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Database: UniProt
Entry: A0A1V3Q4X8_9GAMM
LinkDB: A0A1V3Q4X8_9GAMM
Original site: A0A1V3Q4X8_9GAMM 
ID   A0A1V3Q4X8_9GAMM        Unreviewed;       494 AA.
AC   A0A1V3Q4X8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:OOG59390.1};
GN   ORFNames=B0E48_00740 {ECO:0000313|EMBL:OOG59390.1};
OS   Rhodanobacter sp. C03.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1945858 {ECO:0000313|EMBL:OOG59390.1, ECO:0000313|Proteomes:UP000189128};
RN   [1] {ECO:0000313|EMBL:OOG59390.1, ECO:0000313|Proteomes:UP000189128}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C03 {ECO:0000313|EMBL:OOG59390.1,
RC   ECO:0000313|Proteomes:UP000189128};
RA   Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA   Frostegard A.;
RT   "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT   isolation strategy.";
RL   Submitted (FEB-2017) 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   -!- 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:OOG59390.1}.
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DR   EMBL; MUNT01000001; OOG59390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V3Q4X8; -.
DR   STRING; 1945858.B0E48_00740; -.
DR   OrthoDB; 9808770at2; -.
DR   Proteomes; UP000189128; 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; 3.40.640.10; 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          9..77
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
SQ   SEQUENCE   494 AA;  54686 MW;  0667FA138709793C CRC64;
     MFLELDGQGP QYRQLIRALR AAILSGRLLA HARLPSTREL ALELGCSRIT VLTAYEQLRA
     DGYIDGQVGS GSYVNALPIE TMPLPQVNTT TIAAQSRFAE RARQYQGLPI AELHRGTRFN
     LQYGSSHINP SLSAIWAREL SWAAIQSPLG YGADQGLLAL REQICSYLSL RRGIQTSVDR
     VLIVSGTQQA IALTARVLLN EGDTVAIEEP HYWGAWQQFS AHGARLLPIR SDNEGLLCNE
     LPTVAPRLVL VTPAHQFPTG SVLSLTRRIE LLSYADRASC WIVEDDYDSE LRYDSQPLAT
     LHSLDTRDRV IYVGTLSKVM FGALRLGYMV LPQALRADFV SAKCLDDRGC PTIEQAALAH
     FMEDGGFERH LRFVTRELRS RRGELIESLH RHAGERVQIG GTHAGMHVVV WLPDYDHAQI
     DALIALAHER GLGLHSVAPH YDECPVVPGL ILGYCGLSKA QLRDATQLFG ECLDTIDAIA
     RRHDTKQAVK YASS
//
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