ID A5W407_PSEP1 Unreviewed; 460 AA.
AC A5W407;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:ABQ78867.1};
GN OrderedLocusNames=Pput_2733 {ECO:0000313|EMBL:ABQ78867.1};
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746 {ECO:0000313|EMBL:ABQ78867.1};
RN [1] {ECO:0000313|EMBL:ABQ78867.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F1 {ECO:0000313|EMBL:ABQ78867.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) 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; CP000712; ABQ78867.1; -; Genomic_DNA.
DR AlphaFoldDB; A5W407; -.
DR KEGG; ppf:Pput_2733; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_0_6; -.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd00609; AAT_like; 1.
DR CDD; cd07377; WHTH_GntR; 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.
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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 5..73
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 460 AA; 49775 MW; 0CE40021CA6EF076 CRC64;
MKRDGTRIRT VMGEIQSRIA SRTYTPGARI PSVRAMAQAM QVSVSTVLEA YERLMAEGVL
NSRPGSGFYV AGPVAPLVLT ELGPRLDREV DPLWISRQSL DTASDALKPG CGWLPASWMF
EAGLRKALRT VARSDTSKLT EYASPLGHLP LRQFLSRKLT GIGVEAPLEQ LMLTESGTHA
IDLVCRFLLE PGDTVLVDDP CYFNFHALLK AHRVNIVGVP YTATGPDIDA FGAALLAHSP
RLYITNSGIH NPTGATLSPV TAHRLLKLAD NSSLVIVEDD IFGDFESAPA PRLSAFDGLS
RVIQIGSFSK TISASIRCGY IAARSDWIES LVDLKIATTF GGGRLAADII HLAITDSGYR
KHMESVRLRL AEAMDRTVAR LRAIGIKPWI TPQSGMYVWC QLPQGKDAAT LARACLNEGV
VLAPGNAFSQ SMAAGDFLRF NVAQSGDAKI YEVLKRALSA
//
