ID A0A160FK20_9BURK Unreviewed; 383 AA.
AC A0A160FK20;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:ANB72564.1};
GN ORFNames=AYM40_09440 {ECO:0000313|EMBL:ANB72564.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB72564.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB72564.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB72564.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP014578; ANB72564.1; -; Genomic_DNA.
DR RefSeq; WP_063495992.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FK20; -.
DR STRING; 1804984.AYM40_09440; -.
DR KEGG; buz:AYM40_09440; -.
DR Proteomes; UP000076852; Chromosome 1.
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; 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 Aminotransferase {ECO:0000313|EMBL:ANB72564.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Transferase {ECO:0000313|EMBL:ANB72564.1}.
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 187
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 383 AA; 41989 MW; BBEF89948DB6301F CRC64;
MSQSPVPFLP FVKPEIDEET IQGVVDVLRS GWITTGPQNQ KFEAALSEFC GGRPVRTFNS
GTATLEIGLR IAGVGEGDEV ITTPASWVAT SNVVYEVGAT PVFVDIDPVT RNIDLDLLEK
AITPRTKAII PVYLSGLPVD MDRLYDIARA HKLRVIEDAA QAFGSTWKGE RIGRLGDMVS
FSFHANKNLT SIEGGALVLN NEEEAILAQK YRLQGITRTG FDGMDCDVLG GKYNLTDVAA
RVGLGQLPHL ERFLAQRKKL VRAYFAGLEG GAALKLGIGL PLADFENSNW HMFQITLPLE
KLSIDRAGFM GLLKERGIGS GVHYPAIHLF SLYRARGFKE GMFPHAERFG ATTVTLPLFT
LMNEGDVERV CRAVNEICEQ YGK
//
