ID   PDXR_CORGL              Reviewed;         453 AA.
AC   Q8NS92; Q6M6Z5; Q79K85;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=HTH-type pyridoxine biosynthesis transcriptional regulator PdxR;
GN   Name=pdxR; OrderedLocusNames=Cgl0787, cg0897;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948641; DOI=10.1016/s0168-1656(03)00161-5;
RA   McHardy A.C., Tauch A., Rueckert C., Puehler A., Kalinowski J.;
RT   "Genome-based analysis of biosynthetic aminotransferase genes of
RT   Corynebacterium glutamicum.";
RL   J. Biotechnol. 104:229-240(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: May have a regulatory function in pyridoxine biosynthesis. Is
CC       said to also have an aminotransferase activity in valine biosynthesis
CC       as a double inactivation of ilvE and pdxR results in an auxotrophic
CC       requirement for valine. {ECO:0000269|PubMed:12948641}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000305};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC       pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
CC   -!- CAUTION: Ser-301 is present instead of the conserved Lys which is
CC       expected to be the pyridoxal phosphate-binding residue which is
CC       required for activity in all known pyridoxal-dependent
CC       aminotransferases. {ECO:0000305}.
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DR   EMBL; AY238321; AAO92312.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98180.1; -; Genomic_DNA.
DR   EMBL; BX927150; CAF19492.1; -; Genomic_DNA.
DR   RefSeq; NP_600015.1; NC_003450.3.
DR   RefSeq; WP_011013887.1; NC_006958.1.
DR   AlphaFoldDB; Q8NS92; -.
DR   SMR; Q8NS92; -.
DR   STRING; 196627.cg0897; -.
DR   DNASU; 1018782; -.
DR   KEGG; cgb:cg0897; -.
DR   KEGG; cgl:Cgl0787; -.
DR   PATRIC; fig|196627.13.peg.772; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_1_11; -.
DR   OMA; VEEPSYW; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00392; GntR; 1.
DR   PRINTS; PR00035; HTHGNTR.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; DNA-binding; Pyridoxal phosphate; Reference proteome;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN           1..453
FT                   /note="HTH-type pyridoxine biosynthesis transcriptional
FT                   regulator PdxR"
FT                   /id="PRO_0000305243"
FT   DOMAIN          15..83
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   DNA_BIND        43..62
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
SQ   SEQUENCE   453 AA;  48859 MW;  FB1A73A008A30E66 CRC64;
     MLADLPIALN PHEPTSIPTQ LTEQIRRLVA RGILTPGDPL PSSRSLSTQL GVSRGSVVTA
     YDQLAGEGYL STARGSGTTI NPDLHLLKPV EIEKKETSRS VPPPLLNLSP GVPDTATLAD
     SAWRAAWREA CAKPPTHSPE QGLLRLRIEI ADHLRQMRGL MVEPEQIIVT AGAREGLSLL
     LRTMDAPARI GVESPGYPSL RRIPQVLGHE TIDVPTDESG LVPRALPHDL NALLVTPSHQ
     YPYGGSLPAD RRTALVAWAE ANDALLIEDD FDSELRYVGM PLPPLRALAP DRTILLGTFS
     SVITPQVACG YLIAPTPQAR VLATLRGILG QPVGAITQHA LASYLASGAL RRRTQRLRRL
     YRHRRSIVQD TLGDLPNTQL RPINGGLHAV LLCDKPQDLV VTTLASRGLN VTALSHYWGG
     TGADNGIVFG FGSHDEDTLR WVLAEISDAV SLG