SitesBLAST
Comparing Echvi_3161 FitnessBrowser__Cola:Echvi_3161 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
52% identity, 99% coverage: 1:328/331 of query aligns to 1:328/330 of 4cukA
- active site: S101 (= S100), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y99), G153 (= G152), K154 (= K153), I155 (= I154), F173 (≠ Q172), D174 (= D173), P175 (≠ I174), H204 (= H204), C205 (≠ V205), P206 (= P206), N211 (≠ T211), T232 (= T232), Y260 (= Y260), H295 (= H295), A297 (= A297)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
51% identity, 98% coverage: 1:323/331 of query aligns to 8:330/336 of 5z20F
- active site: S108 (= S100), R241 (= R234), D265 (= D258), E270 (= E263), H302 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y99), G160 (= G152), Q161 (≠ K153), I162 (= I154), Y180 (≠ Q172), D181 (= D173), P182 (≠ I174), C212 (≠ V205), P213 (= P206), T218 (= T211), T239 (= T232), G240 (≠ S233), R241 (= R234), H302 (= H295), A304 (= A297)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
50% identity, 92% coverage: 25:329/331 of query aligns to 27:330/331 of 5z21B
- active site: S101 (= S100), R235 (= R234), D259 (= D258), E264 (= E263), H296 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y99), I105 (= I104), G153 (= G152), K154 (= K153), I155 (= I154), D174 (= D173), L175 (≠ I174), P207 (= P206), T212 (= T211), T233 (= T232), G234 (≠ S233), R235 (= R234), H296 (= H295), Y299 (≠ F298)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
48% identity, 91% coverage: 28:328/331 of query aligns to 39:344/346 of 4zgsA
- active site: S111 (= S100), R244 (= R234), D268 (= D258), E273 (= E263), H311 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y99), G163 (= G152), A164 (≠ K153), I165 (= I154), D184 (= D173), C215 (≠ V205), P216 (= P206), L218 (≠ K208), S220 (= S210), T221 (= T211), S243 (= S233), H311 (= H295), F314 (= F298)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
44% identity, 97% coverage: 1:322/331 of query aligns to 3:325/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (≠ I104), G154 (= G152), N155 (≠ K153), I156 (= I154), D176 (= D173), I177 (= I174), I178 (≠ E175), T208 (≠ V205), P209 (= P206), T214 (= T211), V235 (≠ T232), H298 (= H295), A300 (= A297), W301 (≠ F298)
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
35% identity, 98% coverage: 2:324/331 of query aligns to 3:327/337 of 2dldA
- active site: S103 (= S100), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T151), G155 (= G152), H156 (≠ K153), I157 (= I154), D176 (= D173), I177 (= I174), V207 (= V205), P208 (= P206), N213 (≠ T211), C234 (≠ T232), S235 (= S233), H297 (= H295)
Sites not aligning to the query:
P30901 D-lactate dehydrogenase; D-LDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28 from Lactobacillus helveticus (Lactobacillus suntoryeus) (see paper)
35% identity, 98% coverage: 2:324/331 of query aligns to 3:327/337 of P30901
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P26297 D-lactate dehydrogenase; D-LDH; D-specific 2-hydroxyacid dehydrogenase; EC 1.1.1.28 from Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14) (see 2 papers)
38% identity, 91% coverage: 6:307/331 of query aligns to 7:309/333 of P26297
- HI 156:157 (≠ KI 153:154) binding
- D176 (= D173) binding
- H206 (= H204) mutation to Q: Increase of activity.
- VP 207:208 (= VP 205:206) binding
- N213 (≠ T211) binding
- R236 (= R234) mutation to K: Decrease of activity.
- D260 (= D258) binding ; mutation to N: Decrease of activity.
- E265 (= E263) mutation to Q: Decrease of activity.
- H297 (= H295) mutation to Q: 90% loss of activity.
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
41% identity, 84% coverage: 44:320/331 of query aligns to 43:319/334 of 3kb6B
- active site: S97 (= S100), R231 (= R234), D255 (= D258), E260 (= E263), H294 (= H295)
- binding lactic acid: F49 (= F50), S72 (= S75), V73 (≠ A76), G74 (= G77), Y96 (= Y99), R231 (= R234), H294 (= H295)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A76), Y96 (= Y99), V101 (≠ I104), G150 (= G152), R151 (≠ K153), I152 (= I154), D171 (= D173), V172 (≠ I174), P203 (= P206), T229 (= T232), A230 (≠ S233), R231 (= R234), H294 (= H295), A296 (= A297), Y297 (≠ F298)
1j49A Insights into domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from lactobacillus bulgaricus (see paper)
37% identity, 91% coverage: 6:307/331 of query aligns to 7:309/332 of 1j49A
- active site: S103 (= S100), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y99), I107 (= I104), G153 (= G150), G155 (= G152), I157 (= I154), Y175 (≠ Q172), D176 (= D173), I177 (= I174), V207 (= V205), P208 (= P206), N213 (≠ T211), V234 (≠ T232), S235 (= S233), R236 (= R234), H297 (= H295), A299 (= A297), F300 (= F298)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
32% identity, 92% coverage: 27:329/331 of query aligns to 25:329/333 of P17584
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
32% identity, 92% coverage: 27:329/331 of query aligns to 25:329/330 of 1dxyA
