SGCG_STRGL
ID SGCG_STRGL Reviewed; 223 AA.
AC Q8GMH2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=2-amino-4-deoxychorismate dehydrogenase;
DE Short=ADIC dehydrogenase;
DE EC=1.3.8.16 {ECO:0000269|PubMed:18182490};
GN Name=sgcG;
OS Streptomyces globisporus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1908;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C-1027;
RX PubMed=12183628; DOI=10.1126/science.1072110;
RA Liu W., Christenson S.D., Standage S., Shen B.;
RT "Biosynthesis of the enediyne antitumor antibiotic C-1027.";
RL Science 297:1170-1173(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=C-1027;
RX PubMed=18182490; DOI=10.1073/pnas.0708750105;
RA Van Lanen S.G., Lin S., Shen B.;
RT "Biosynthesis of the enediyne antitumor antibiotic C-1027 involves a new
RT branching point in chorismate metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:494-499(2008).
CC -!- FUNCTION: Converts 2-amino-4-deoxychorismate (ADIC) to 3-O-
CC enolpyruvoylanthranilic acid (OPA). Involved in the biosynthesis of the
CC benzoxazolinate moiety of the enediyne antitumor antibiotic C-1027.
CC {ECO:0000269|PubMed:18182490}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-amino-4-deoxychorismate + FMN = 3-(1-
CC carboxyvinyloxy)anthranilate + FMNH2; Xref=Rhea:RHEA:25371,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58790,
CC ChEBI:CHEBI:58792; EC=1.3.8.16;
CC Evidence={ECO:0000269|PubMed:18182490};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56 uM for ADIC {ECO:0000269|PubMed:18182490};
CC KM=1.2 uM for FMN {ECO:0000269|PubMed:18182490};
CC Note=kcat is 15 sec(-1) for ADIC. kcat is 17 sec(-1) for FMN.;
CC -!- SIMILARITY: Belongs to the SsuE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY048670; AAL06666.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GMH2; -.
DR SMR; Q8GMH2; -.
DR KEGG; ag:AAL06666; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR005025; FMN_Rdtase-like.
DR Pfam; PF03358; FMN_red; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Antibiotic biosynthesis; Flavoprotein; FMN; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..223
FT /note="2-amino-4-deoxychorismate dehydrogenase"
FT /id="PRO_0000418510"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 223 AA; 24133 MW; 25B98C28B1C2581F CRC64;
MSAQLKILAI NGSERDGNTA DVLRHAARVA ENRGVDFEAV DLRSIRMERC GPCGDCNDRP
VACTLADGVP EVVAKMVAAD GIIFAAPVHG FGTASLMQTF IERAGVGYLR FDRPLSNKVA
GIISVARRYS AGEVWAQLTV NALLNRMILV GSGFPATVHA LHRGDALKDE EGLTNVSRLV
ERMTDMIELL DEHRRLTGRS DVLASNEVNE RVGLALNELQ AQP
