SitesBLAST
Comparing 351103 FitnessBrowser__Btheta:351103 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)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
57% identity, 99% coverage: 5:333/333 of query aligns to 4:331/331 of 5z21B
- active site: S101 (= S103), R235 (= R237), D259 (= D261), E264 (= E266), H296 (= H298)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y102), I105 (≠ V107), G153 (= G155), K154 (= K156), I155 (= I157), D174 (= D176), L175 (= L177), P207 (= P209), T212 (= T214), T233 (= T235), G234 (= G236), R235 (= R237), H296 (= H298), Y299 (≠ F301)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
52% identity, 97% coverage: 5:326/333 of query aligns to 10:330/336 of 5z20F
- active site: S108 (= S103), R241 (= R237), D265 (= D261), E270 (= E266), H302 (= H298)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y102), G160 (= G155), Q161 (≠ K156), I162 (= I157), Y180 (= Y175), D181 (= D176), P182 (≠ L177), C212 (= C208), P213 (= P209), T218 (= T214), T239 (= T235), G240 (= G236), R241 (= R237), H302 (= H298), A304 (= A300)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
52% identity, 95% coverage: 5:321/333 of query aligns to 3:318/330 of 4cukA
- active site: S101 (= S103), R234 (= R237), D258 (= D261), E263 (= E266), H295 (= H298)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y102), G153 (= G155), K154 (= K156), I155 (= I157), F173 (≠ Y175), D174 (= D176), P175 (≠ L177), H204 (= H207), C205 (= C208), P206 (= P209), N211 (≠ T214), T232 (= T235), Y260 (= Y263), H295 (= H298), A297 (= A300)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
47% identity, 95% coverage: 5:321/333 of query aligns to 5:321/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V107), G154 (= G155), N155 (≠ K156), I156 (= I157), D176 (= D176), I177 (≠ L177), I178 (≠ Y178), T208 (≠ C208), P209 (= P209), T214 (= T214), V235 (≠ T235), H298 (= H298), A300 (= A300), W301 (≠ F301)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
50% identity, 91% coverage: 31:332/333 of query aligns to 39:345/346 of 4zgsA
- active site: S111 (= S103), R244 (= R237), D268 (= D261), E273 (= E266), H311 (= H298)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y102), G163 (= G155), A164 (≠ K156), I165 (= I157), D184 (= D176), C215 (= C208), P216 (= P209), L218 (≠ T211), S220 (≠ A213), T221 (= T214), S243 (≠ G236), H311 (= H298), F314 (= F301)
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)
34% identity, 95% coverage: 17:332/333 of query aligns to 19:331/333 of P26297
- HI 156:157 (≠ KI 156:157) binding
- D176 (= D176) binding
- H206 (= H207) mutation to Q: Increase of activity.
- VP 207:208 (≠ CP 208:209) binding
- N213 (≠ T214) binding
- R236 (= R237) mutation to K: Decrease of activity.
- D260 (= D261) binding ; mutation to N: Decrease of activity.
- E265 (= E266) mutation to Q: Decrease of activity.
- H297 (= H298) mutation to Q: 90% loss of activity.
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
34% identity, 94% coverage: 14:326/333 of query aligns to 12:326/337 of 2dldA
- active site: S103 (= S103), R236 (= R237), D260 (= D261), E265 (= E266), H297 (= H298)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T154), G155 (= G155), H156 (≠ K156), I157 (= I157), D176 (= D176), I177 (≠ L177), V207 (≠ C208), P208 (= P209), N213 (≠ T214), C234 (≠ T235), S235 (≠ G236), H297 (= H298)
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)
34% identity, 94% coverage: 14:326/333 of query aligns to 12:326/337 of P30901
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1j49A Insights into domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from lactobacillus bulgaricus (see paper)
33% identity, 95% coverage: 17:332/333 of query aligns to 19:331/332 of 1j49A
- active site: S103 (= S103), R236 (= R237), D260 (= D261), E265 (= E266), H297 (= H298)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y102), I107 (≠ V107), G153 (= G153), G155 (= G155), I157 (= I157), Y175 (= Y175), D176 (= D176), I177 (≠ L177), V207 (≠ C208), P208 (= P209), N213 (≠ T214), V234 (≠ T235), S235 (≠ G236), R236 (= R237), H297 (= H298), A299 (= A300), F300 (= F301)
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
32% identity, 94% coverage: 18:331/333 of query aligns to 16:328/330 of 1dxyA
- active site: S101 (= S103), R234 (= R237), D258 (= D261), E263 (= E266), H295 (= H298)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ A79), Y100 (= Y102), Y298 (≠ F301)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y102), G152 (= G153), G154 (= G155), H155 (≠ K156), I156 (= I157), Y174 (= Y175), D175 (= D176), P176 (≠ L177), H204 (= H207), V205 (≠ C208), P206 (= P209), N211 (≠ T214), T232 (= T235), A233 (≠ G236), R234 (= R237), H295 (= H298), Y298 (≠ F301)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
