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The gene TM0487 from Thermotoga maritima encodes the NP_228297 protein of unknown function from the DUF59 group PF01883. SCOP classifies 1uwd inthe alpha+beta class, Fe-S cluster superfamily, PaaD-like family. 1uwd DALI top hits are with the uncharacterized proteins 3lno (Z=13), TTHB138 3cq2 (Z=12), and the dTDP-4-keto-L-rhamnose reductase-related protein 2cu6 (Z=11). Based on structural similarity with nitrogen fixation proteins (NifU, PDB id: 1XHJ, HHPred, P-value 1.6E-07, probability 96.4%, 21% identities; Z=3) and sequence homology with the same (HHPred P-value 9.6E-05 with PF0116 over 71 residues), we propose an involvement of this family in Fe-S cluster biosynthesis. This hypothesis finds further support in an analysis of the genome context of TM0487, where with a probability of 0.87, an association is found with the NifU-like protein, HemK [TM0488].
The BLAST alignment indicates 53% sequence identity to a putative dTDP-4-keto-l-rhamnose reductase RELATED protein EC:1.1.1.133 from Pyrococcus abyssi GE5 COG1091. The structure comparison of 1uwd with the structurally similar proteins from Thermus thermophilus HB8, 2CU6 3CQ1 (Z=11), also suggests that 1uwd is most probably a dTDP-4-keto-l-rhamnose reductase-RELATED protein. The enzyme (2GGS) catalyzes the following reaction: dTDP-6-deoxy-L-mannose + NADP(+) <=> dTDP-4-dehydro-6-deoxy-L-mannose + NADPH. The enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.
Annotation of "putative dTDP-4-keto-l-rhamnose reductase" does not match TM0487 either in terms of structure (rmsd 4.5 Å over 56 residues between TM0487 and PDB id: 2GGS) or sequence homology. The folds of the two proteins are different, alpha-lytic protease prodomain like (Fe-S cluster assembly domain like superfamily) for TM0487 and NAD(P)-binding Rossmann fold-like for 2GGS and there's no indication of dTDP binding in TM0487 (the NDP observed in 2GGS clashes sterically with TM0487 loops).
No references found.