ID B3R154_CUPTR Unreviewed; 472 AA.
AC B3R154;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Transcriptional regulator, GntR family with aminotransferase activity {ECO:0000313|EMBL:CAQ69464.1};
DE EC=2.6.1.1 {ECO:0000313|EMBL:CAQ69464.1};
GN OrderedLocusNames=RALTA_A1516 {ECO:0000313|EMBL:CAQ69464.1};
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ69464.1, ECO:0000313|Proteomes:UP000001692};
RN [1] {ECO:0000313|EMBL:CAQ69464.1, ECO:0000313|Proteomes:UP000001692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC R1 {ECO:0000313|Proteomes:UP000001692};
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69464.1; -; Genomic_DNA.
DR RefSeq; WP_012352787.1; NC_010528.1.
DR AlphaFoldDB; B3R154; -.
DR GeneID; 29761200; -.
DR KEGG; cti:RALTA_A1516; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_0_4; -.
DR BioCyc; CTAI977880:RALTA_RS07265-MONOMER; -.
DR Proteomes; UP000001692; Chromosome 1.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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; 3.90.1150.10; 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 Aminotransferase {ECO:0000313|EMBL:CAQ69464.1};
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};
KW Transferase {ECO:0000313|EMBL:CAQ69464.1}.
FT DOMAIN 1..69
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 472 AA; 51813 MW; 131C56997FC8E1A5 CRC64;
MKRYEALAET LAADIRNGSL PPGTRLPSIR KTVAQYGVSP STAFQAYYRL EERGLVRARE
RSGYYVAGPA RRELPQPQAR PSRQVSTQVD ISKLVFAVLE GARDRELVQF GSAFPSPELF
PWERLGKSLA RAGRALDPWY SVNDLPPGNA ALRRQIALRY LGAGAPQPAE DLVVTNGALE
ALNLCLMAVT QPGDVVAIES PGFYASLQAL ERLRLKAVEI PVDPAEGIDL GALDTALSRH
PVKACWFMTQ FQNPLGASMS EDKKKALVAL LARHQVPLIE DDVYGELYFG NRCPLPAKAF
DTHGLVMHCS SFSKTLAPGF RIGWVAPGRF GEAIQRLKLM TTLSAGVPTQ VALAEYLQHG
GYDKHLRKLR HVLEMQQGRM IDAIGQHFPE EVRVSRPEGG YFLWVEFAAD FDALALHHAA
LEAGIGIAPG PIFSARQGYR NCIRLNYGHL WNEDAETAVA TLGRLIAQQQ AG
//