SitesBLAST
Comparing WP_012409068.1 NCBI__GCF_000020025.1:WP_012409068.1 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)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
57% identity, 99% coverage: 1:330/334 of query aligns to 8:336/336 of 5z20F
- active site: S108 (= S101), R241 (= R234), D265 (= D258), E270 (= E263), H302 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y100), G160 (= G153), Q161 (≠ K154), I162 (= I155), Y180 (= Y173), D181 (= D174), P182 (≠ V175), C212 (= C205), P213 (= P206), T218 (= T211), T239 (= T232), G240 (≠ S233), R241 (= R234), H302 (= H295), A304 (= A297)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
58% identity, 98% coverage: 1:328/334 of query aligns to 1:328/330 of 4cukA
- active site: S101 (= S101), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y100), G153 (= G153), K154 (= K154), I155 (= I155), F173 (≠ Y173), D174 (= D174), P175 (≠ V175), H204 (= H204), C205 (= C205), P206 (= P206), N211 (≠ T211), T232 (= T232), Y260 (= Y260), H295 (= H295), A297 (= A297)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
50% identity, 97% coverage: 6:330/334 of query aligns to 16:346/346 of 4zgsA
- active site: S111 (= S101), R244 (= R234), D268 (= D258), E273 (= E263), H311 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y100), G163 (= G153), A164 (≠ K154), I165 (= I155), D184 (= D174), C215 (= C205), P216 (= P206), L218 (≠ T208), S220 (≠ E210), T221 (= T211), S243 (= S233), H311 (= H295), F314 (= F298)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
49% identity, 98% coverage: 2:328/334 of query aligns to 3:329/331 of 5z21B
- active site: S101 (= S101), R235 (= R234), D259 (= D258), E264 (= E263), H296 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y100), I105 (≠ V105), G153 (= G153), K154 (= K154), I155 (= I155), D174 (= D174), L175 (≠ V175), P207 (= P206), T212 (= T211), T233 (= T232), G234 (≠ S233), R235 (= R234), H296 (= H295), Y299 (≠ F298)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
45% identity, 95% coverage: 1:317/334 of query aligns to 3:320/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V105), G154 (= G153), N155 (≠ K154), I156 (= I155), D176 (= D174), I177 (≠ V175), I178 (≠ Y176), T208 (≠ C205), P209 (= P206), T214 (= T211), V235 (≠ T232), H298 (= H295), A300 (= A297), W301 (≠ F298)
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)
36% identity, 98% coverage: 2:329/334 of query aligns to 3:331/333 of P26297
- HI 156:157 (≠ KI 154:155) binding NAD(+)
- D176 (= D174) binding NAD(+)
- H206 (= H204) mutation to Q: Increase of activity.
- VP 207:208 (≠ CP 205:206) binding NAD(+)
- N213 (≠ T211) binding NAD(+)
- R236 (= R234) mutation to K: Decrease of activity.
- D260 (= D258) binding NAD(+); mutation to N: Decrease of activity.
- E265 (= E263) mutation to Q: Decrease of activity.
- H297 (= H295) mutation to Q: 90% loss of activity.
