ID Q138F3_RHOPS Unreviewed; 475 AA.
AC Q138F3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:ABE39536.1};
GN OrderedLocusNames=RPD_2304 {ECO:0000313|EMBL:ABE39536.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE39536.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE39536.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE39536.1,
RC ECO:0000313|Proteomes:UP000001818};
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., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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}.
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; CP000283; ABE39536.1; -; Genomic_DNA.
DR AlphaFoldDB; Q138F3; -.
DR STRING; 316057.RPD_2304; -.
DR KEGG; rpd:RPD_2304; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_1_5; -.
DR Proteomes; UP000001818; Chromosome.
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 CDD; cd00609; AAT_like; 1.
DR CDD; cd07377; WHTH_GntR; 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; 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:SF1; HTH-TYPE TRANSCRIPTIONAL REGULATORY PROTEIN GABR; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00392; GntR; 1.
DR PRINTS; PR00035; HTHGNTR.
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 1..69
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 475 AA; 52081 MW; A5BF71ED38CDE03D CRC64;
MPLHARIQRA IRQLIVDGAL GPGKPLPASR VLAKSLGVSR DTIEAAYAQL HAEGFIDRRV
GSGSFVAEMT EFTPGRRLSQ RDALSRNQAP NLSKRGAAMF HSGGVREMLS PRPFAHGVPE
TRTFPLQLWE RLERQVRKEV GVQTLLHGDP QGTEPLRRAI ADYVNLERGA RATADRVLVL
TSSQQAMSLC ANMLLDPGER IFIEDPAYYG ARKAFDAAGL ECVPIRVDRQ GIVVDQITAE
PRRAKAVFLT PSHQFPTGAT LTLDRRLALI EWATRHQAWI IEDDYDSEFH YAGKPTACVQ
GLDPHDRTIY IGTFTKSLFP GLRIGYVVLP PQLVKPMTVA RTLLDGHTAP MAQLTLARFM
EGGHFGAHVR TMRGVYAERL DVLARLVSKH LSDFVEPRVP TGGLQMPCLL SCAVSERVAI
DAARRVGIDL LGLSALHAGG DGKAGFLVGF AAYTPLEIEM AVKKLANALR TVMKP
//