- active site: S101 (= S100), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ A76), Y100 (= Y99), Y298 (≠ F298)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y99), G152 (= G150), G154 (= G152), H155 (≠ K153), I156 (= I154), Y174 (≠ Q172), D175 (= D173), P176 (≠ I174), H204 (= H204), V205 (= V205), P206 (= P206), N211 (≠ T211), T232 (= T232), A233 (≠ S233), R234 (= R234), H295 (= H295), Y298 (≠ F298)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
38% identity, 76% coverage: 63:312/331 of query aligns to 65:312/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y99), I106 (= I104), V154 (≠ T151), G155 (= G152), H156 (≠ K153), I157 (= I154), Y175 (≠ Q172), D176 (= D173), H205 (= H204), T206 (≠ V205), P207 (= P206), A233 (≠ T232), A234 (≠ S233), D259 (= D258), H295 (= H295), A297 (= A297)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
35% identity, 94% coverage: 1:312/331 of query aligns to 1:312/332 of 4xkjA
- active site: S102 (= S100), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y99), V106 (≠ I104), G152 (= G150), G154 (= G152), R155 (≠ K153), I156 (= I154), D175 (= D173), I176 (= I174), R179 (≠ S177), H204 (= H204), V205 (= V205), P206 (= P206), T211 (= T211), A232 (≠ T232), R234 (= R234), H295 (= H295), G297 (≠ A297), F298 (= F298)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
33% identity, 93% coverage: 2:309/331 of query aligns to 2:311/331 of 2yq5C
- active site: S102 (= S100), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y99), I106 (= I104), V155 (≠ T151), G156 (= G152), H157 (≠ K153), I158 (= I154), Y176 (≠ Q172), D177 (= D173), V178 (≠ I174), H206 (= H204), T207 (≠ V205), P208 (= P206), A235 (≠ S233), R236 (= R234), H297 (= H295), F300 (= F298)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 77% coverage: 40:295/331 of query aligns to 38:278/304 of 1wwkA
- active site: S96 (= S100), R230 (= R234), D254 (= D258), E259 (= E263), H278 (= H295)
- binding nicotinamide-adenine-dinucleotide: V100 (≠ I104), G146 (= G150), F147 (≠ T151), G148 (= G152), R149 (≠ K153), I150 (= I154), Y168 (≠ Q172), D169 (= D173), P170 (≠ I174), V201 (= V205), P202 (= P206), T207 (= T211), T228 (= T232), S229 (= S233), D254 (= D258), H278 (= H295)
Sites not aligning to the query:
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
31% identity, 76% coverage: 68:320/331 of query aligns to 68:313/334 of 5aovA
- active site: L100 (≠ S100), R241 (= R234), D265 (= D258), E270 (= E263), H288 (= H295)
- binding glyoxylic acid: Y74 (≠ R74), A75 (≠ S75), V76 (≠ A76), G77 (= G77), R241 (= R234), H288 (= H295)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A76), T104 (≠ I104), F158 (≠ T151), G159 (= G152), R160 (≠ K153), I161 (= I154), S180 (≠ D173), R181 (≠ I174), A211 (≠ H204), V212 (= V205), P213 (= P206), T218 (= T211), I239 (≠ T232), A240 (≠ S233), R241 (= R234), H288 (= H295), G290 (≠ A297)
Sites not aligning to the query:
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
31% identity, 83% coverage: 46:319/331 of query aligns to 47:311/332 of 6biiA
- active site: L99 (≠ S100), R240 (= R234), D264 (= D258), E269 (= E263), H287 (= H295)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ A76), T103 (≠ I104), G156 (= G150), F157 (≠ T151), G158 (= G152), R159 (≠ K153), I160 (= I154), A179 (≠ D173), R180 (≠ I174), S181 (≠ E175), K183 (≠ S177), V211 (= V205), P212 (= P206), E216 (≠ S210), T217 (= T211), V238 (≠ T232), A239 (≠ S233), R240 (= R234), D264 (= D258), H287 (= H295), G289 (≠ A297)
3wr5A Structural basis on the efficient co2 reduction of acidophilic formate dehydrogenase
30% identity, 77% coverage: 77:330/331 of query aligns to 128:372/401 of 3wr5A
- active site: N151 (≠ S100), R289 (= R234), D313 (= D258), Q318 (≠ E263), H337 (= H295)
- binding nicotinamide-adenine-dinucleotide: N151 (≠ S100), V155 (≠ I104), A203 (≠ G150), G205 (= G152), R206 (≠ K153), I207 (= I154), D226 (= D173), R227 (≠ I174), V260 (= V205), P261 (= P206), T287 (= T232), A288 (≠ S233), R289 (= R234), D313 (= D258), H337 (= H295), S339 (≠ A297), G340 (≠ F298)
Sites not aligning to the query:
Q9S7E4 Formate dehydrogenase, chloroplastic/mitochondrial; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Arabidopsis thaliana (Mouse-ear cress)
31% identity, 56% coverage: 77:263/331 of query aligns to 129:319/384 of Q9S7E4
Sites not aligning to the query:
- 1:29 modified: transit peptide, Chloroplast and mitochondrion
- 338:341 binding
Query Sequence
>Echvi_3161 FitnessBrowser__Cola:Echvi_3161
MKTTIYSTHKFDKPSIENANKGKHQLNFLEFRLTKETALLAEGSKAIALFSNDDASSEVL
DILHKLGIKFIALRSAGFNHVDLEKAAELNIKVARVPAYSPYAIAEHTMALILALNRRLI
KAHNRVREQNFSLNGLTGFDLNGKTVGVIGTGKIGSVLVKILHGFGCNILAQDIEESKDL
IDKYGLIYSDCATLCKHADIISLHVPLKASTKHLINKEHIALMKSGVMLINTSRGGLVDT
KAVIEGLKTKKIGYLGLDVYEEEEGLFFEDHSDDILQDDVIARLMTFNNVLITSHQAFLT
KTALTNIAETTIYNLDCFEKQKPSGNEISIN
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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