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Database: UniProt
Entry: E3HG14_ACHXA
LinkDB: E3HG14_ACHXA
Original site: E3HG14_ACHXA 
ID   E3HG14_ACHXA            Unreviewed;       503 AA.
AC   E3HG14;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Rhizopine catabolism regulatory protein MocR {ECO:0000313|EMBL:ADP17787.1};
GN   Name=mocR {ECO:0000313|EMBL:ADP17787.1};
GN   OrderedLocusNames=AXYL_04468 {ECO:0000313|EMBL:ADP17787.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17787.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP17787.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP17787.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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; CP002287; ADP17787.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3HG14; -.
DR   STRING; 762376.AXYL_04468; -.
DR   KEGG; axy:AXYL_04468; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_1_4; -.
DR   Proteomes; UP000006876; 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: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   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"
FT   REGION          94..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   503 AA;  55403 MW;  E536EC7284532DAC CRC64;
     MRSIVGDLLQ LRLADGSSEP MNKRLYRGIR EAILDGAIAA DSRLPASRDL AAELGIARNT
     VVHVYSQLLA EGYTRSRQGN GTFVNASVPD SYLASGRRMR QPPPAQPRPA LSPRGAAIVD
     GVSASPYQWG AFMPGVPDLT EFPHKKFGRI FSALWRNPSP DLLTYAYGGG LPALREALAQ
     HLALTRSIDC DPEQIIITEG SHQAIDLTTR ILGEAGETAW VEDPGYWGAR TVLQANGLHT
     VHLPVDEEGM RLPETVGTPP RFIFVTPSHQ YPLGPVMSLT RRRQLLAVAR QSGSWIIEDD
     YDSEFRFSGR PIASLLGLEP DAPVIYMGTF SKTLYPGLRV GYLVLPKTLT AAFQAAHAEL
     YREGHLMTHA ALATFISEGH YAAHIRRMRM LYGRRRAMLV NLIERRLGPD WLHRDASMAG
     LHLVLTLPED MDDLRVVDVA RGKGVLTRAL SRYYVNDEGR RPGLLLGYAC VPEHDIARKF
     EVLLESLNEV ARAPAALAVS GGR
//
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