ID A0A0G1KVP2_9BACT Unreviewed; 398 AA.
AC A0A0G1KVP2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KKT60402.1};
GN ORFNames=UW53_C0001G0052 {ECO:0000313|EMBL:KKT60402.1};
OS Candidatus Giovannonibacteria bacterium GW2011_GWA1_44_25.
OC Bacteria; Candidatus Giovannonibacteria.
OX NCBI_TaxID=1618645 {ECO:0000313|EMBL:KKT60402.1, ECO:0000313|Proteomes:UP000034087};
RN [1] {ECO:0000313|EMBL:KKT60402.1, ECO:0000313|Proteomes:UP000034087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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:KKT60402.1}.
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DR EMBL; LCIR01000001; KKT60402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KVP2; -.
DR PATRIC; fig|1618645.3.peg.53; -.
DR Proteomes; UP000034087; 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:KKT60402.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KKT60402.1}.
FT ACT_SITE 208
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 398 AA; 44716 MW; 690765FC07482169 CRC64;
MASNTTAFGL VIYIQMAKKK IKINLAKPWF DRREPEAAYR VVKSGYLISG PLVEKFEREF
AKKIGVKYAI AVNSGSSALL VVQQALGIGR GDEVIVPNMT FISTASSSLY LGARPVFADI
EMKTYGIDPE AIVKRIANLP ASRRKKLKAI IPVHYAGQSC DLDPILKIAR KHKLFVVEDA
AEAHLAEYNG RKVGGIGDIG IFSFTPSKPM TTGEGGMITT NNAELAKKCK LIRNFYDINK
FQWHEFGFHF RMPETMGAIG LVQLAKLERA VAMRMSIAHR YTKELNKLGC IVTPYERTRK
DINFQLYTIM LIPGALSIDR DKFIDELGLR GVQARLYYPC LHKQNVFKGM GRYNDNEFPN
SIAFEKNALS LPIYPGLKNK EVNYVISSIQ EIVKKYKT
//
