SitesBLAST
Comparing H281DRAFT_02928 H281DRAFT_02928 uncharacterized oxidoreductase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
P30178 Hydroxycarboxylate dehydrogenase B; 2-oxoglutarate reductase; Hydroxyphenylpyruvate reductase; Phenylpyruvate reductase; EC 1.1.1.-; EC 1.1.1.237 from Escherichia coli (strain K12)
58% identity, 93% coverage: 13:354/367 of query aligns to 6:347/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
58% identity, 93% coverage: 13:354/367 of query aligns to 4:345/359 of 2g8yA
- active site: H46 (= H55)
- binding nicotinamide-adenine-dinucleotide: H43 (= H52), H46 (= H55), G120 (= G129), I122 (= I131), T160 (= T169), P162 (= P171), L176 (≠ V185), L177 (= L186), D178 (= D187), Y179 (≠ F188), A180 (= A189), H232 (= H241), Y235 (≠ F244), N268 (= N276), G311 (= G320), E314 (= E323)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
31% identity, 91% coverage: 26:358/367 of query aligns to 15:341/344 of 2x06A
- active site: H44 (= H55)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ H52), H44 (= H55), H116 (= H127), F117 (≠ I128), G118 (= G129), I119 (≠ R130), A120 (≠ I131), T156 (= T169), P158 (= P171), D173 (= D187), M174 (≠ F188), A175 (= A189), L301 (≠ Y317), I306 (≠ P322), E307 (= E323)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
36% identity, 88% coverage: 13:335/367 of query aligns to 2:319/340 of 1vbiA
- active site: H44 (= H55)
- binding nicotinamide-adenine-dinucleotide: H44 (= H55), H115 (= H127), G117 (= G129), A119 (≠ I131), T155 (= T169), P157 (= P171), A171 (≠ L186), D172 (= D187), L173 (≠ F188), A174 (= A189), F301 (≠ Y317), P303 (= P319), L306 (≠ P322), E307 (= E323)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
30% identity, 97% coverage: 1:355/367 of query aligns to 1:346/348 of 1v9nA
- active site: H55 (= H55)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: K4 (= K4), H55 (= H55), H127 (= H127), G129 (= G129), I130 (≠ R130), A131 (≠ I131), T167 (= T169), P169 (= P171), L183 (= L186), D184 (= D187), M185 (≠ F188), A186 (= A189), P191 (≠ A194), W308 (≠ Y317), H310 (≠ P319), G311 (= G320), K313 (≠ P322), G314 (≠ E323)
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
30% identity, 91% coverage: 11:345/367 of query aligns to 4:331/337 of 2cwfB
- active site: H48 (= H55)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H55), H120 (= H127), A122 (≠ G129), A123 (≠ R130), L124 (≠ I131), T160 (= T169), P162 (= P171), F177 (≠ L186), D178 (= D187), L179 (≠ F188), A180 (= A189), H230 (= H241), K231 (= K242), R303 (≠ Y317), G306 (= G320), R308 (≠ P322), R309 (≠ E323)
Q4U331 Delta(1)-pyrroline-2-carboxylate/Delta(1)-piperideine-2-carboxylate reductase; Pyr2C/Pip2C reductase; N-methyl-L-amino acid dehydrogenase; EC 1.5.1.21; EC 1.4.1.17 from Pseudomonas syringae pv. tomato (see paper)
30% identity, 92% coverage: 7:345/367 of query aligns to 6:337/343 of Q4U331
- HFAAL 126:130 (≠ HIGRI 127:131) binding in other chain
- DLA 184:186 (≠ DFA 187:189) binding in other chain
- HK 236:237 (= HK 241:242) binding
- 309:315 (vs. 317:323, 29% identical) binding in other chain
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
30% identity, 91% coverage: 11:345/367 of query aligns to 1:328/332 of 2cwhA
- active site: H45 (= H55)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H55), A119 (≠ G129), A120 (≠ R130), L121 (≠ I131), H148 (≠ F160), T157 (= T169), P159 (= P171), F174 (≠ L186), D175 (= D187), L176 (≠ F188), A177 (= A189), H227 (= H241), K228 (= K242), R300 (≠ Y317), G303 (= G320), R305 (≠ P322), R306 (≠ E323)
- binding pyrrole-2-carboxylate: H45 (= H55), R49 (≠ M59), M142 (≠ A152), T157 (= T169), H183 (≠ Y195), G184 (= G196)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
28% identity, 92% coverage: 13:350/367 of query aligns to 2:336/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ M59), H116 (= H127), S140 (≠ G153), D141 (= D154)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ H52), H44 (= H55), H116 (= H127), G118 (= G129), I120 (= I131), S140 (≠ G153), F147 (= F160), T156 (= T169), P158 (= P171), F173 (≠ L186), D174 (= D187), M175 (≠ F188), A176 (= A189), P223 (≠ H241), K224 (= K242), Y303 (= Y317), G306 (= G320), D308 (≠ P322), Q309 (≠ E323)
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
28% identity, 92% coverage: 13:350/367 of query aligns to 2:336/349 of P77555
- S43 (= S54) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H55) mutation to A: 16-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.
