ID A0A0F0HRN0_9PSEU Unreviewed; 385 AA.
AC A0A0F0HRN0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Aminotransferase DegT {ECO:0008006|Google:ProtNLM};
GN ORFNames=UK12_11775 {ECO:0000313|EMBL:KJK58184.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK58184.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK58184.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK58184.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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|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:KJK58184.1}.
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DR EMBL; JYJF01000026; KJK58184.1; -; Genomic_DNA.
DR RefSeq; WP_045302655.1; NZ_JYJF01000026.1.
DR AlphaFoldDB; A0A0F0HRN0; -.
DR PATRIC; fig|1427391.3.peg.3425; -.
DR Proteomes; UP000033409; Unassembled WGS sequence.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000033409}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 385 AA; 40473 MW; 643619427E436F27 CRC64;
MSAVRTKNFP SWPQLGPQEV DAAAAVLLTN ELSQNSGRHV AEFEEAYAQW HSVPHAIAVN
NGTSAIHLAL AALGIGPGDE VLVPAYTFVG SASPLAYLGA TPVFVDIDPD TYCIDPADAE
AKLSERTRAV IAVHLNGYPA PVGQLAEMAR RHGIKLIEDT AQGHGAEIDG RRVGSVGDVG
CFSFWQDKTM TTGGEGGALL TADAELAASL RTLRDHGLVP AGPGLFHHAV VGYNYRLTSP
QAAVGLVQLG RLDDFVAARR RNGALLDEGL AQLPGLSLPK VVPGGVAAPW KYTLRLTTDP
SVLDVVTLVS ELQQAGIPAQ RRYPIPLTRQ PIFAGNPSNE TCPNSDLCAS TAFCLPVHPA
AEPEDIQDCI DALAKVLSDH GVSAA
//
