ID A0A0S8L3I6_9PROT Unreviewed; 374 AA.
AC A0A0S8L3I6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KPL28706.1};
GN ORFNames=AMJ72_01905 {ECO:0000313|EMBL:KPL28706.1};
OS Acidithiobacillales bacterium SM1_46.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL28706.1, ECO:0000313|Proteomes:UP000052054};
RN [1] {ECO:0000313|EMBL:KPL28706.1, ECO:0000313|Proteomes:UP000052054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL28706.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL28706.1}.
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DR EMBL; LJVB01000009; KPL28706.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8L3I6; -.
DR PATRIC; fig|1703384.3.peg.2567; -.
DR Proteomes; UP000052054; 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; 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:KPL28706.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KPL28706.1}.
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 183
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 374 AA; 40010 MW; 8B397643C657D611 CRC64;
MSMLPFTRPT LGEEELQSVR EVLESGWITT GPKAKALEEA IAAYVGGGVQ ARVFNSATSA
LEACLFAAGV GPGDEVIVPA MSFVATANVV VRVGARPVFV DVDLNSRNIR ADRVGKAINS
RTRAIMPVHF AGLAADLDPL YALAGQHGLL VIEDAAQAIG TEHAGHKVGA NGNPVCFSFH
PNKNMTTIEG GAVTATDPAF LQRLERIRFH GIERDADGNM DVKAWGGKMN LPDVNSAIGL
IQLSKLDGFN ARRRELASRY LQRLANVPHL VLPADGPGHS WHMFCVCVDL NATGLTRPQI
QARLEKQGVG TGTHYPAMTL FSLYRDLGNA PGDFPVAERI GRETLTLPLF PTMTEADVDH
VCDALQQSIS SEAA
//
