ID A0A1Y5TD15_9RHOB Unreviewed; 381 AA.
AC A0A1Y5TD15;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=UDP-4-amino-4, 6-dideoxy-N-acetyl-beta-L-altrosamine transaminase {ECO:0000313|EMBL:SLN57669.1};
DE EC=2.6.1.92 {ECO:0000313|EMBL:SLN57669.1};
GN Name=pseC {ECO:0000313|EMBL:SLN57669.1};
GN ORFNames=PSA7680_03027 {ECO:0000313|EMBL:SLN57669.1};
OS Pseudoruegeria aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN57669.1, ECO:0000313|Proteomes:UP000193409};
RN [1] {ECO:0000313|EMBL:SLN57669.1, ECO:0000313|Proteomes:UP000193409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN57669.1,
RC ECO:0000313|Proteomes:UP000193409};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; FWFQ01000025; SLN57669.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5TD15; -.
DR OrthoDB; 9768668at2; -.
DR Proteomes; UP000193409; 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:SLN57669.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000193409};
KW Transferase {ECO:0000313|EMBL:SLN57669.1}.
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 188
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 381 AA; 40998 MW; 262CA7A800A1AE3F CRC64;
MIPYGRQDIR QEDIDAVVDV LKSDFLTQGP QVPAFEQAVA KAAGARHAVA VNSATSALHI
ACLALGLGPG DLLWTSPITF VASANVGRLC GADVDFVDVD PDTANMCPQA LAEKLAAAKA
AGRLPKVLIP VHMCGQSCDM AAIGALARDY GVKIVEDASH AIGGSFEGKP VGDCRHSDIT
VFSFHPVKIV TTAEGGVATT QDADLARRME LFRSHGVTRD PALMEGESEG GWYYQQVELG
LNYRMTELQA ALGVTQMTRL AEYVDRRNAL AERYDAALGN LPLKRPGRLA QARSSFHLYV
IRVEAARRRA VFDALRAEGI GVNVHYIPVH TQPYYRRLGF APGQFPQAEG YYAQAISIPL
YHGLTEAAQD QVVAAVEKAL A
//
