SitesBLAST
Comparing WP_010964851.1 NCBI__GCF_000008765.1:WP_010964851.1 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)
32% identity, 98% coverage: 1:318/326 of query aligns to 8:328/336 of 5z20F
- active site: S108 (= S99), R241 (= R231), D265 (= D255), E270 (= E260), H302 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y98), G160 (= G151), Q161 (≠ K152), I162 (= I153), Y180 (= Y171), D181 (= D172), P182 (≠ I173), C212 (≠ V202), P213 (= P203), T218 (≠ N208), T239 (= T229), G240 (≠ A230), R241 (= R231), H302 (= H292), A304 (= A294)
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
38% identity, 93% coverage: 2:305/326 of query aligns to 3:310/337 of 2dldA
- active site: S103 (= S99), R236 (= R231), D260 (= D255), E265 (= E260), H297 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T150), G155 (= G151), H156 (≠ K152), I157 (= I153), D176 (= D172), I177 (= I173), V207 (= V202), P208 (= P203), N213 (= N208), C234 (≠ T229), 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, 93% coverage: 2:305/326 of query aligns to 3:310/337 of P30901
- D176 (= D172) binding NAD(+)
- VP 207:208 (= VP 202:203) binding NAD(+)
- N213 (= N208) binding NAD(+)
- D260 (= D255) binding NAD(+)
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)
37% identity, 99% coverage: 2:325/326 of query aligns to 3:332/333 of P26297
- HI 156:157 (≠ KI 152:153) binding NAD(+)
- D176 (= D172) binding NAD(+)
- H206 (= H201) mutation to Q: Increase of activity.
- VP 207:208 (= VP 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)
36% identity, 99% coverage: 2:325/326 of query aligns to 3:332/332 of 1j49A
- active site: S103 (= S99), R236 (= R231), D260 (= D255), E265 (= E260), H297 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y98), I107 (≠ V103), G153 (= G149), G155 (= G151), I157 (= I153), Y175 (= Y171), D176 (= D172), I177 (= I173), V207 (= V202), P208 (= P203), N213 (= N208), V234 (≠ T229), S235 (≠ A230), R236 (= R231), H297 (= H292), A299 (= A294), F300 (= F295)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
37% identity, 91% coverage: 13:309/326 of query aligns to 19:328/346 of 4zgsA
- active site: S111 (= S99), R244 (= R231), D268 (= D255), E273 (= E260), H311 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y98), G163 (= G151), A164 (≠ K152), I165 (= I153), D184 (= D172), C215 (≠ V202), P216 (= P203), L218 (≠ A205), S220 (≠ D207), T221 (≠ N208), S243 (≠ A230), H311 (= H292), F314 (= F295)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
37% identity, 97% coverage: 1:315/326 of query aligns to 1:318/333 of P17584
- HI 155:156 (≠ KI 152:153) binding NAD(+)
- D175 (= D172) binding NAD(+)
- V205 (= V202) binding NAD(+)
- N211 (= N208) binding NAD(+)
- TAR 232:234 (= TAR 229:231) binding NAD(+)
- D258 (= D255) binding NAD(+)
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
37% identity, 97% coverage: 1:315/326 of query aligns to 1:318/330 of 1dxyA
- active site: S101 (= S99), R234 (= R231), D258 (= D255), E263 (= E260), H295 (= H292)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ I76), Y100 (= Y98), Y298 (≠ F295)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y98), G152 (= G149), G154 (= G151), H155 (≠ K152), I156 (= I153), Y174 (= Y171), D175 (= D172), P176 (≠ I173), H204 (= H201), V205 (= V202), P206 (= P203), N211 (= N208), T232 (= T229), A233 (= A230), R234 (= R231), H295 (= H292), Y298 (≠ F295)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
33% identity, 99% coverage: 1:322/326 of query aligns to 1:325/330 of 4cukA
- active site: S101 (= S99), R234 (= R231), D258 (= D255), E263 (= E260), H295 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y98), G153 (= G151), K154 (= K152), I155 (= I153), F173 (≠ Y171), D174 (= D172), P175 (vs. gap), H204 (= H201), C205 (≠ V202), P206 (= P203), N211 (= N208), T232 (= T229), Y260 (≠ I257), H295 (= H292), A297 (= A294)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
35% identity, 98% coverage: 2:319/326 of query aligns to 3:323/331 of 5z21B
- active site: S101 (= S99), R235 (= R231), D259 (= D255), E264 (= E260), H296 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y98), I105 (≠ V103), G153 (= G151), K154 (= K152), I155 (= I153), D174 (= D172), L175 (≠ I173), P207 (= P203), T212 (≠ N208), T233 (= T229), G234 (≠ A230), R235 (= R231), H296 (= H292), Y299 (≠ F295)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
36% identity, 97% coverage: 1:315/326 of query aligns to 1:318/332 of 4xkjA
- active site: S102 (= S99), R234 (= R231), D258 (= D255), E263 (= E260), H295 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y98), V106 (= V103), G152 (= G149), G154 (= G151), R155 (≠ K152), I156 (= I153), D175 (= D172), I176 (= I173), R179 (≠ N176), H204 (= H201), V205 (= V202), P206 (= P203), T211 (≠ N208), A232 (≠ T229), R234 (= R231), H295 (= H292), G297 (≠ A294), F298 (= F295)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
