ID   FDTB_ANETH              Reviewed;         363 AA.
AC   Q6T1W6;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase;
DE            EC=2.6.1.90;
DE   AltName: Full=dTDP-6-deoxy-D-xylo-hex-3-ulose aminase;
GN   Name=fdtB;
OS   Aneurinibacillus thermoaerophilus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=143495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   COFACTOR.
RC   STRAIN=L420-91T;
RX   PubMed=12740380; DOI=10.1074/jbc.m300858200;
RA   Pfoestl A., Hofinger A., Kosma P., Messner P.;
RT   "Biosynthesis of dTDP-3-acetamido-3,6-dideoxy-alpha-D-galactose in
RT   Aneurinibacillus thermoaerophilus L420-91T.";
RL   J. Biol. Chem. 278:26410-26417(2003).
CC   -!- FUNCTION: Specifically aminates dTDP-6-deoxy-D-xylohex-3-ulose to form
CC       dTDP-D-Fucp3N in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-
CC       alpha-D-galactose, a glycan chain of the S-layer.
CC       {ECO:0000269|PubMed:12740380}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + dTDP-3-amino-3,6-dideoxy-alpha-D-
CC         galactopyranose = dTDP-3-dehydro-6-deoxy-alpha-D-galactose + L-
CC         glutamate; Xref=Rhea:RHEA:31619, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:63303, ChEBI:CHEBI:63305; EC=2.6.1.90;
CC         Evidence={ECO:0000269|PubMed:12740380};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:12740380};
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}.
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DR   EMBL; AY442352; AAS55722.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6T1W6; -.
DR   SMR; Q6T1W6; -.
DR   KEGG; ag:AAS55722; -.
DR   BioCyc; MetaCyc:MON-17005; -.
DR   BRENDA; 2.6.1.90; 344.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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; PTHR30244; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           1..363
FT                   /note="dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose
FT                   transaminase"
FT                   /id="PRO_0000421824"
FT   MOD_RES         185
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  41040 MW;  32FC3829EC02D6E0 CRC64;
     MIPFLDLRQI NMRYQKEIQQ AMNRVLESGW YILGGEVDDF ERKFASYCGA KYCIGVANGL
     DALTLIIRAY DIGLGDEVIV PSNTYIASIL AISANGATPV LVEPDINTYN IDPLKIEEKI
     TSRTKAIMVV HLYGQSCDME SINLIAKKYN LKVIEDCAQA HGAIYNGKRV GSLGDAAGFS
     FYPGKNLGAL GDGGAITTND AELAERLNVL RNYGSHKKYE NLFKGVNSRL DELQAAILSI
     KLSYLDDDNQ RRREIAAYYL EHIKNPFIHL PTVTDDKAHV WHLFVVRVKE REAFQYYLAE
     QNIQTLIHYP IPPHKQKAYS EWQQESFPIS EQIHSEVVSL PISPVMSREE VERVVEAVNR
     YGY