SitesBLAST
Comparing H281DRAFT_05436 FitnessBrowser__Burk376:H281DRAFT_05436 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)
1vbiA Crystal structure of type 2 malate/lactate dehydrogenase from thermus thermophilus hb8
30% identity, 98% coverage: 2:323/330 of query aligns to 22:339/340 of 1vbiA
- active site: H44 (= H24)
- binding nicotinamide-adenine-dinucleotide: H44 (= H24), H115 (= H96), G117 (≠ A98), A119 (≠ L100), T155 (≠ P138), P157 (= P140), A171 (≠ I154), D172 (= D155), L173 (≠ I156), A174 (≠ S157), F301 (≠ R285), P303 (= P287), L306 (≠ R290), E307 (≠ G291)
2x06A Sulfolactate dehydrogenase from methanocaldococcus jannaschii (see paper)
28% identity, 95% coverage: 2:316/330 of query aligns to 24:332/344 of 2x06A
- active site: H44 (= H24)
- binding nicotinamide-adenine-dinucleotide: F41 (≠ H21), H44 (= H24), H116 (= H96), F117 (≠ I97), G118 (≠ A98), I119 (≠ C99), A120 (≠ L100), T156 (≠ P138), P158 (= P140), D173 (= D155), M174 (≠ I156), A175 (≠ S157), L301 (≠ R285), I306 (≠ R290), E307 (≠ G291)
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)
26% identity, 98% coverage: 2:323/330 of query aligns to 26:348/361 of P30178
2g8yA The structure of a putative malate/lactate dehydrogenase from e. Coli.
26% identity, 98% coverage: 2:323/330 of query aligns to 24:346/359 of 2g8yA
- active site: H46 (= H24)
- binding nicotinamide-adenine-dinucleotide: H43 (= H21), H46 (= H24), G120 (≠ A98), I122 (≠ L100), T160 (≠ P138), P162 (= P140), L176 (= L153), L177 (≠ I154), D178 (= D155), Y179 (≠ I156), A180 (≠ S157), H232 (= H213), Y235 (≠ F216), N268 (≠ G243), G311 (= G288), E314 (≠ G291)
3i0pA Crystal structure of malate dehydrogenase from entamoeba histolytica
24% identity, 98% coverage: 2:325/330 of query aligns to 24:360/361 of 3i0pA
- active site: H46 (= H24)
- binding nicotinamide-adenine-dinucleotide: M43 (≠ H21), H46 (= H24), H119 (= H96), I122 (≠ C99), A123 (≠ L100), T159 (≠ P138), P161 (= P140), F176 (≠ I154), D177 (= D155), G178 (≠ I156), A179 (≠ S157), P184 (≠ T162), R187 (≠ M165), Y320 (≠ R285), A322 (≠ P287), G323 (= G288), K325 (≠ R290), E326 (≠ G291)
1v9nA Structure of malate dehydrogenase from pyrococcus horikoshii ot3
25% identity, 96% coverage: 2:319/330 of query aligns to 35:342/348 of 1v9nA
- active site: H55 (= H24)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H55 (= H24), H127 (= H96), G129 (≠ A98), I130 (≠ C99), A131 (≠ L100), T167 (≠ P138), P169 (= P140), L183 (≠ I154), D184 (= D155), M185 (≠ I156), A186 (≠ S157), P191 (≠ T162), W308 (≠ R285), H310 (≠ P287), G311 (= G288), K313 (≠ R290), G314 (= G291)
Sites not aligning to the query:
1z2iA Crystal structure of agrobacterium tumefaciens malate dehydrogenase, new york structural genomics consortium
25% identity, 98% coverage: 2:326/330 of query aligns to 23:348/350 of 1z2iA
- active site: H45 (= H24)
- binding nicotinamide-adenine-dinucleotide: V42 (≠ H21), H45 (= H24), H117 (= H96), F118 (≠ I97), G119 (≠ A98), P120 (≠ C99), A121 (≠ L100), T157 (≠ P138), P159 (= P140), D175 (= D155), M176 (≠ I156), A177 (≠ S157), P182 (≠ T162), F227 (≠ H213), K228 (= K214), M307 (≠ R285), R312 (= R290), E313 (≠ G291)
2cwhA Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH and pyrrole-2-carboxylate (see paper)
30% identity, 64% coverage: 20:231/330 of query aligns to 41:245/332 of 2cwhA
