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Database: UniProt
Entry: A0A0G1WKI2_9BACT
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ID   A0A0G1WKI2_9BACT        Unreviewed;       371 AA.
AC   A0A0G1WKI2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 27.
DE   SubName: Full=Putative pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:KKW19333.1};
GN   ORFNames=UY63_C0016G0003 {ECO:0000313|EMBL:KKW19333.1};
OS   Parcubacteria group bacterium GW2011_GWA2_51_10.
OC   Bacteria.
OX   NCBI_TaxID=1618855 {ECO:0000313|EMBL:KKW19333.1, ECO:0000313|Proteomes:UP000034456};
RN   [1] {ECO:0000313|EMBL:KKW19333.1, ECO:0000313|Proteomes:UP000034456}
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:KKW19333.1}.
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DR   EMBL; LCQS01000016; KKW19333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WKI2; -.
DR   STRING; 1618855.UY63_C0016G0003; -.
DR   PATRIC; fig|1618855.3.peg.620; -.
DR   Proteomes; UP000034456; 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:SF39; BLR3650 PROTEIN; 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}.
FT   ACT_SITE        182
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         182
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   371 AA;  41737 MW;  BCD066B57982AB61 CRC64;
     MKKYSASRPY IGKKEERYVL EVLRSGVLSM GPFVERLEKK FAKKVGRRFA CAVSSGTAGL
     HLALLAAEIG KGDEVITSPF SFIASANAIL YVGGKPVFAD IDPKTYNIDP KELEKKITKR
     TKAILPVHIF GQPADMHAIM SIARKHKLVV IEDACEALLA AQNGKNAGTF GSAGVFAFYP
     NKQMTTGEGG MIVTNDKRLD SLYRSMRNQG RGEDRRWLDH SRLGYNYRMP ELSAAVGLAQ
     IEKLDFLIKK RRHVAMLYEK ALAPLARYLA LPKTAPRMTH TWFVYVVRLL DPRMRREKIM
     SELSKRGIET RPYLPSIHLF DVYRKLGHKE GELPVSEAVS ARTIALPFYS ELTKKDVGHI
     ARMLRAIITK K
//
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