ID A0A0G1W2U0_9BACT Unreviewed; 380 AA.
AC A0A0G1W2U0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=UDP-4-keto-6-deoxy-N-acetylglucosamine 4-aminotransferase {ECO:0000313|EMBL:KKW13043.1};
GN ORFNames=UY52_C0050G0006 {ECO:0000313|EMBL:KKW13043.1};
OS Parcubacteria group bacterium GW2011_GWC2_49_9.
OC Bacteria.
OX NCBI_TaxID=1618934 {ECO:0000313|EMBL:KKW13043.1, ECO:0000313|Proteomes:UP000034059};
RN [1] {ECO:0000313|EMBL:KKW13043.1, ECO:0000313|Proteomes:UP000034059}
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:KKW13043.1}.
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DR EMBL; LCQH01000050; KKW13043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1W2U0; -.
DR PATRIC; fig|1618934.3.peg.1356; -.
DR Proteomes; UP000034059; 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; 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 Aminotransferase {ECO:0000313|EMBL:KKW13043.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:KKW13043.1}.
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 180
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 380 AA; 42019 MW; F0F5B9F7E885E094 CRC64;
MIPYSTQDIN EADIKAVGRA LRSGWLTQGP AIGRFEKALA KKVGARFAVA FNSGTAALHA
AYFAAGVRKG DEVIVPSLTF AATANAALYL GAKPVFADSD MQTGNINIAD ARKKITKKTK
AIVPVDYGGR PADLREFRAL AKKHKLVFIE DAAQALGATY RGKPVGTHAD MTMFSFHPVK
SITTGEGGVI VTNNKKFDTA LRLFRSHGIS KDTNTFARKG HGAWYQEMQE LGFNYRMPEM
SAALGESQLK RLGFFITKRR VAAKRYRRLL AKVPNLILPP AERAHEKSAW HLYPVRLAPQ
VAHKRDEVFA TMRKAGIGVQ VHYVPVHLHL FYEKLGYKKG LCPNTEAFVA SEISIPLFPN
ITQKQQKFIA DTLKRILAQI
//
