ID A0A0F2PNU9_9FIRM Unreviewed; 398 AA.
AC A0A0F2PNU9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KJS15923.1};
GN ORFNames=VR69_11745 {ECO:0000313|EMBL:KJS15923.1};
OS Peptococcaceae bacterium BRH_c4b.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629717 {ECO:0000313|EMBL:KJS15923.1, ECO:0000313|Proteomes:UP000033446};
RN [1] {ECO:0000313|EMBL:KJS15923.1, ECO:0000313|Proteomes:UP000033446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c4b {ECO:0000313|EMBL:KJS15923.1};
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, 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:KJS15923.1}.
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DR EMBL; LADO01000045; KJS15923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PNU9; -.
DR STRING; 1629717.VR69_11745; -.
DR PATRIC; fig|1629717.3.peg.3083; -.
DR Proteomes; UP000033446; 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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:KJS15923.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:KJS15923.1}.
FT ACT_SITE 225
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 225
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 398 AA; 44436 MW; 9C4AFCF34DE55ED7 CRC64;
MSRSFKDEKN IIYSIINAIE SVVSHREEFV PLHEPCFSGN EWAYVKDCLD TGWVSSVGSY
VDRFELMLAD FIGVKYAVAV VNGTAALHIC LKLVGVAPGD EVLIPALTFV ATANAVTYCN
AIPHFVDSEE RTLGIDPYKL RDYLYDIAII RTDDCINKIT GRRIKAVVPM HTFGHPVDMD
PLLDVCSEFK LELVEDAAES LGSYYKGKHT GNFGKVSALS FNGNKIITTG GGGAILSNNK
ELAKLAKHIT TTAKLPHRWL FYHDMVGYNY RMPNLNAALG CAQMENLNDF IYMKRCLAQN
YKAAFSSINE VHFFTENNFS KSNYWLNALI IKRNSICKKE EILEALNDVG IMTRPAWMLL
SELPIYGQCP KMDLSVAKNL QSFLINIPSS SKLGVKRG
//
