ID C6DA18_PECCP Unreviewed; 483 AA.
AC C6DA18;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Transcriptional regulator, GntR family with aminotransferase domain {ECO:0000313|EMBL:ACT13774.1};
GN OrderedLocusNames=PC1_2744 {ECO:0000313|EMBL:ACT13774.1};
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13774.1, ECO:0000313|Proteomes:UP000002736};
RN [1] {ECO:0000313|EMBL:ACT13774.1, ECO:0000313|Proteomes:UP000002736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1 {ECO:0000313|EMBL:ACT13774.1,
RC ECO:0000313|Proteomes:UP000002736};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) 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; CP001657; ACT13774.1; -; Genomic_DNA.
DR RefSeq; WP_015840941.1; NC_012917.1.
DR AlphaFoldDB; C6DA18; -.
DR STRING; 561230.PC1_2744; -.
DR KEGG; pct:PC1_2744; -.
DR eggNOG; COG1167; Bacteria.
DR HOGENOM; CLU_017584_0_0_6; -.
DR OrthoDB; 9804020at2; -.
DR Proteomes; UP000002736; 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; PTHR42790; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42790:SF9; GNTR FAMILY REGULATORY PROTEIN-RELATED; 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:ACT13774.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:ACT13774.1}.
FT DOMAIN 1..69
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 483 AA; 53612 MW; 3650E270BD5C1D75 CRC64;
MAKFEQLAHQ IREQLQEGIW QPGDKLPSLR EKSLHSGMSL MTVLHAYQLL ESQGLIVSRP
QSGYYAAPQL SALPADSLHS PVGQERVQLT EDVDVNAFIF DVLQASKDPA VMPFGSAFPD
PQLFPQRQLT RSLASVARHM QPQSALDNLP PGNESLRKNI AQRYALQGIA VSPDEIVITA
GAMESLNLSL QVLTEPGDYV VIESPAFYGA LQAIERLKLK AIAIATDPQQ GIDLDALQQA
LNDYPIKACW LMTNFHNPLG CTLSWEKKQQ LVAMLEKHGV GLVEDDVYSE LYAGLQRPLP
AKALDKKGTI LHCSSFSKNL VAGFRVGWVA AGRYAGSIQR LQLMSTLSTS APMQLAIADY
LATSSYDSHL RRLRRALEQR KHAALQSLRR HLPGDVRINH SQGGYFLWLE LPEGISSTEL
YRRALARGVS IAPGKMFTTG DKYDRYFRFN ASYAWDDRCE QSVIVLAALI RTQIGERPPR
SPL
//
