24985

ACTL:

L3i22_092820

AOU:	ACTOB_006416 ACTOB_006455

PFLA:

Pflav_008020

PRY:	Prubr_65000

» show all

Reference

1 [PMID:11752437]

Authors

Chen H, Tseng CC, Hubbard BK, Walsh CT

Title

Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.

Journal

Proc Natl Acad Sci U S A 98:14901-6 (2001)
DOI:10.1073/pnas.221582098

Reference

2 [PMID:17507985]

Authors

Widboom PF, Fielding EN, Liu Y, Bruner SD.

Title

Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis.

Journal

Nature 447:342-5 (2007)
DOI:10.1038/nature05702

Reference

3 [PMID:18004875]

Authors

Fielding EN, Widboom PF, Bruner SD

Title

Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC.

Journal

Biochemistry 46:13994-4000 (2007)
DOI:10.1021/bi701148b

Other DBs

ExplorEnz - The Enzyme Database:

1.13.11.80

IUBMB Enzyme Nomenclature:

1.13.11.80

ExPASy - ENZYME nomenclature database:

1.13.11.80

BRENDA, the Enzyme Database:

1.13.11.80

DBGET integrated database retrieval system