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Database: UniProt
Entry: B4SME1_STRM5
LinkDB: B4SME1_STRM5
Original site: B4SME1_STRM5 
ID   B4SME1_STRM5            Unreviewed;       459 AA.
AC   B4SME1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=Transcriptional regulator, GntR family with aminotransferase domain {ECO:0000313|EMBL:ACF50618.1};
GN   OrderedLocusNames=Smal_0913 {ECO:0000313|EMBL:ACF50618.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50618.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50618.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50618.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA   Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) 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}.
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DR   EMBL; CP001111; ACF50618.1; -; Genomic_DNA.
DR   RefSeq; WP_012510255.1; NC_011071.1.
DR   AlphaFoldDB; B4SME1; -.
DR   STRING; 391008.Smal_0913; -.
DR   KEGG; smt:Smal_0913; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_0_0_6; -.
DR   OrthoDB; 9802328at2; -.
DR   Proteomes; UP000001867; 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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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; IPR015422; PyrdxlP-dep_Trfase_small.
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:SF2; TRANSCRIPTIONAL REGULATORY PROTEIN; 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   Aminotransferase {ECO:0000313|EMBL:ACF50618.1};
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};
KW   Transferase {ECO:0000313|EMBL:ACF50618.1}.
FT   DOMAIN          5..73
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
SQ   SEQUENCE   459 AA;  50110 MW;  E5FBA2B655058A70 CRC64;
     MPRSLTRIES VIQTVRTRIG ARVDGPGSRL PSVRAQAAAM GVSVSTVVEA YERLAAEGLI
     SARAGSGFYV SGPAAPLALA EMEPRLDRAV DPLWVSRQSL ETPAGHLKPG CGWMPSDWLY
     HDGMRRGLRR LARADASQLV DYAGPLGLPA LRQLLQRRSA AVGIDAPMEQ ILLTESGTHS
     VELICRFLLK PGDCVLVDDP SYFNYHALLK AHQVQAIGVP YTHSGPDLEA FAQALQAHSP
     RLYITNSGLH NPTGAILSAS TAHRLLGLAE RSELIIVEDD IFADFELQPA PRLAALDGLS
     RVIHVGSFSK TLSAASRCGY IAARHEWIEA LTDLKLATSF GGGHLAMQLM HIALTDSGYR
     RHMQSVRSRL ADARRHTLRK LQALGITPWL QPEAGLFLWC QLPDGRDAAA LARQCLREGI
     VLAPGNAFSQ SQRAADYVRF NVSQCQDPRI WQVLARELR
//
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