- active site: H45 (= H24)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H45 (= H24), A119 (= A98), A120 (≠ C99), L121 (= L100), H148 (= H129), T157 (≠ P138), P159 (= P140), F174 (≠ I154), D175 (= D155), L176 (≠ I156), A177 (≠ S157), H227 (= H213), K228 (= K214)
- binding pyrrole-2-carboxylate: H45 (= H24), R49 (≠ L28), M142 (≠ G123), T157 (≠ P138), H183 (≠ Q163), G184 (= G164)
Sites not aligning to the query:
2cwfB Crystal structure of delta1-piperideine-2-carboxylate reductase from pseudomonas syringae complexed with NADPH (see paper)
30% identity, 64% coverage: 20:231/330 of query aligns to 44:248/337 of 2cwfB
- active site: H48 (= H24)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: H48 (= H24), H120 (= H96), A122 (= A98), A123 (≠ C99), L124 (= L100), T160 (≠ P138), P162 (= P140), F177 (≠ I154), D178 (= D155), L179 (≠ I156), A180 (≠ S157), H230 (= H213), K231 (= K214)
Sites not aligning to the query:
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, 64% coverage: 20:231/330 of query aligns to 50:254/343 of Q4U331
Sites not aligning to the query:
- 309:315 binding in other chain
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)
23% identity, 89% coverage: 23:315/330 of query aligns to 43:331/335 of 1s20G
- active site: H44 (= H24)
- binding nicotinamide-adenine-dinucleotide: H44 (= H24), H116 (= H96), W147 (≠ H129), T156 (≠ P138), P158 (= P140), D172 (= D155), M173 (≠ I156), S174 (= S157), W224 (≠ M209), K225 (≠ T210), R301 (= R285), G304 (= G288), E306 (≠ R290)
4fjuA Crystal structure of ureidoglycolate dehydrogenase in ternary complex with nadh and glyoxylate (see paper)
27% identity, 68% coverage: 6:231/330 of query aligns to 26:241/338 of 4fjuA
- binding glyoxylic acid: R48 (≠ L28), H116 (= H96), S140 (= S119), D141 (= D120)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I41 (≠ H21), H44 (= H24), H116 (= H96), G118 (≠ A98), I120 (≠ L100), S140 (= S119), F147 (≠ H129), T156 (≠ P138), P158 (= P140), F173 (≠ I154), D174 (= D155), M175 (≠ I156), A176 (≠ S157), P223 (≠ H213), K224 (= K214)
Sites not aligning to the query:
P77555 Ureidoglycolate dehydrogenase (NAD(+)); EC 1.1.1.350 from Escherichia coli (strain K12) (see paper)
27% identity, 68% coverage: 6:231/330 of query aligns to 26:241/349 of P77555
- S43 (≠ T23) mutation to A: 4- and 10-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H44 (= H24) 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 (≠ L28) mutation to A: Loss of dehydrogenase activity.
- Y52 (= Y32) mutation to F: 2- and 16-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- H116 (= H96) mutation to A: Loss of dehydrogenase activity.
- S140 (= S119) mutation to A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Strong decrease of the catalytic efficiency.
- D141 (= D120) 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.
Sites not aligning to the query:
- 251 M→A: 2- and 13-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
- 259 R→A: 2- and 12-fold decrease of the affinity for NAD and (S)-ureidoglycolate, respectively. Slight decrease of the catalytic efficiency.
Query Sequence
>H281DRAFT_05436 FitnessBrowser__Burk376:H281DRAFT_05436
MEDVKALAVARTLVDGDLMGHDTHGLALLPAYIGEIENGAMTCSGEPEVVSDRGGSVLWD
GRRLPGPWLVLSGIETLAPRAKKYGTATLVIRRSHHIACLASYLERATADGFMILLSSSD
PAGQSVAPHGGTRSVFTPNPIAAGIPTSGSPFLIDISSSMVTQGMTARRHKAGQHFEEAC
FLDADGQPSGDPSVLCTDPPGSILPIGGMTGGHKGFGLALLIEALTGGLAGHGRADPADG
WGGTVFLSLYDTAAFGGLAAFVRQMDWLGDACRNNPPRPGTAGVRMPGDRGLNLKREQLR
DGVALHSTIAPALEACARRYDIPLPSALPG
Or try a new SitesBLAST search
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