ID   TLL_AGGAC               Reviewed;         270 AA.
AC   O66256;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD(+));
DE            EC=1.1.1.339;
DE   AltName: Full=dTDP-6-deoxy-L-lyxo-4-hexulose reductase;
GN   Name=tll;
OS   Aggregatibacter actinomycetemcomitans (Actinobacillus
OS   actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=714;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33384 / DSM 8324 / CCUG 13227 / NCTC 9710 / Serotype c;
RX   PubMed=9805002; DOI=10.1016/s0167-4781(98)00174-2;
RA   Nakano Y., Yoshida Y., Yamashita Y., Koga T.;
RT   "A gene cluster for 6-deoxy-L-talan synthesis in Actinobacillus
RT   actinomycetemcomitans.";
RL   Biochim. Biophys. Acta 1442:409-414(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND GENE NAME.
RC   STRAIN=ATCC 33384 / DSM 8324 / CCUG 13227 / NCTC 9710 / Serotype c;
RX   PubMed=10702238; DOI=10.1074/jbc.275.10.6806;
RA   Nakano Y., Suzuki N., Yoshida Y., Nezu T., Yamashita Y., Koga T.;
RT   "Thymidine diphosphate-6-deoxy-L-lyxo-4-hexulose reductase synthesizing
RT   dTDP-6-deoxy-L-talose from Actinobacillus actinomycetemcomitans.";
RL   J. Biol. Chem. 275:6806-6812(2000).
CC   -!- FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to
CC       dTDP-6-deoxy-L-talose. {ECO:0000269|PubMed:10702238}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-6-deoxy-beta-L-talose + NAD(+) = dTDP-4-dehydro-beta-L-
CC         rhamnose + H(+) + NADH; Xref=Rhea:RHEA:34447, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62830,
CC         ChEBI:CHEBI:68576; EC=1.1.1.339;
CC         Evidence={ECO:0000269|PubMed:10702238};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000269|PubMed:10702238}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; AB010415; BAA28138.1; -; Genomic_DNA.
DR   PIR; T00109; T00109.
DR   RefSeq; WP_005574044.1; NZ_VSEW01000001.1.
DR   AlphaFoldDB; O66256; -.
DR   SMR; O66256; -.
DR   KEGG; ag:BAA28138; -.
DR   OMA; WIGKYVV; -.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Lipopolysaccharide biosynthesis; NAD; Oxidoreductase.
FT   CHAIN           1..270
FT                   /note="dTDP-6-deoxy-L-talose 4-dehydrogenase (NAD(+))"
FT                   /id="PRO_0000424092"
FT   ACT_SITE        135
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..76
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         87
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         139
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  30680 MW;  33376885638DFB0F CRC64;
     MNIIITGANG YIGRYVVKEL LNKGHKVIAI LFDGESPHSF LSGAELFYGD IFALSQEKKV
     DLVQNAECLL HLAWQAGFNH RDPSHLNNVM KHYQFLTSMA ELGIKNISVA GTMHEVGYFV
     GPIDANTPCN PRNPYGIAKN FLRQAMFDFA SVTPELNLRW LRFYYITGDD RFNNSIFTKI
     LKAEDEVQEY FPLNSGEMLY DFVDIKDLSL QIEERIISKE SGIFNCCSGK PKSLRTAVEE
     FIAEHNLKIK PKYNVFPARS YDSMAVWGAK