ID A0A0G0JHR6_9BACT Unreviewed; 434 AA.
AC A0A0G0JHR6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:KKQ67218.1};
GN ORFNames=US86_C0001G0145 {ECO:0000313|EMBL:KKQ67218.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWA2_38_24.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618422 {ECO:0000313|EMBL:KKQ67218.1, ECO:0000313|Proteomes:UP000034235};
RN [1] {ECO:0000313|EMBL:KKQ67218.1, ECO:0000313|Proteomes:UP000034235}
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KKQ67218.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LBUP01000001; KKQ67218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JHR6; -.
DR PATRIC; fig|1618422.5.peg.148; -.
DR Proteomes; UP000034235; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KKQ67218.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KKQ67218.1}.
SQ SEQUENCE 434 AA; 47986 MW; 5F3470B1F25ED80A CRC64;
MTKSQELWKK AKKIIPGGSQ LLSKRSEMFL PDNWPSYFQS AKGVTLTDLD GRTFIDMAYM
GVGPCVLGYA DEDVNLVVKK AIDSGISATL NCPEEVELAE LLLQLHPWAQ MVRYARSGGE
AAAIAVRIAR AHTKKDKVAF CGYHGWHDWY LSSNLADDSN LDGHLIPGLN PLGVPRGLIG
TSLPFEYNKI EQLEEIVKVH DIGTIIMEPI RHQEPKNNFL EKVREIATAK GVVLIYDEIS
SGFRSTVGGV HLEFGVTPDI VVFAKAISNG FPMAAIVGKG EVMDAAQESF ISSTNWTDRI
GPVAAIATIK KMQKENVPAH LKRIGCLIGR GWESLGKKHN LDITVTGPDP LITFSLNYEK
SLELKTLFTQ EMLKRGYLAT LTVYVSFSHT EDTVDKYLQS VDEVFALLKK AIDDDNIDDL
LEGPVAHKGF RRLT
//
