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Database: UniProt
Entry: Q8G576_BIFLO
LinkDB: Q8G576_BIFLO
Original site: Q8G576_BIFLO 
ID   Q8G576_BIFLO            Unreviewed;       554 AA.
AC   Q8G576;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   SubName: Full=Probable multiple substrate aminotransferase (MsaT) containing domain of GntR family {ECO:0000313|EMBL:AAN24949.1};
GN   OrderedLocusNames=BL1144 {ECO:0000313|EMBL:AAN24949.1};
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24949.1, ECO:0000313|Proteomes:UP000000439};
RN   [1] {ECO:0000313|EMBL:AAN24949.1, ECO:0000313|Proteomes:UP000000439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN24949.1; -; Genomic_DNA.
DR   RefSeq; NP_696313.1; NC_004307.2.
DR   RefSeq; WP_007056415.1; NC_004307.2.
DR   AlphaFoldDB; Q8G576; -.
DR   STRING; 206672.BL1144; -.
DR   EnsemblBacteria; AAN24949; AAN24949; BL1144.
DR   KEGG; blo:BL1144; -.
DR   PATRIC; fig|206672.9.peg.854; -.
DR   HOGENOM; CLU_017584_0_0_11; -.
DR   OrthoDB; 199743at2; -.
DR   PhylomeDB; Q8G576; -.
DR   Proteomes; UP000000439; 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: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   Aminotransferase {ECO:0000313|EMBL:AAN24949.1};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000313|EMBL:AAN24949.1}.
FT   DOMAIN          11..79
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50949"
FT   REGION          101..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  61406 MW;  4B8AE6E7130FA1ED CRC64;
     MQLELNRRSK VPMYRQLAAE LREQIVSGAM AEGYRLPPER ELSSRLEVNR TTVLQAYQQL
     KDEGLIASKV GKGTFVLPAA SASRTSHTSN SDFGNAITRT TRSSAEMGTS QASSSGDVER
     ATSTDFLTTD QGSSSAAVHT IRESRSVQGP EPTVVRPPWS VLFSDYSNRF TYHDIASAER
     AQRGDTIIDF ATGSPNPADI PDDLLRKVSI EAFESREFDG QPESPIEGFE ELRALLAEHM
     RARGVQCGVR NVMVLSGSEQ GIDLIVRAFI NPGDCVLVEQ STFFPALQTF RSADARIIGV
     PVDEHGMRTD LLDGYCARFR PKLIYTVPTF QNPTGTTLSP ERRSELIDVA RRYQCLIVED
     DAYGDLWYGG ESSDAHRPIP LKGMENAGYV MYLSTFSKTV TSGLRTGWVV ADPHVINRLA
     ALRRMVDQHT STSSQRICLE LLKEGRIAEH LRGLIKAYRI RRDAAIAALE QYAPDEVYWT
     MPAGGYYIWV SLPDGVRSLD VLESCRSQGV TFMPGSVFDV DEMDDSHIRL NFVRPDAADI
     DTGIRIIGET IAQM
//
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