ID A0A014MAG8_9GAMM Unreviewed; 497 AA.
AC A0A014MAG8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Decarboxylase {ECO:0000313|EMBL:EXU75089.1};
GN ORFNames=BG55_13215 {ECO:0000313|EMBL:EXU75089.1};
OS Erwinia mallotivora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU75089.1, ECO:0000313|Proteomes:UP000019918};
RN [1] {ECO:0000313|EMBL:EXU75089.1, ECO:0000313|Proteomes:UP000019918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU75089.1,
RC ECO:0000313|Proteomes:UP000019918};
RA Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA Mat Amin N.;
RT "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT pathogen.";
RL Submitted (FEB-2014) 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:EXU75089.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JFHN01000052; EXU75089.1; -; Genomic_DNA.
DR RefSeq; WP_034938130.1; NZ_VFIK01000001.1.
DR AlphaFoldDB; A0A014MAG8; -.
DR STRING; 69222.BG55_13215; -.
DR PATRIC; fig|69222.5.peg.2709; -.
DR OrthoDB; 9808770at2; -.
DR Proteomes; UP000019918; 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 Reference proteome {ECO:0000313|Proteomes:UP000019918};
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 497 AA; 54689 MW; F7D314E25D7E6F7C CRC64;
MRTLLGDLLA HRLSQAPAGA LNKRLYDVLQ AAIQEGAIAT GSRLPASRDL AKELGVSRNT
VLAAYEQLQS EGYLQTRTGS GTFVSEQLPE VAPENSEPEL VSARPFRYAS LSRRGIRVLT
RSGAGAYQWG AFMPGVPDVS HMPHDIWRKI QLRLSRRMPV EALSYSSHGG CLQLQQALAD
YLRVIRSLNC THDQILITAG THQSLDLLAK MLCDPGDGAW IEEPGYWGFR NVLAVNGVEL
LPTPVDEQGM VLPDIAARDN QTPLPKLICV TPSHQYPLGS VMSLQRRQQL LALAKSSGSW
VVEDDYDGEF RFGDTPIPAL QGLSADAPVI YLGTFSKSLY PGLRLSYMVV PKPLAARMKM
AHSELYRGGN GLVQLTLAEF IREGHYAAHV RRMRQLYSRR RDALVEVITT RLGPAFLASQ
SNAGLHLILS LPDSIDDVAL AAELEQTGIL TRPLSAYYLS GTQRRGLLLG YACVEEQQMA
ATFEPVLHCL QRRLQPA
//