- R48 (≠ M59) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y63) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H127) mutation to A: Loss of dehydrogenase activity.
- S140 (≠ G153) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (= D154) mutation to A: 5-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.; mutation to E: 14-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.; mutation to N: 6-fold decrease of the affinity for (S)-ureidoglycolate, but same affinity for NAD compared to the wild-type. Strong decrease of the catalytic efficiency.
- M251 (≠ H264) mutation to A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- R259 (≠ N272) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
31% identity, 89% coverage: 17:341/367 of query aligns to 7:331/350 of 1z2iA
- active site: H45 (= H55)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ H52), H45 (= H55), H117 (= H127), F118 (≠ I128), G119 (= G129), P120 (≠ R130), A121 (≠ I131), T157 (= T169), P159 (= P171), D175 (= D187), M176 (≠ F188), A177 (= A189), P182 (≠ A194), F227 (= F244), K228 (vs. gap), M307 (≠ Y317), R312 (≠ P322), E313 (= E323)
1s20G A novel NAD binding protein revealed by the crystal structure of e. Coli 2,3-diketogulonate reductase (yiak) northeast structural genomics consortium target er82 (see paper)
26% identity, 91% coverage: 13:345/367 of query aligns to 2:329/335 of 1s20G
- active site: H44 (= H55)
- binding nicotinamide-adenine-dinucleotide: H44 (= H55), H116 (= H127), W147 (≠ F160), T156 (= T169), P158 (= P171), D172 (= D187), M173 (≠ F188), S174 (≠ A189), W224 (≠ H241), K225 (= K242), R301 (≠ Y317), G304 (= G320), E306 (≠ P322)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
26% identity, 91% coverage: 11:345/367 of query aligns to 2:348/361 of 3i0pA
- active site: H46 (= H55)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ H52), H46 (= H55), H119 (= H127), I122 (≠ R130), A123 (≠ I131), T159 (= T169), P161 (= P171), F176 (≠ L186), D177 (= D187), G178 (≠ F188), A179 (= A189), P184 (≠ A194), R187 (≠ K197), Y320 (= Y317), A322 (≠ P319), G323 (= G320), K325 (≠ P322), E326 (= E323)
Query Sequence
>H281DRAFT_02928 H281DRAFT_02928 uncharacterized oxidoreductase
MTDKELAGSTTPRIAADQLHAFVRAIWEQAGSAPREAELVADHLVAANLTGHDSHGVGMI
PRYVASLADGQLQLNLHADVVKDAGAVLTVEGRKGFGQVVAFEAMEEGIARAQRIGICAV
GLRDAHHIGRIGHWAEQCARAGLVSFHFVNVAGDPLVAPFGGADRRIGTNPFCAAYPRPG
KPPLVLDFATSTVAYGKTRVAYNQGKQVPPGALIDHEGVPTADPKVMHEEPFGSLTPFGG
HKGFGLAAMCEIFSGALAGGFTTHADTLGTTNAIINCMLSVIIDPAAFDAPDAQAEADAF
IAWVKASPLAAGVDHIYEPGEPERVTRAEREAQGIPVDAATWTQICTAALAVGMHADEVA
RWSAMLK
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory