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Database: UniProt
Entry: N9JGZ8_ACIBA
LinkDB: N9JGZ8_ACIBA
Original site: N9JGZ8_ACIBA 
ID   N9JGZ8_ACIBA            Unreviewed;       472 AA.
AC   N9JGZ8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=HTH gntR-type domain-containing protein {ECO:0000259|PROSITE:PS50949};
GN   ORFNames=F913_02667 {ECO:0000313|EMBL:ENW70983.1};
OS   Acinetobacter baumannii NIPH 80.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=1217629 {ECO:0000313|EMBL:ENW70983.1, ECO:0000313|Proteomes:UP000013021};
RN   [1] {ECO:0000313|EMBL:ENW70983.1, ECO:0000313|Proteomes:UP000013021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIPH 80 {ECO:0000313|EMBL:ENW70983.1,
RC   ECO:0000313|Proteomes:UP000013021};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter baumannii NIPH 80.";
RL   Submitted (FEB-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ENW70983.1}.
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DR   EMBL; APRE01000050; ENW70983.1; -; Genomic_DNA.
DR   RefSeq; WP_002057751.1; NZ_KB849947.1.
DR   AlphaFoldDB; N9JGZ8; -.
DR   PATRIC; fig|1217629.3.peg.2590; -.
DR   HOGENOM; CLU_017584_0_0_6; -.
DR   Proteomes; UP000013021; Unassembled WGS sequence.
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; 3.90.1150.10; 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   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          1..69
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
SQ   SEQUENCE   472 AA;  54171 MW;  8617A4514D804913 CRC64;
     MYKSEQLAHS IRQLIESGNL NAHEKLPSLR DQVQRSGFSL MTVMNAYQEL ESQGLIYSKE
     KSGYFVAEQI ALKPLEQYSI VSLNSKIEIN SLVFKYLKSI QHESVVPFGS AFPDSQLLAA
     PKLIQIMGQL ARQRQSYDQT ASLPPGNLAL RKLIAQRYCM QGIQTDPDDI VITSGGLDAL
     NLSLQAVAKP GDYILLQQTV FYGAWQAAER LGLKVITIPE HPQHGFDLEA FEQVIHTYPI
     KVCWLMLNSH NPIGFTVSDE IKYKIAKLLH EHQIYLIEDD VYEELYYGGQ KPLSMKYFDQ
     QNLVLHCSSF SKTLGAGFRV GWVYAGKFSD HIQHLQLMST ISVNALIQNA LVEFLSHHHY
     EKHLRTLRLS LERYKKQFYH YLKQHLPATC EIYYYPSGYF LWVKLPHKLD SMQIYEELIQ
     QDIGVAPSPL FSVLPAQQHY LRINCSFEWN EKIQAALDQV IKTIQQRVEA SL
//
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