SitesBLAST
Comparing WP_077276850.1 NCBI__GCF_001998885.1:WP_077276850.1 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)
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)
41% identity, 98% coverage: 5:326/327 of query aligns to 10:331/333 of P26297
- HI 156:157 (≠ RI 151:152) binding NAD(+)
- D176 (= D171) binding NAD(+)
- H206 (= H201) mutation to Q: Increase of activity.
- VP 207:208 (≠ MP 202:203) binding NAD(+)
- N213 (= N208) binding NAD(+)
- R236 (= R231) mutation to K: Decrease of activity.
- D260 (= D255) binding NAD(+); mutation to N: Decrease of activity.
- E265 (= E260) mutation to Q: Decrease of activity.
- H297 (= H292) 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)
41% identity, 98% coverage: 5:326/327 of query aligns to 10:331/332 of 1j49A
- active site: S103 (= S97), R236 (= R231), D260 (= D255), E265 (= E260), H297 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y96), I107 (= I101), G153 (= G148), G155 (= G150), I157 (= I152), Y175 (= Y170), D176 (= D171), I177 (≠ V172), V207 (≠ M202), P208 (= P203), N213 (= N208), V234 (≠ P229), S235 (≠ A230), R236 (= R231), H297 (= H292), A299 (= A294), F300 (= F295)
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
38% identity, 98% coverage: 5:325/327 of query aligns to 10:330/337 of 2dldA
- active site: S103 (= S97), R236 (= R231), D260 (= D255), E265 (= E260), H297 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T149), G155 (= G150), H156 (≠ R151), I157 (= I152), D176 (= D171), I177 (≠ V172), V207 (≠ M202), P208 (= P203), N213 (= N208), C234 (≠ P229), S235 (≠ A230), H297 (= H292)
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)
38% identity, 98% coverage: 5:325/327 of query aligns to 10:330/337 of P30901
- D176 (= D171) binding NAD(+)
- VP 207:208 (≠ MP 202:203) binding NAD(+)
- N213 (= N208) binding NAD(+)
- D260 (= D255) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
38% identity, 99% coverage: 3:325/327 of query aligns to 7:328/330 of 1dxyA
- active site: S101 (= S97), R234 (= R231), D258 (= D255), E263 (= E260), H295 (= H292)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ A73), Y100 (= Y96), Y298 (≠ F295)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y96), G152 (= G148), G154 (= G150), H155 (≠ R151), I156 (= I152), Y174 (= Y170), D175 (= D171), P176 (≠ V172), H204 (= H201), V205 (≠ M202), P206 (= P203), N211 (= N208), T232 (≠ P229), A233 (= A230), R234 (= R231), H295 (= H292), Y298 (≠ F295)
P17584 D-2-hydroxyacid dehydrogenase (NAD+); D-2-hydroxyisocaproate dehydrogenase; D-HicDH; EC 1.1.1.345 from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
38% identity, 99% coverage: 3:325/327 of query aligns to 7:328/333 of P17584
- Y100 (= Y96) binding 4-methyl-2-oxopentanoate
- H155 (≠ R151) binding NAD(+)
- I156 (= I152) binding NAD(+)
- D175 (= D171) binding NAD(+)
- V205 (≠ M202) binding NAD(+)
- N211 (= N208) binding NAD(+)
- T232 (≠ P229) binding NAD(+)
- R234 (= R231) binding NAD(+)
- D258 (= D255) binding NAD(+)
- H295 (= H292) binding 4-methyl-2-oxopentanoate
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
39% identity, 100% coverage: 1:326/327 of query aligns to 5:329/332 of 4xkjA
- active site: S102 (= S97), R234 (= R231), D258 (= D255), E263 (= E260), H295 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y96), V106 (≠ I101), G152 (= G148), G154 (= G150), R155 (= R151), I156 (= I152), D175 (= D171), I176 (≠ V172), R179 (≠ N175), H204 (= H201), V205 (≠ M202), P206 (= P203), T211 (≠ N208), A232 (≠ P229), R234 (= R231), H295 (= H292), G297 (≠ A294), F298 (= F295)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
