ID   C6DA18_PECCP            Unreviewed;       483 AA.
AC   C6DA18;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   02-SEP-2026, entry version 89.
DE   SubName: Full=Transcriptional regulator, GntR family with aminotransferase domain {ECO:0000313|EMBL:ACT13774.1};
GN   OrderedLocusNames=PC1_2744 {ECO:0000313|EMBL:ACT13774.1};
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13774.1, ECO:0000313|Proteomes:UP000002736};
RN   [1] {ECO:0000313|EMBL:ACT13774.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1 {ECO:0000313|EMBL:ACT13774.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC       pyridoxal-phosphate-dependent aminotransferase family.
CC       {ECO:0000256|ARBA:ARBA00005384}.
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DR   EMBL; CP001657; ACT13774.1; -; Genomic_DNA.
DR   RefSeq; WP_015840941.1; NC_012917.1.
DR   AlphaFoldDB; C6DA18; -.
DR   STRING; 561230.PC1_2744; -.
DR   PaxDb; 561230-PC1_2744; -.
DR   KEGG; pct:PC1_2744; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_0_6; -.
DR   OrthoDB; 9804020at2; -.
DR   Proteomes; UP000002736; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   FunFam; 3.40.640.10:FF:000023; Transcriptional regulator, GntR family; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR051446; HTH_trans_reg/aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR46577; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR   PANTHER; PTHR46577:SF2; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00392; GntR; 1.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ACT13774.1};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00307}; Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002736};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE-
KW   ProRule:PRU00307};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW   ECO:0000256|PROSITE-ProRule:PRU00307};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..69
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
FT   DNA_BIND        29..48
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00307"
SQ   SEQUENCE   483 AA;  53612 MW;  3650E270BD5C1D75 CRC64;
     MAKFEQLAHQ IREQLQEGIW QPGDKLPSLR EKSLHSGMSL MTVLHAYQLL ESQGLIVSRP
     QSGYYAAPQL SALPADSLHS PVGQERVQLT EDVDVNAFIF DVLQASKDPA VMPFGSAFPD
     PQLFPQRQLT RSLASVARHM QPQSALDNLP PGNESLRKNI AQRYALQGIA VSPDEIVITA
     GAMESLNLSL QVLTEPGDYV VIESPAFYGA LQAIERLKLK AIAIATDPQQ GIDLDALQQA
     LNDYPIKACW LMTNFHNPLG CTLSWEKKQQ LVAMLEKHGV GLVEDDVYSE LYAGLQRPLP
     AKALDKKGTI LHCSSFSKNL VAGFRVGWVA AGRYAGSIQR LQLMSTLSTS APMQLAIADY
     LATSSYDSHL RRLRRALEQR KHAALQSLRR HLPGDVRINH SQGGYFLWLE LPEGISSTEL
     YRRALARGVS IAPGKMFTTG DKYDRYFRFN ASYAWDDRCE QSVIVLAALI RTQIGERPPR
     SPL
//