SitesBLAST
Comparing WP_029933667.1 NCBI__GCF_000711195.1:WP_029933667.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
52% identity, 99% coverage: 1:327/331 of query aligns to 8:334/336 of 5z20F
- active site: S108 (= S100), R241 (= R233), D265 (= D257), E270 (= E262), H302 (= H294)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y99), G160 (= G152), Q161 (≠ K153), I162 (= I154), Y180 (= Y172), D181 (= D173), P182 (= P174), C212 (= C204), P213 (= P205), T218 (= T210), T239 (= T231), G240 (= G232), R241 (= R233), H302 (= H294), A304 (= A296)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
51% identity, 98% coverage: 1:325/331 of query aligns to 1:326/330 of 4cukA
- active site: S101 (= S100), R234 (= R233), D258 (= D257), E263 (= E262), H295 (= H294)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y99), G153 (= G152), K154 (= K153), I155 (= I154), F173 (≠ Y172), D174 (= D173), P175 (= P174), H204 (= H203), C205 (= C204), P206 (= P205), N211 (≠ T210), T232 (= T231), Y260 (= Y259), H295 (= H294), A297 (= A296)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
52% identity, 98% coverage: 2:327/331 of query aligns to 3:329/331 of 5z21B
- active site: S101 (= S100), R235 (= R233), D259 (= D257), E264 (= E262), H296 (= H294)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y99), I105 (≠ V104), G153 (= G152), K154 (= K153), I155 (= I154), D174 (= D173), L175 (≠ P174), P207 (= P205), T212 (= T210), T233 (= T231), G234 (= G232), R235 (= R233), H296 (= H294), Y299 (= Y297)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
43% identity, 99% coverage: 1:328/331 of query aligns to 3:332/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V104), G154 (= G152), N155 (≠ K153), I156 (= I154), D176 (= D173), I177 (≠ P174), I178 (≠ Y175), T208 (≠ C204), P209 (= P205), T214 (= T210), V235 (≠ T231), H298 (= H294), A300 (= A296), W301 (≠ Y297)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
47% identity, 91% coverage: 28:327/331 of query aligns to 39:344/346 of 4zgsA
- active site: S111 (= S100), R244 (= R233), D268 (= D257), E273 (= E262), H311 (= H294)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y99), G163 (= G152), A164 (≠ K153), I165 (= I154), D184 (= D173), C215 (= C204), P216 (= P205), L218 (≠ N207), S220 (≠ D209), T221 (= T210), S243 (≠ G232), H311 (= H294), F314 (≠ Y297)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
35% identity, 96% coverage: 4:321/331 of query aligns to 3:321/334 of 3kb6B
- active site: S97 (= S100), R231 (= R233), D255 (= D257), E260 (= E262), H294 (= H294)
- binding lactic acid: F49 (= F50), S72 (≠ C75), V73 (≠ A76), G74 (= G77), Y96 (= Y99), R231 (= R233), H294 (= H294)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A76), Y96 (= Y99), V101 (= V104), G150 (= G152), R151 (≠ K153), I152 (= I154), D171 (= D173), V172 (≠ P174), P203 (= P205), T229 (= T231), A230 (≠ G232), R231 (= R233), H294 (= H294), A296 (= A296), Y297 (= Y297)
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)
33% identity, 98% coverage: 2:324/331 of query aligns to 3:331/333 of P26297
- HI 156:157 (≠ KI 153:154) binding
- D176 (= D173) binding
- H206 (= H203) mutation to Q: Increase of activity.
- VP 207:208 (≠ CP 204:205) binding
- N213 (≠ T210) binding
- R236 (= R233) mutation to K: Decrease of activity.
- D260 (= D257) binding ; mutation to N: Decrease of activity.
- E265 (= E262) mutation to Q: Decrease of activity.
- H297 (= H294) 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)
33% identity, 98% coverage: 2:324/331 of query aligns to 3:331/332 of 1j49A
- active site: S103 (= S100), R236 (= R233), D260 (= D257), E265 (= E262), H297 (= H294)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y99), I107 (≠ V104), G153 (= G150), G155 (= G152), I157 (= I154), Y175 (= Y172), D176 (= D173), I177 (≠ P174), V207 (≠ C204), P208 (= P205), N213 (≠ T210), V234 (≠ T231), S235 (≠ G232), R236 (= R233), H297 (= H294), A299 (= A296), F300 (≠ Y297)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
31% identity, 100% coverage: 1:330/331 of query aligns to 1:331/333 of P17584
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
33% identity, 93% coverage: 23:329/331 of query aligns to 26:332/337 of 2dldA
- active site: S103 (= S100), R236 (= R233), D260 (= D257), E265 (= E262), H297 (= H294)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (≠ A151), G155 (= G152), H156 (≠ K153), I157 (= I154), D176 (= D173), I177 (≠ P174), V207 (≠ C204), P208 (= P205), N213 (≠ T210), C234 (≠ T231), S235 (≠ G232), H297 (= H294)
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)
33% identity, 93% coverage: 23:329/331 of query aligns to 26:332/337 of P30901
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
31% identity, 99% coverage: 1:328/331 of query aligns to 1:329/330 of 1dxyA
