ID B1Y0L8_LEPCP Unreviewed; 482 AA.
AC B1Y0L8;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Transcriptional regulator, GntR family with aminotransferase domain {ECO:0000313|EMBL:ACB32999.1};
GN OrderedLocusNames=Lcho_0726 {ECO:0000313|EMBL:ACB32999.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB32999.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB32999.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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; CP001013; ACB32999.1; -; Genomic_DNA.
DR AlphaFoldDB; B1Y0L8; -.
DR STRING; 395495.Lcho_0726; -.
DR KEGG; lch:Lcho_0726; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_0_4; -.
DR Proteomes; UP000001693; 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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:ACB32999.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:ACB32999.1}.
FT DOMAIN 10..78
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 482 AA; 51951 MW; 0B6FBF9E5AD9D819 CRC64;
MLTMDNPTAL PRYQQLADDL GEAMRSGVLR PGDRLPSVRE TCRERGLSPA TVFHAYGQLE
AEGLIEARPR SGYFVCTPRR ALRAPPRAAP ASSTAQPVAV SALVFDLLGS TSRPGVVPLG
SAFPAAHLFP FEALARSGAR TMRKLGPAQI TGALLSGDDG LRQALRRRYA LHGVALADDE
LVITNGAMEA LNLCLQAVTQ PGDVVVVESP TFYAALHALE RLHLQAVEVR TDPQEGVDLA
ALEALLAAQP VAACWFMPSF QNPLGALMPA ARKQALVELL ARHRVPLIED DVYGELHAGA
RRPLPAKAFD RDGGVLHCAS FSKCLAPGYR VGWAAAGRYT AQVQRLKMMS SLATALPPQM
ALADYLGQGV YDRHLRQLRA ALAAQQRRAL RLIERHFPAG TRVTRPSGGY FLWLDLPEAV
DGVTLHRRAM ALSISTAPGV LFSADARFAH HLRLNVGHPD DPRVDAALRT LGELACEMAA
GR
//
