ID   CMLC_STRVP              Reviewed;         328 AA.
AC   F2RB78;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=4-amino-4-deoxyprephenate dehydrogenase {ECO:0000305};
DE            EC=1.3.1.121 {ECO:0000305|PubMed:11577160};
GN   Name=cmlC {ECO:0000303|PubMed:11577160};
GN   OrderedLocusNames=SVEN_0919 {ECO:0000312|EMBL:CCA54206.1};
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=953739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC   04745;
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Chandra G., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
RN   [2]
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC   04745;
RX   PubMed=11577160; DOI=10.1099/00221287-147-10-2817;
RA   He J., Magarvey N., Piraee M., Vining L.C.;
RT   "The gene cluster for chloramphenicol biosynthesis in Streptomyces
RT   venezuelae ISP5230 includes novel shikimate pathway homologues and a
RT   monomodular non-ribosomal peptide synthetase gene.";
RL   Microbiology 147:2817-2829(2001).
CC   -!- FUNCTION: Involved in chloramphenicol biosynthesis (PubMed:11577160).
CC       Probably catalyzes the formation of 3-(4-aminophenyl)pyruvate from 4-
CC       amino-4-deoxyprephenate (Probable). {ECO:0000269|PubMed:11577160,
CC       ECO:0000305|PubMed:11577160}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-amino-4-deoxyprephenate + NAD(+) = 3-(4-aminophenyl)pyruvate
CC         + CO2 + H(+) + NADH; Xref=Rhea:RHEA:59380, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:143070, ChEBI:CHEBI:143071; EC=1.3.1.121;
CC         Evidence={ECO:0000305|PubMed:11577160};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59381;
CC         Evidence={ECO:0000305|PubMed:11577160};
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:11577160}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene causes severe decrease in
CC       chloramphenicol production. {ECO:0000269|PubMed:11577160}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; FR845719; CCA54206.1; -; Genomic_DNA.
DR   RefSeq; WP_015032125.1; NZ_CP029197.1.
DR   AlphaFoldDB; F2RB78; -.
DR   SMR; F2RB78; -.
DR   STRING; 953739.SVEN_0919; -.
DR   EnsemblBacteria; CCA54206; CCA54206; SVEN_0919.
DR   KEGG; sve:SVEN_0919; -.
DR   PATRIC; fig|953739.5.peg.2965; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_036672_1_1_11; -.
DR   OMA; TDGLGKW; -.
DR   BioCyc; MetaCyc:MON-20702; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003099; Prephen_DH.
DR   Pfam; PF02153; PDH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Oxidoreductase; Reference proteome.
FT   CHAIN           1..328
FT                   /note="4-amino-4-deoxyprephenate dehydrogenase"
FT                   /id="PRO_0000447221"
FT   DOMAIN          6..284
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT   REGION          254..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   328 AA;  33830 MW;  686F9AF61D818E30 CRC64;
     MSGFPRSVVV GGSGAVGGMF AGLLREAGSR TLVVDLVPPP GRPDACLVGD VTAPGPELAA
     ALRDADLVLL AVHEDVALKA VAPVTRLMRP GALLADTLSV RTGMAAELAA HAPGVQHVGL
     NPMFAPAAGM TGRPVAAVVT RDGPGVTALL RLVEGGGGRP VRLTAEEHDR TTAATQALTH
     AVILSFGLAL ARLGVDVRAL AATAPPPHQV LLALLARVLG GSPEVYGDIQ RSNPRAASAR
     RALAEALRSF AALIGDDPDR AEDPDRADDP DRTDNPGHPG GCDGAGNLDG VFEELRRLMG
     PELAAGQDHC QELFRTLHRT DDEGEKDR