1j49A Insights into domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from lactobacillus bulgaricus (see paper)
36% identity, 98% coverage: 2:329/334 of query aligns to 3:331/332 of 1j49A
- active site: S103 (= S101), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y100), I107 (≠ V105), G153 (= G151), G155 (= G153), I157 (= I155), Y175 (= Y173), D176 (= D174), I177 (≠ V175), V207 (≠ C205), P208 (= P206), N213 (≠ T211), V234 (≠ T232), S235 (= S233), R236 (= R234), H297 (= H295), A299 (= A297), F300 (= F298)
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
36% identity, 96% coverage: 2:321/334 of query aligns to 3:323/337 of 2dldA
- active site: S103 (= S101), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T152), G155 (= G153), H156 (≠ K154), I157 (= I155), D176 (= D174), I177 (≠ V175), V207 (≠ C205), 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)
36% identity, 96% coverage: 2:321/334 of query aligns to 3:323/337 of P30901
- D176 (= D174) binding NAD(+)
- VP 207:208 (≠ CP 205:206) binding NAD(+)
- N213 (≠ T211) binding NAD(+)
- D260 (= D258) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
39% identity, 79% coverage: 48:311/334 of query aligns to 46:310/334 of 3kb6B
- active site: S97 (= S101), R231 (= R234), D255 (= D258), E260 (= E263), H294 (= H295)
- binding lactic acid: F49 (= F51), S72 (≠ C76), V73 (≠ A77), G74 (= G78), Y96 (= Y100), R231 (= R234), H294 (= H295)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A77), Y96 (= Y100), V101 (= V105), G150 (= G153), R151 (≠ K154), I152 (= I155), D171 (= D174), V172 (= V175), P203 (= P206), T229 (= T232), A230 (≠ S233), R231 (= R234), H294 (= H295), A296 (= A297), Y297 (≠ F298)
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
32% identity, 98% coverage: 1:328/334 of query aligns to 1:328/330 of 1dxyA
- active site: S101 (= S101), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ A77), Y100 (= Y100), Y298 (≠ F298)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y100), G152 (= G151), G154 (= G153), H155 (≠ K154), I156 (= I155), Y174 (= Y173), D175 (= D174), P176 (≠ V175), H204 (= H204), V205 (≠ C205), P206 (= P206), N211 (≠ T211), T232 (= T232), A233 (≠ S233), R234 (= R234), H295 (= H295), Y298 (≠ F298)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
32% identity, 98% coverage: 1:328/334 of query aligns to 1:328/333 of P17584
- HI 155:156 (≠ KI 154:155) binding NAD(+)
- D175 (= D174) binding NAD(+)
- V205 (≠ C205) binding NAD(+)
- N211 (≠ T211) binding NAD(+)
- TAR 232:234 (≠ TSR 232:234) binding NAD(+)
- D258 (= D258) binding NAD(+)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
33% identity, 96% coverage: 1:322/334 of query aligns to 1:322/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V154 (≠ T152), G155 (= G153), H156 (≠ K154), I157 (= I155), Y175 (= Y173), D176 (= D174), H205 (= H204), T206 (≠ C205), P207 (= P206), A233 (≠ T232), A234 (≠ S233), D259 (= D258), H295 (= H295), A297 (= A297)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
32% identity, 94% coverage: 1:315/334 of query aligns to 1:315/332 of 4xkjA
- active site: S102 (= S101), R234 (= R234), D258 (= D258), E263 (= E263), H295 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), V106 (= V105), G152 (= G151), G154 (= G153), R155 (≠ K154), I156 (= I155), D175 (= D174), I176 (≠ V175), R179 (≠ N178), H204 (= H204), V205 (≠ C205), P206 (= P206), T211 (= T211), A232 (≠ T232), R234 (= R234), H295 (= H295), G297 (≠ A297), F298 (= F298)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
39% identity, 79% coverage: 39:303/334 of query aligns to 44:286/304 of 1wwkA
- active site: S96 (= S101), R230 (= R234), D254 (= D258), E259 (= E263), H278 (= H295)
