ID   K2CG81_9BACT            Unreviewed;       376 AA.
AC   K2CG81;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ACD_40C00213G0037 {ECO:0000313|EMBL:EKD80053.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD80053.1};
RN   [1] {ECO:0000313|EMBL:EKD80053.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD80053.1}.
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DR   EMBL; AMFJ01016759; EKD80053.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2CG81; -.
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        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         184
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   376 AA;  41952 MW;  15CA266C138BA3CE CRC64;
     MKTYSYGRQS INKKDVDAVV STLRSYFLTQ GPKVAEFEAK LCHVTGAKYA VAVSSGTAAL
     HLAVLALGIK RGDQGITTPM TFVASANCLR YVGADVQFAD INSSTGLIDP TEINKKITKK
     TKVLIPVHYA GQSCNMEAIA KIAKKHSLFV IEDAAHAIGS LYNGHPVGSC YYSDLTTFSF
     HPVKTITTGE GGAITTNNFA LYQQLLMFRT HGIIQKPEIA PWYYEMHGLG YNYRLPDILA
     SLGLSQLSKL QHFIARRSQI VKKYRQAFAG DSRFTVLQES SQSRSAFHLF PLLLNFDQLT
     KSKQQIFTDL LSHGLKLQVH YIPVHFHPYY RNLGFKPGDY PIAEAFYEQE ISLPLYPSLS
     DQDIKSIIKI IKEVVK
//