TLD_AGGAC
ID TLD_AGGAC Reviewed; 294 AA.
AC Q9JRN7; D4EEL4;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=GDP-6-deoxy-D-talose 4-dehydrogenase;
DE EC=1.1.1.135;
DE AltName: Full=GDP-4-keto-6-deoxy-D-mannose reductase;
GN Name=tld;
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=SUNYaB 75 / Serotype a;
RX PubMed=11118626; DOI=10.1016/s0167-4781(00)00229-3;
RA Suzuki N., Nakano Y., Yoshida Y., Nakao H., Yamashita Y., Koga T.;
RT "Genetic analysis of the gene cluster for the synthesis of serotype a-
RT specific polysaccharide antigen in Aactinobacillus actinomycetemcomitans.";
RL Biochim. Biophys. Acta 1517:135-138(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=SUNYaB 75 / Serotype a;
RX PubMed=12444986; DOI=10.1046/j.1432-1033.2002.03331.x;
RA Suzuki N., Nakano Y., Yoshida Y., Nezu T., Terada Y., Yamashita Y.,
RA Koga T.;
RT "Guanosine diphosphate-4-keto-6-deoxy-d-mannose reductase in the pathway
RT for the synthesis of GDP-6-deoxy-d-talose in Actinobacillus
RT actinomycetemcomitans.";
RL Eur. J. Biochem. 269:5963-5971(2002).
CC -!- FUNCTION: Catalyzes the conversion of GDP-4-dehydro-6-deoxy-D-mannose
CC to GDP-6-deoxy-D-talose. {ECO:0000269|PubMed:12444986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-6-deoxy-alpha-D-talose + NAD(+) = GDP-4-dehydro-alpha-D-
CC rhamnose + H(+) + NADH; Xref=Rhea:RHEA:10728, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57638, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:57964; EC=1.1.1.135;
CC Evidence={ECO:0000269|PubMed:12444986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-6-deoxy-alpha-D-talose + NADP(+) = GDP-4-dehydro-alpha-D-
CC rhamnose + H(+) + NADPH; Xref=Rhea:RHEA:10724, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57638, ChEBI:CHEBI:57783, ChEBI:CHEBI:57964,
CC ChEBI:CHEBI:58349; EC=1.1.1.135;
CC Evidence={ECO:0000269|PubMed:12444986};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC biosynthesis. {ECO:0000269|PubMed:12444986}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AB046360; BAB03206.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9JRN7; -.
DR SMR; Q9JRN7; -.
DR STRING; 714.ACT75_06325; -.
DR eggNOG; COG0451; Bacteria.
DR BioCyc; MetaCyc:MON-13570; -.
DR UniPathway; UPA00281; -.
DR GO; GO:0047916; F:GDP-6-deoxy-D-talose 4-dehydrogenase activity; IEA:UniProtKB-EC.
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..294
FT /note="GDP-6-deoxy-D-talose 4-dehydrogenase"
FT /id="PRO_0000424094"
FT ACT_SITE 128
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 38..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 60..64
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 33342 MW; ABC3F7E2C8C0DE84 CRC64;
MKILVTGGSG FIGKNLIYLL REKREFEVFG ATVEETMDLT NPCSVQSVLE KTKPDFIVHL
AALTFVPNNN PITFYLVNTI GTENLLRSIV DLNVAKLGVL CFSTAGIYGI QETKLLSESL
TPKPVNHYSM SKHCMEHIVN KYRCFRGITV VRPFNVLGLG QNINFLVPKM VSAFVKKDKT
IELGNLDSVR DFISVNDCCD IIYRLISKLI ENETINICTG IGYSVYQIFQ LLCEISMHQM
EIKQNELFVR HDDIPQMIGD PSKLLNVLGN DYRFTSVRAI LEEMYKNRLL ELSI