37% identity, 98% coverage: 8:326/327 of query aligns to 12:331/331 of 2yq5C
- active site: S102 (= S97), R236 (= R231), D260 (= D255), E265 (= E260), H297 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y96), I106 (= I101), V155 (≠ T149), G156 (= G150), H157 (≠ R151), I158 (= I152), Y176 (= Y170), D177 (= D171), V178 (= V172), H206 (= H201), T207 (≠ M202), P208 (= P203), A235 (= A230), R236 (= R231), H297 (= H292), F300 (= F295)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
39% identity, 79% coverage: 46:304/327 of query aligns to 40:306/334 of 3kb6B
- active site: S97 (= S97), R231 (= R231), D255 (= D255), E260 (= E260), H294 (= H292)
- binding lactic acid: F49 (≠ E55), S72 (= S72), V73 (≠ A73), G74 (= G74), Y96 (= Y96), R231 (= R231), H294 (= H292)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A73), Y96 (= Y96), V101 (≠ I101), G150 (= G150), R151 (= R151), I152 (= I152), D171 (= D171), V172 (= V172), P203 (= P203), T229 (≠ P229), A230 (= A230), R231 (= R231), H294 (= H292), A296 (= A294), Y297 (≠ F295)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
34% identity, 96% coverage: 6:319/327 of query aligns to 10:321/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y96), I106 (= I101), V154 (≠ T149), G155 (= G150), H156 (≠ R151), I157 (= I152), Y175 (= Y170), D176 (= D171), H205 (= H201), T206 (≠ M202), P207 (= P203), A233 (≠ P229), A234 (= A230), D259 (= D255), H295 (= H292), A297 (= A294)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
38% identity, 84% coverage: 30:304/327 of query aligns to 44:323/346 of 4zgsA
- active site: S111 (= S97), R244 (= R231), D268 (= D255), E273 (= E260), H311 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y96), G163 (= G150), A164 (≠ R151), I165 (= I152), D184 (= D171), C215 (≠ M202), P216 (= P203), L218 (≠ T205), S220 (≠ D207), T221 (≠ N208), S243 (≠ A230), H311 (= H292), F314 (= F295)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
34% identity, 89% coverage: 19:310/327 of query aligns to 30:320/336 of 5z20F
- active site: S108 (= S97), R241 (= R231), D265 (= D255), E270 (= E260), H302 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y96), G160 (= G150), Q161 (≠ R151), I162 (= I152), Y180 (= Y170), D181 (= D171), P182 (≠ V172), C212 (≠ M202), P213 (= P203), T218 (≠ N208), T239 (≠ P229), G240 (≠ A230), R241 (= R231), H302 (= H292), A304 (= A294)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
34% identity, 91% coverage: 5:301/327 of query aligns to 10:305/331 of 5z21B
- active site: S101 (= S97), R235 (= R231), D259 (= D255), E264 (= E260), H296 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y96), I105 (= I101), G153 (= G150), K154 (≠ R151), I155 (= I152), D174 (= D171), L175 (≠ V172), P207 (= P203), T212 (≠ N208), T233 (≠ P229), G234 (≠ A230), R235 (= R231), H296 (= H292), Y299 (≠ F295)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
35% identity, 76% coverage: 52:301/327 of query aligns to 57:307/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (≠ I101), G154 (= G150), N155 (≠ R151), I156 (= I152), D176 (= D171), I177 (≠ V172), I178 (≠ Y173), T208 (≠ M202), P209 (= P203), T214 (≠ N208), V235 (≠ P229), H298 (= H292), A300 (= A294), W301 (≠ F295)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
30% identity, 92% coverage: 5:304/327 of query aligns to 9:315/330 of 4cukA
- active site: S101 (= S97), R234 (= R231), D258 (= D255), E263 (= E260), H295 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y96), G153 (= G150), K154 (≠ R151), I155 (= I152), F173 (≠ Y170), D174 (= D171), P175 (≠ V172), H204 (= H201), C205 (≠ M202), P206 (= P203), N211 (= N208), T232 (≠ P229), Y260 (= Y257), H295 (= H292), A297 (= A294)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
