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Database: UniProt
Entry: H6MYR7_GORPV
LinkDB: H6MYR7_GORPV
Original site: H6MYR7_GORPV 
ID   H6MYR7_GORPV            Unreviewed;       460 AA.
AC   H6MYR7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Putative transcriptional regulator, GntR family with aminotransferase domain {ECO:0000313|EMBL:AFA71945.1};
GN   OrderedLocusNames=GPOL_c08800 {ECO:0000313|EMBL:AFA71945.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA71945.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA71945.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA71945.1; -; Genomic_DNA.
DR   RefSeq; WP_014358885.1; NC_016906.1.
DR   AlphaFoldDB; H6MYR7; -.
DR   STRING; 1112204.GPOL_c08800; -.
DR   KEGG; gpo:GPOL_c08800; -.
DR   eggNOG; COG1167; Bacteria.
DR   HOGENOM; CLU_017584_2_0_11; -.
DR   Proteomes; UP000009154; 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; 3.40.640.10; 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   Aminotransferase {ECO:0000313|EMBL:AFA71945.1};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:AFA71945.1}.
FT   DOMAIN          19..87
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
SQ   SEQUENCE   460 AA;  48887 MW;  A6CA4E032AE07614 CRC64;
     MTVHDPATEV TPQRIVIDDP TPAGIAGAIG RMIRNGELVP GDRLPTVRDL SAQLGVSPAT
     VSYGWKALSR SGLVVSRGRS GTFVADGAVS PEVPRVSRTA TMARTHGSIG LDLSKGSPDP
     ELLPELKAAL SNVAERAATT SYHDHPVVPE LGDLLRTRWP SKAQALTVVD GALDAVTRSL
     QAVTRFGDRV IVEDPTFPQF LDLLDTLGLQ HIPVPVDRHG PDPDAFARAM AQAPTVALLQ
     PRAHNPTGVS MTAARARDLA RAVRGTRCVV IEDDHSGAAV AAPDISLGRW LPDQVVHVRS
     FSKSHGPDLR IAAMTGPREV IDRVTATRML GPGWTPRLLQ RVLYELLTDE ASVAAVDNAR
     AAYRSRRAAL VEALADKGID VGGTDGLNVW VPVADERNAL IHLAANGIQV APGDPFIVEP
     QRGGDHVRVT IATLRDDVER VAATLAAAAS GNQADFYPLR
//
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