ID   SGCD_STRGL              Reviewed;         493 AA.
AC   Q8GMH4;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=2-amino-4-deoxychorismate synthase;
DE            Short=ADIC synthase;
DE            EC=2.6.1.86;
GN   Name=sgcD;
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 COFACTOR.
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 chorismate to 2-amino-4-deoxychorismate (ADIC).
CC       Involved in the biosynthesis of the benzoxazolinate moiety of the
CC       enediyne antitumor antibiotic C-1027. {ECO:0000269|PubMed:18182490}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-amino-4-deoxychorismate + L-glutamate = chorismate + L-
CC         glutamine; Xref=Rhea:RHEA:25512, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58792; EC=2.6.1.86;
CC         Evidence={ECO:0000269|PubMed:18182490};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:18182490};
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {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; AAL06664.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GMH4; -.
DR   SMR; Q8GMH4; -.
DR   PRIDE; Q8GMH4; -.
DR   KEGG; ag:AAL06664; -.
DR   GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.60.120.10; -; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR015890; Chorismate_C.
DR   PANTHER; PTHR11236; PTHR11236; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; SSF56322; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Magnesium; Transferase.
FT   CHAIN           1..493
FT                   /note="2-amino-4-deoxychorismate synthase"
FT                   /id="PRO_0000418509"
SQ   SEQUENCE   493 AA;  53461 MW;  FCF46B5B4D06A036 CRC64;
     MTDQCVVSAP VRVRTRRLDV KETGALPAYR ALAEHFGPDE VYLLESAAGP ARDRRHQFVG
     FGALLSLSVT DRVVRVEGVP ALRGLLLERA GALLEDGPQG LRLRTAGGLW PLLRAMRDMF
     DAEGSASGFR FGFLGFFGYD TARYIEDLPH LIENRPGLPD VRMVLHRGSV VTDLATGRCE
     LLLHESPYWP GLAPETVTGL LADVEQAWPD PSADGFPASA VTDDSAPEVF ANDVERCLKH
     IAVGDIYQVQ IGHELSIRST ADPADVYQRL RGRNASPYMY LAGIDGHRLI GASPELFVRI
     EDGEVTMRPI AGTVPRSGAD GGIAAGVRLR SDPKEIAEHT MLVDLCRNDI GRIARPNTLD
     VPDQLDVEGY SHVLHLVSTV VGRARVDTDA FDTIAALFPA GTMTGAPKIR AMEIIESVER
     SRRGLYAGAL GLLDVGGYTN LALCIRTLFH HEGVYRTRAS AGIVADSEPG AEWTETLAKM
     SATHWAVTGE ELL