ID A0A1E4IG76_9PROT Unreviewed; 467 AA.
AC A0A1E4IG76;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=GntR family transcriptional regulator {ECO:0000313|EMBL:ODU08671.1};
GN ORFNames=ABS91_03470 {ECO:0000313|EMBL:ODU08671.1};
OS Thiobacillus sp. SCN 64-35.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660150 {ECO:0000313|EMBL:ODU08671.1, ECO:0000313|Proteomes:UP000094432};
RN [1] {ECO:0000313|EMBL:ODU08671.1, ECO:0000313|Proteomes:UP000094432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
CC -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC pyridoxal-phosphate-dependent aminotransferase family.
CC {ECO:0000256|ARBA:ARBA00005384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODU08671.1}.
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DR EMBL; MEFJ01000074; ODU08671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4IG76; -.
DR Proteomes; UP000094432; Unassembled WGS sequence.
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; 3.90.1150.10; 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 2..70
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 467 AA; 50443 MW; 254BE79A6C4DC4BA CRC64;
MRSRYRQLAD EIAQHIERGV YAAGDRLPSV RALARSRGVS VVTVVTAYQT LLDEGRIEAR
PRSGFYVRAQ RPIQPIEAES GASAVPPRPV TGQAMAMTLI KAANTSGIVQ LGAAVPDPSF
LPTQAIGRAM AQVMRTRRAQ AAGYMMPPGA PELRRQIARR MSENGAGVAA DDIVVTTGCQ
EALSLALRAV TRPGDVVAVE SPAFYGLLHV LESLGLEALE IPARPRDGPA LDALAFALER
WPVRACVLAP NYGNPLGYCM PDEIKRALIR LLGRHRVPLI EDDVYGDLGF GVPRPSTCKG
LAPRADILYC SSFSKTLSPG LRVGWIAAGR HHARVEYLKY VTSIASPTAP QLAVADLLAG
GRYERHLREI RGKYASAVAR MSDRVMEVFP EGTRISQPQG GFVLWVELPE GTDSVALARR
ALRQGVSVAP GPLFSASGKY GNFIRLSCAR VWDAQLDRAL LTLAKLL
//