- active site: S101 (= S100), R234 (= R233), D258 (= D257), E263 (= E262), H295 (= H294)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ A76), Y100 (= Y99), Y298 (= Y297)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y99), G152 (= G150), G154 (= G152), H155 (≠ K153), I156 (= I154), Y174 (= Y172), D175 (= D173), P176 (= P174), H204 (= H203), V205 (≠ C204), P206 (= P205), N211 (≠ D209), T232 (= T231), A233 (≠ G232), R234 (= R233), H295 (= H294), Y298 (= Y297)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
34% identity, 80% coverage: 56:321/331 of query aligns to 58:322/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y99), I106 (≠ V104), V154 (≠ A151), G155 (= G152), H156 (≠ K153), I157 (= I154), Y175 (= Y172), D176 (= D173), H205 (= H203), T206 (≠ C204), P207 (= P205), A233 (≠ T231), A234 (≠ G232), D259 (= D257), H295 (= H294), A297 (= A296)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 84% coverage: 45:321/331 of query aligns to 47:315/334 of 5aovA
- active site: L100 (≠ S100), R241 (= R233), D265 (= D257), E270 (= E262), H288 (= H294)
- binding glyoxylic acid: M52 (≠ F50), L53 (≠ V51), L53 (≠ V51), Y74 (≠ R74), A75 (≠ C75), V76 (≠ A76), G77 (= G77), R241 (= R233), H288 (= H294)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A76), T104 (≠ V104), F158 (≠ A151), G159 (= G152), R160 (≠ K153), I161 (= I154), S180 (≠ D173), R181 (vs. gap), A211 (≠ H203), V212 (≠ C204), P213 (= P205), T218 (= T210), I239 (≠ T231), A240 (≠ G232), R241 (= R233), H288 (= H294), G290 (≠ A296)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
28% identity, 96% coverage: 2:320/331 of query aligns to 2:323/331 of 2yq5C
- active site: S102 (= S100), R236 (= R233), D260 (= D257), E265 (= E262), H297 (= H294)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y99), I106 (≠ V104), V155 (≠ A151), G156 (= G152), H157 (≠ K153), I158 (= I154), Y176 (= Y172), D177 (= D173), V178 (vs. gap), H206 (= H203), T207 (≠ C204), P208 (= P205), A235 (≠ G232), R236 (= R233), H297 (= H294), F300 (≠ Y297)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
31% identity, 96% coverage: 1:317/331 of query aligns to 1:318/332 of 4xkjA
- active site: S102 (= S100), R234 (= R233), D258 (= D257), E263 (= E262), H295 (= H294)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y99), V106 (= V104), G152 (= G150), G154 (= G152), R155 (≠ K153), I156 (= I154), D175 (= D173), I176 (≠ Y175), R179 (≠ K178), H204 (= H203), V205 (≠ C204), P206 (= P205), T211 (= T210), A232 (≠ T231), R234 (= R233), H295 (= H294), G297 (≠ A296), F298 (≠ Y297)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
39% identity, 72% coverage: 68:305/331 of query aligns to 64:289/304 of 1wwkA
- active site: S96 (= S100), R230 (= R233), D254 (= D257), E259 (= E262), H278 (= H294)
- binding nicotinamide-adenine-dinucleotide: V100 (= V104), G146 (= G150), F147 (≠ A151), G148 (= G152), R149 (≠ K153), I150 (= I154), Y168 (= Y172), D169 (= D173), P170 (= P174), V201 (≠ C204), P202 (= P205), T207 (= T210), T228 (= T231), S229 (≠ G232), D254 (= D257), H278 (= H294), G280 (≠ A296)
6cdfA Human ctbp1 (28-378) (see paper)
36% identity, 71% coverage: 69:302/331 of query aligns to 69:299/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V104), G157 (= G150), R160 (≠ K153), V161 (≠ I154), Y179 (= Y172), D180 (= D173), P181 (= P174), Y182 (= Y175), H212 (= H203), C213 (= C204), N219 (≠ T210), T240 (= T231), A241 (≠ G232), R242 (= R233), H291 (= H294), W294 (≠ Y297)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
36% identity, 71% coverage: 69:302/331 of query aligns to 68:298/331 of 1hl3A
- active site: S99 (= S100), R241 (= R233), D265 (= D257), E270 (= E262), H290 (= H294)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V104), G158 (= G152), R159 (≠ K153), V160 (≠ I154), D179 (= D173), Y181 (= Y175), H211 (= H203), C212 (= C204), G213 (≠ P205), N218 (≠ T210), T239 (= T231), A240 (≠ G232), R241 (= R233), D265 (= D257), H290 (= H294)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
36% identity, 71% coverage: 69:302/331 of query aligns to 68:298/331 of 1hkuA
- active site: S99 (= S100), R241 (= R233), D265 (= D257), E270 (= E262), H290 (= H294)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ A76), T103 (≠ V104), G156 (= G150), G158 (= G152), R159 (≠ K153), V160 (≠ I154), Y178 (= Y172), D179 (= D173), P180 (= P174), Y181 (= Y175), C212 (= C204), N218 (≠ T210), T239 (= T231), A240 (≠ G232), R241 (= R233), H290 (= H294), W293 (≠ Y297)
Sites not aligning to the query:
Query Sequence
>WP_029933667.1 NCBI__GCF_000711195.1:WP_029933667.1
MKVAVFSSKPYDKESLRHYEVTEIAMQYFEVPLNVATAHYAQGFDAVSAFVNDELNEATI
EILADGGCKIIALRCAGFNNVDLKAAENLGVKIVRVPAYSPYAVAEHTIGLMLALSRKLY
KSYNRVREGNFSLNGLLGFDFYGKTVGIIGAGKIGLLVAERMKAFGCHVLVYDPYLCKTC
KEQGFEQVPLDQLYEESHVISLHCPLNNDTHRMINQASIEKMRGGVMLINTGRGALIDTQ
ALIYALKSRKVGYVGLDVYEEEGPLFFEDHSNDIILDDNFERLMTFPNVLVTGHQAYFTK
EALEHIAETTIDNLLAFKRAEPLKNEVVLPN
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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