- binding nicotinamide-adenine-dinucleotide: V100 (= V105), G146 (= G151), F147 (≠ T152), G148 (= G153), R149 (≠ K154), I150 (= I155), Y168 (= Y173), D169 (= D174), P170 (≠ V175), V201 (≠ C205), P202 (= P206), T207 (= T211), T228 (= T232), S229 (= S233), D254 (= D258), H278 (= H295), G280 (≠ A297)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
30% identity, 96% coverage: 2:323/334 of query aligns to 2:326/331 of 2yq5C
- active site: S102 (= S101), R236 (= R234), D260 (= D258), E265 (= E263), H297 (= H295)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V155 (≠ T152), G156 (= G153), H157 (≠ K154), I158 (= I155), Y176 (= Y173), D177 (= D174), V178 (= V175), H206 (= H204), T207 (≠ C205), P208 (= P206), A235 (≠ S233), R236 (= R234), H297 (= H295), F300 (= F298)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
33% identity, 75% coverage: 70:321/334 of query aligns to 69:314/334 of 5aovA
- active site: L100 (≠ S101), R241 (= R234), D265 (= D258), E270 (= E263), H288 (= H295)
- binding glyoxylic acid: Y74 (≠ R75), A75 (≠ C76), V76 (≠ A77), G77 (= G78), R241 (= R234), H288 (= H295)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A77), T104 (≠ V105), F158 (≠ T152), G159 (= G153), R160 (≠ K154), I161 (= I155), S180 (≠ D174), R181 (≠ V175), A211 (≠ H204), V212 (≠ C205), P213 (= P206), T218 (= T211), I239 (≠ T232), A240 (≠ S233), R241 (= R234), H288 (= H295), G290 (≠ A297)
Sites not aligning to the query:
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
33% identity, 77% coverage: 67:322/334 of query aligns to 65:317/331 of 1hl3A
- active site: S99 (= S101), R241 (= R234), D265 (= D258), E270 (= E263), H290 (= H295)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V105), G158 (= G153), R159 (≠ K154), V160 (≠ I155), D179 (= D174), Y181 (= Y176), H211 (= H204), C212 (= C205), G213 (≠ P206), N218 (≠ T211), T239 (= T232), A240 (≠ S233), R241 (= R234), D265 (= D258), H290 (= H295)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
33% identity, 77% coverage: 67:322/334 of query aligns to 65:317/331 of 1hkuA
- active site: S99 (= S101), R241 (= R234), D265 (= D258), E270 (= E263), H290 (= H295)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ A77), T103 (≠ V105), G156 (= G151), G158 (= G153), R159 (≠ K154), V160 (≠ I155), Y178 (= Y173), D179 (= D174), P180 (≠ V175), Y181 (= Y176), C212 (= C205), N218 (≠ T211), T239 (= T232), A240 (≠ S233), R241 (= R234), H290 (= H295), W293 (≠ F298)
Sites not aligning to the query:
Q9Z2F5 C-terminal-binding protein 1; CtBP1; 50 kDa BFA-dependent ADP-ribosylation substrate; BARS-50; C-terminal-binding protein 3; CtBP3; EC 1.1.1.- from Rattus norvegicus (Rat) (see 3 papers)
33% identity, 77% coverage: 67:322/334 of query aligns to 79:331/430 of Q9Z2F5
- S89 (≠ A77) binding NAD(+)
- IGLGRV 169:174 (≠ VGTGKI 150:155) binding NAD(+)
- G172 (= G153) mutation to E: Loss dimerization and of NAD binding.
- D193 (= D174) binding NAD(+)
- 226:232 (vs. 205:211, 29% identical) binding NAD(+)
- TAR 253:255 (≠ TSR 232:234) binding NAD(+)
- D279 (= D258) binding NAD(+)
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
- 55 V→R: Strongly reduces interaction with E1A.
Query Sequence
>WP_012409068.1 NCBI__GCF_000020025.1:WP_012409068.1
MKVAVFSTKVYDRQFLSTVNSPTQHELVFFEPRLNRDTAILAAGFPAVCVFVHDQVDAPT
LKLLASRGTRLVVLRCAGFNNVDLQAAADLGITVVRVPAYSPYGVAEHAVGLILSLNRKI
HRAYNRVREGNFSLDGLLGFNLHERTVGIVGTGKIGLILGQIMKGFGCNLLAYDVYRNPE
LEALGGKYVELPELFANSDIISLHCPLTPETHHLINAEAIEQIKPGVMLINTSRGALIDT
QAVIEGLKSGKIGYLGVDVYEQESELFFEDLSGEIIQDDIFQRLTTFPNVLITGHQAFFT
AEALHNIAETTFANIADVENGRPCANEIRAQPSA
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