39% identity, 77% coverage: 68:318/326 of query aligns to 65:320/334 of 3kb6B
- active site: S97 (= S99), R231 (= R231), D255 (= D255), E260 (= E260), H294 (= H292)
- binding lactic acid: S72 (≠ T75), V73 (≠ I76), G74 (= G77), Y96 (= Y98), R231 (= R231), H294 (= H292)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ I76), Y96 (= Y98), V101 (= V103), G150 (= G151), R151 (≠ K152), I152 (= I153), D171 (= D172), V172 (≠ I173), P203 (= P203), T229 (= T229), A230 (= A230), R231 (= R231), H294 (= H292), A296 (= A294), Y297 (≠ F295)
Sites not aligning to the query:
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
32% identity, 97% coverage: 1:315/326 of query aligns to 3:321/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V103), G154 (= G151), N155 (≠ K152), I156 (= I153), D176 (= D172), I177 (= I173), I178 (≠ N174), T208 (≠ V202), P209 (= P203), T214 (≠ N208), V235 (≠ T229), H298 (= H292), A300 (= A294), W301 (≠ F295)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
30% identity, 100% coverage: 1:325/326 of query aligns to 1:328/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y98), I106 (≠ V103), V154 (≠ T150), G155 (= G151), H156 (≠ K152), I157 (= I153), Y175 (= Y171), D176 (= D172), H205 (= H201), T206 (≠ V202), P207 (= P203), A233 (≠ T229), A234 (= A230), D259 (= D255), H295 (= H292), A297 (= A294)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
30% identity, 94% coverage: 2:306/326 of query aligns to 2:311/331 of 2yq5C
- active site: S102 (= S99), R236 (= R231), D260 (= D255), E265 (= E260), H297 (= H292)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y98), I106 (≠ V103), V155 (≠ T150), G156 (= G151), H157 (≠ K152), I158 (= I153), Y176 (= Y171), D177 (= D172), V178 (≠ I173), H206 (= H201), T207 (≠ V202), P208 (= P203), A235 (= A230), R236 (= R231), H297 (= H292), F300 (= F295)
6cdfA Human ctbp1 (28-378) (see paper)
34% identity, 74% coverage: 69:308/326 of query aligns to 64:307/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V103), G157 (= G149), R160 (≠ K152), V161 (≠ I153), Y179 (= Y171), D180 (= D172), P181 (≠ I173), Y182 (≠ N174), H212 (= H201), C213 (≠ V202), N219 (= N208), T240 (= T229), A241 (= A230), R242 (= R231), H291 (= H292), W294 (≠ F295)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
34% identity, 74% coverage: 69:308/326 of query aligns to 63:306/332 of 6v89A
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
34% identity, 74% coverage: 69:308/326 of query aligns to 63:306/328 of 4u6sA
- active site: S99 (= S99), R241 (= R231), D265 (= D255), E270 (= E260), H290 (= H292)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V103), G156 (= G149), G158 (= G151), R159 (≠ K152), V160 (≠ I153), Y178 (= Y171), D179 (= D172), P180 (≠ I173), Y181 (vs. gap), H211 (= H201), C212 (≠ V202), G213 (≠ P203), N218 (= N208), T239 (= T229), A240 (= A230), R241 (= R231), H290 (= H292), W293 (≠ F295)
- binding 3-phenylpyruvic acid: I73 (vs. gap), G74 (vs. gap), S75 (vs. gap), G76 (= G77), R241 (= R231), W293 (≠ F295), M302 (= M304)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
34% identity, 74% coverage: 69:308/326 of query aligns to 63:306/328 of 4u6qA
- active site: S99 (= S99), R241 (= R231), D265 (= D255), E270 (= E260), H290 (= H292)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: I73 (vs. gap), G74 (vs. gap), S75 (vs. gap), G76 (= G77), R241 (= R231), H290 (= H292), W293 (≠ F295), M302 (= M304)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (vs. gap), T103 (≠ V103), G156 (= G149), R159 (≠ K152), V160 (≠ I153), Y178 (= Y171), D179 (= D172), P180 (≠ I173), Y181 (vs. gap), H211 (= H201), C212 (≠ V202), G213 (≠ P203), N218 (= N208), T239 (= T229), A240 (= A230), R241 (= R231), H290 (= H292), W293 (≠ F295)
Sites not aligning to the query:
4lceA Ctbp1 in complex with substrate mtob (see paper)
34% identity, 74% coverage: 69:308/326 of query aligns to 62:305/327 of 4lceA
- active site: S98 (= S99), R240 (= R231), D264 (= D255), E269 (= E260), H289 (= H292)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (vs. gap), G73 (vs. gap), S74 (vs. gap), G75 (= G77), R240 (= R231), H289 (= H292), W292 (≠ F295)
- binding nicotinamide-adenine-dinucleotide: S74 (vs. gap), T102 (≠ V103), G155 (= G149), G157 (= G151), R158 (≠ K152), V159 (≠ I153), Y177 (= Y171), D178 (= D172), P179 (≠ I173), Y180 (vs. gap), H210 (= H201), C211 (≠ V202), N214 (≠ A205), N217 (= N208), T238 (= T229), A239 (= A230), R240 (= R231), W292 (≠ F295)
Query Sequence
>WP_010964851.1 NCBI__GCF_000008765.1:WP_010964851.1
MKILVYNHRADETEYFQKFKEKYNVDLMLTDKTPTIETADFAKGFDCISIITTPINAALI
KKFNDVGVKFISTRTIGYDHIDIKKAKELRIGVGNVTYSPRSVADYTVMMILMATRKVKA
IMQNSYVQDYSLEGIQGKELHNLTVGVIGTGKIGRTVIKNLKGFECNIIAYDINENEEVK
AHAKYVKLEELLMSSDVITVHVPGAEDNYHLINKNSISKMKDGVFIINTARGSIINTYDF
IDAVEKGKIGGAALDVIENETNLYYKNLKGEVLGNRELAVLKSYPNVIITPHTAFYTDQA
VSDMVENSILSCIAFYEGKENPWKVL
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