35% identity, 76% coverage: 56:304/327 of query aligns to 52:299/332 of 6biiA
- active site: L99 (≠ S97), R240 (= R231), D264 (= D255), E269 (= E260), H287 (= H292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ A73), T103 (≠ I101), G156 (= G148), F157 (≠ T149), G158 (= G150), R159 (= R151), I160 (= I152), A179 (≠ D171), R180 (≠ V172), S181 (≠ Y173), K183 (≠ N175), V211 (≠ M202), P212 (= P203), E216 (≠ D207), T217 (≠ N208), V238 (≠ P229), A239 (= A230), R240 (= R231), D264 (= D255), H287 (= H292), G289 (≠ A294)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 76% coverage: 56:304/327 of query aligns to 53:300/334 of 5aovA
- active site: L100 (≠ S97), R241 (= R231), D265 (= D255), E270 (= E260), H288 (= H292)
- binding glyoxylic acid: L53 (≠ M56), L53 (≠ M56), Y74 (≠ R71), A75 (≠ S72), V76 (≠ A73), G77 (= G74), R241 (= R231), H288 (= H292)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A73), T104 (≠ I101), F158 (≠ T149), G159 (= G150), R160 (= R151), I161 (= I152), S180 (≠ D171), R181 (≠ V172), A211 (≠ H201), V212 (≠ M202), P213 (= P203), T218 (≠ N208), I239 (≠ P229), A240 (= A230), R241 (= R231), H288 (= H292), G290 (≠ A294)
Sites not aligning to the query:
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
32% identity, 81% coverage: 37:300/327 of query aligns to 41:298/328 of 4u6sA
- active site: S99 (= S97), R241 (= R231), D265 (= D255), E270 (= E260), H290 (= H292)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ I101), G156 (= G148), G158 (= G150), R159 (= R151), V160 (≠ I152), Y178 (= Y170), D179 (= D171), P180 (≠ V172), Y181 (= Y173), H211 (= H201), C212 (≠ M202), G213 (≠ P203), N218 (= N208), T239 (≠ P229), A240 (= A230), R241 (= R231), H290 (= H292), W293 (≠ F295)
- binding 3-phenylpyruvic acid: Y51 (≠ Q47), H52 (≠ Q48), I73 (≠ R71), G74 (≠ S72), S75 (≠ A73), G76 (= G74), R241 (= R231), W293 (≠ F295)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
32% identity, 81% coverage: 37:300/327 of query aligns to 41:298/328 of 4u6qA
- active site: S99 (= S97), R241 (= R231), D265 (= D255), E270 (= E260), H290 (= H292)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ Q47), I73 (≠ R71), G74 (≠ S72), S75 (≠ A73), G76 (= G74), R241 (= R231), H290 (= H292), W293 (≠ F295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ A73), T103 (≠ I101), G156 (= G148), R159 (= R151), V160 (≠ I152), Y178 (= Y170), D179 (= D171), P180 (≠ V172), Y181 (= Y173), H211 (= H201), C212 (≠ M202), G213 (≠ P203), N218 (= N208), T239 (≠ P229), A240 (= A230), R241 (= R231), H290 (= H292), W293 (≠ F295)
Sites not aligning to the query:
6cdfA Human ctbp1 (28-378) (see paper)
32% identity, 81% coverage: 37:300/327 of query aligns to 42:299/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ I101), G157 (= G148), R160 (= R151), V161 (≠ I152), Y179 (= Y170), D180 (= D171), P181 (≠ V172), Y182 (= Y173), H212 (= H201), C213 (≠ M202), N219 (= N208), T240 (≠ P229), A241 (= A230), R242 (= R231), H291 (= H292), W294 (≠ F295)
Query Sequence
>WP_077276850.1 NCBI__GCF_001998885.1:WP_077276850.1
MMGAREDERRFAEKWAKDHNVTIEVSTDILSDDTYHLLNGYDGLSLQQTMGIPAEMYEKL
SQDGFRQIAQRSAGVDMYDLKEAKKHGISITNVPAYSPNAIAEFTVASALNCLRHMQAIQ
KRVKNHNFSWDKSILAREVRSLTIGVMGTGRIGQITAQLFAAFGAKVIGYDVYQNPNAEN
YLTYIDSFDEFLAQSDLLTIHMPLTDDNYHQFNTETFNKMKPGAILLNPARGAIIDTKDL
IAALDSGQISCCALDTYENEMPYVTKDWSGKTLNDPILEELINREDVLYTPHIAFYTETA
VENLVFGGLDACLSILTNGTADTIVNP
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