ID   A0A0F2N7H4_9FIRM        Unreviewed;       380 AA.
AC   A0A0F2N7H4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KJR96196.1};
GN   ORFNames=VR68_14735 {ECO:0000313|EMBL:KJR96196.1};
OS   Peptococcaceae bacterium BRH_c4a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJR96196.1, ECO:0000313|Proteomes:UP000033439};
RN   [1] {ECO:0000313|EMBL:KJR96196.1, ECO:0000313|Proteomes:UP000033439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c4a {ECO:0000313|EMBL:KJR96196.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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:KJR96196.1}.
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DR   EMBL; LADN01000089; KJR96196.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2N7H4; -.
DR   STRING; 1629716.VR68_14735; -.
DR   PATRIC; fig|1629716.3.peg.2365; -.
DR   Proteomes; UP000033439; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR020026; PseC.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03588; PseC; 1.
DR   PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KJR96196.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KJR96196.1}.
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   380 AA;  42727 MW;  576DB73EB9BD8BCA CRC64;
     MEFLPYGKQY LDEDDIQAVV EVLRSDRLTT GPKVEEFERS LARRSGTGYA VAFNSGTAAL
     HAAYFAAGVG PGDEVITSPV TFAATANAAL FLGARPVFAD IRRDTANIDP AELERHITPR
     TKVLAPVDFA GHPADLNIIM DIAGKYGLVV VEDAAHALGA AYCGRPVGSL AHLTIFSFHP
     VKHITTGEGG AVVTDNKDYY EKMLAFRSHG IVRETKKLSR WHGPWYHEMH YLGYNYRLTD
     IQCALGVSQL KKLDQFLEKR QALVDYYNRQ LSGLKMIVLP VTLADCSPAW HLYVIRLKGH
     RPHRRELYEE LHRAGIGVQV HYLPVYWHPY YQKLGYPEGL CPIAEDYYQR ALSLPLFPAM
     SEDIARRIVL ELTQILDKNF
//