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Database: UniProt
Entry: A0A1G3KCA8_9SPHN
LinkDB: A0A1G3KCA8_9SPHN
Original site: A0A1G3KCA8_9SPHN 
ID   A0A1G3KCA8_9SPHN        Unreviewed;       491 AA.
AC   A0A1G3KCA8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=GntR family transcriptional regulator {ECO:0000313|EMBL:OHD03158.1};
GN   ORFNames=A3H25_15410 {ECO:0000313|EMBL:OHD03158.1};
OS   Sphingomonadales bacterium RIFCSPLOWO2_12_FULL_63_15.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX   NCBI_TaxID=1802170 {ECO:0000313|EMBL:OHD03158.1, ECO:0000313|Proteomes:UP000176465};
RN   [1] {ECO:0000313|EMBL:OHD03158.1, ECO:0000313|Proteomes:UP000176465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OHD03158.1}.
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DR   EMBL; MIAK01000006; OHD03158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3KCA8; -.
DR   Proteomes; UP000176465; 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          19..87
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
SQ   SEQUENCE   491 AA;  54178 MW;  D5E3740F051B72A4 CRC64;
     MLRPWTLLLK ERVKIAPDSP RYMQIAHGLV HEIERGRLQP GDYLPSSRDL AEALEVNRKT
     IVTAYEELIA QGWLASAGTR GTRVSTSLPR GETATTPHLP VAKAAAPDDT EYPFLAAPDR
     PIAVPVGHWR KLDEGVPDGR LLPADLLARA YRKAAEEAAR TNSLSYRDPR GSPDLRRAIA
     DMLRRQRGLM VSPDHICITR GSQMGVFLTA RILIRPGDAV LVERLTYEPA VAAFRACGAE
     IVTVGLDEDG VDVADVERAC RKHRVRAIFV TPHHQFPTTV SMRPDRRLRL LELARQFGFA
     VIEDDYDHEF HFGAQPLLPM ASYAPARVIY AGSMSKLLVP ALRIGYIAAA PQVIDALAYQ
     ISLIDGMGNS ITELVAAHLL QSGEVRRHIR KTAQIYAARR DAFARSLDAT LGDLIDYRVP
     DGGLAFWLRF RDLAALDRIE ARAPALGLSF ASSHSYAADD SAERGLRLGF ASLDEKEARA
     VLQALQDCTH N
//
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