ID A0A0G1VPE0_9BACT Unreviewed; 378 AA.
AC A0A0G1VPE0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UY39_C0001G0015 {ECO:0000313|EMBL:KKW08135.1};
OS Candidatus Kaiserbacteria bacterium GW2011_GWC2_49_12.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1618675 {ECO:0000313|EMBL:KKW08135.1, ECO:0000313|Proteomes:UP000034589};
RN [1] {ECO:0000313|EMBL:KKW08135.1, ECO:0000313|Proteomes:UP000034589}
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:KKW08135.1}.
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DR EMBL; LCPV01000001; KKW08135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VPE0; -.
DR PATRIC; fig|1618675.3.peg.15; -.
DR Proteomes; UP000034589; 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; IPR020026; PseC.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR03588; PseC; 1.
DR PANTHER; PTHR30244:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 378 AA; 42117 MW; FBB41F0F79167AC6 CRC64;
MKLPYSRQTI YEDDIRAVSK VLRSPFLTQG PEVGKFESSL SRYSGARYCV AFSSGTAALH
AAYFAAGIGH GDEVVMPALT FAATANAALY LGAKPVFADI HSDTGNINVK DAERKLTKRT
KAIIAVDYAG LPAELGSVRR LAKKHKLVFI EDAAQGLGAS YKGKKLGTFA DMTMFSFHPV
KSITTGEGGA ILTDDRSYYE KLQMFRTHGL TRDPKKLKNK THASWHQEMQ ILGYNYRLTD
IQAALGTSQM KKLDRFIKTR RIAAKRYVEL LADVPGITLP SRAGLENSAH HLFVIRVDKR
IRDRVFEALR ASGIGVQVHY LPVYLHPYYR SLGYRKGLCP SAETYAAQAI SIPLYPTLAR
RDQEYVVKKI REIIGKNH
//
