ID A2SIK7_METPP Unreviewed; 449 AA.
AC A2SIK7;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Transcriptional regulator, GntR family {ECO:0000313|EMBL:ABM95396.1};
GN OrderedLocusNames=Mpe_A2441 {ECO:0000313|EMBL:ABM95396.1};
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=420662 {ECO:0000313|EMBL:ABM95396.1, ECO:0000313|Proteomes:UP000000366};
RN [1] {ECO:0000313|EMBL:ABM95396.1, ECO:0000313|Proteomes:UP000000366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1
RC {ECO:0000313|Proteomes:UP000000366};
RX PubMed=17158667; DOI=10.1128/JB.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM95396.1; -; Genomic_DNA.
DR AlphaFoldDB; A2SIK7; -.
DR STRING; 420662.Mpe_A2441; -.
DR KEGG; mpt:Mpe_A2441; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_0_4; -.
DR Proteomes; UP000000366; 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 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:UP000000366};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..56
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 449 AA; 48846 MW; 8775CDCDFEB621C7 CRC64;
MVLDGRLPVM TRLPSERSLA AELAISRTTV AAAYDLLRQC GFLQSQQGSG TWIALPEDVD
SKATAPWLPG AARSELDLSH AALSAPVEVF HSAMAEATGQ LSIHLRGHGY NLLGLPKLRE
VVAARFSARG LPTHAEQVLI TSGAQQALSL AIMAFADHGS KVIVEHPTYP NALDAIRQRG
ARPVPVPFNE GKWDLDLIAS TMRDSGAQLG YFVPDFHNPT GLCMSPADRK QLVLAAHRTR
TPLIIDETLV ELGIEHDAPE PTGVYGSEEA TPIVTIGSAS KIFWGGIRVG WLRAPAAVIR
KVAGLRPPLD MSSPILEQLI VASLFPRLHE VVAHRRQVLR TARDELVSQL NNHIPEWRPT
RALGGLSLWV DLQERISSRF VSAAGHAGVL LSAGPRFGID DAFERFVRLP FTVPTETSNE
AIRRLAEVWR AMHSQSPAGD VRRGPRLPI
//