37% identity, 83% coverage: 48:323/333 of query aligns to 44:319/334 of 3kb6B
- active site: S97 (= S103), R231 (= R237), D255 (= D261), E260 (= E266), H294 (= H298)
- binding lactic acid: F49 (= F53), S72 (≠ C78), V73 (≠ A79), G74 (= G80), Y96 (= Y102), R231 (= R237), H294 (= H298)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A79), Y96 (= Y102), V101 (= V107), G150 (= G155), R151 (≠ K156), I152 (= I157), D171 (= D176), V172 (≠ L177), P203 (= P209), T229 (= T235), A230 (≠ G236), R231 (= R237), H294 (= H298), A296 (= A300), Y297 (≠ F301)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
32% identity, 94% coverage: 18:331/333 of query aligns to 16:328/333 of P17584
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
34% identity, 94% coverage: 5:317/333 of query aligns to 3:314/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y102), I106 (≠ V107), V154 (≠ T154), G155 (= G155), H156 (≠ K156), I157 (= I157), Y175 (= Y175), D176 (= D176), H205 (= H207), T206 (≠ C208), P207 (= P209), A233 (≠ T235), A234 (≠ G236), D259 (= D261), H295 (= H298), A297 (= A300)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
32% identity, 94% coverage: 5:317/333 of query aligns to 3:316/331 of 2yq5C
- active site: S102 (= S103), R236 (= R237), D260 (= D261), E265 (= E266), H297 (= H298)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y102), I106 (≠ V107), V155 (≠ T154), G156 (= G155), H157 (≠ K156), I158 (= I157), Y176 (= Y175), D177 (= D176), V178 (≠ L177), H206 (= H207), T207 (≠ C208), P208 (= P209), A235 (≠ G236), R236 (= R237), H297 (= H298), F300 (= F301)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
30% identity, 94% coverage: 5:318/333 of query aligns to 3:315/332 of 4xkjA
- active site: S102 (= S103), R234 (= R237), D258 (= D261), E263 (= E266), H295 (= H298)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y102), V106 (= V107), G152 (= G153), G154 (= G155), R155 (≠ K156), I156 (= I157), D175 (= D176), I176 (≠ L177), R179 (≠ D180), H204 (= H207), V205 (≠ C208), P206 (= P209), T211 (= T214), A232 (≠ T235), R234 (= R237), H295 (= H298), G297 (≠ A300), F298 (= F301)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 83% coverage: 41:318/333 of query aligns to 36:298/304 of 1wwkA
- active site: S96 (= S103), R230 (= R237), D254 (= D261), E259 (= E266), H278 (= H298)
- binding nicotinamide-adenine-dinucleotide: V100 (= V107), G146 (= G153), F147 (≠ T154), G148 (= G155), R149 (≠ K156), I150 (= I157), Y168 (= Y175), D169 (= D176), P170 (≠ L177), V201 (≠ C208), P202 (= P209), T207 (= T214), T228 (= T235), S229 (≠ G236), D254 (= D261), H278 (= H298), G280 (≠ A300)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
31% identity, 82% coverage: 44:315/333 of query aligns to 43:308/334 of 5aovA
- active site: L100 (≠ S103), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H298)
- binding glyoxylic acid: M52 (≠ F53), L53 (≠ V54), L53 (≠ V54), Y74 (≠ R77), A75 (≠ C78), V76 (≠ A79), G77 (= G80), R241 (= R237), H288 (= H298)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A79), T104 (≠ V107), F158 (≠ T154), G159 (= G155), R160 (≠ K156), I161 (= I157), S180 (≠ D176), R181 (≠ L177), A211 (≠ H207), V212 (≠ C208), P213 (= P209), T218 (= T214), I239 (≠ T235), A240 (≠ G236), R241 (= R237), H288 (= H298), G290 (vs. gap)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
31% identity, 81% coverage: 36:306/333 of query aligns to 25:277/292 of 6plfB
- binding 4-{(1S)-1-[(5-chloro-6-{[(5S)-2-oxo-1,3-oxazolidin-5-yl]methoxy}-1H-indole-2-carbonyl)amino]-2-hydroxyethyl}benzoic acid: R141 (≠ K156), Y160 (= Y175), D161 (= D176), P162 (≠ L177), I164 (≠ P179), L179 (= L194), T193 (≠ C208), P194 (= P209), S198 (≠ A213), L202 (= L217)
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
32% identity, 74% coverage: 60:306/333 of query aligns to 55:285/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ S103), A100 (≠ V107), R149 (≠ K156), I150 (= I157), Y168 (= Y175), D169 (= D176), P170 (≠ L177), I171 (≠ Y178), H200 (= H207), T201 (≠ C208), P202 (= P209), T207 (= T214), C228 (≠ T235), A229 (≠ G236), R230 (= R237), H277 (= H298), G279 (≠ A300)
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
30% identity, 80% coverage: 60:327/333 of query aligns to 61:312/533 of O43175
- T78 (≠ A79) binding
- R135 (≠ L136) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ KI 156:157) binding
- D175 (= D176) binding
- T207 (≠ C208) binding
- CAR 234:236 (≠ TGR 235:237) binding
- D260 (= D261) binding
- V261 (= V262) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HQAF 298:301) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
Query Sequence
>351103 FitnessBrowser__Btheta:351103
MAYTIAFFGTKPYDEASFNDKNKEFRFEFRYYKGHLNKNNVLLTQGVDAVCIFVNDTADA
EVIHAMAANGVKLLALRCAGFNNVDLNAAATAGITVVRVPAYSPYAVAEYTVALMLSLNR
KIPRASWRTKDGNFSLHGLMGFDMHGKTAGIIGTGKIAKILIHILKGFGMNILAYDLYPD
YNFAREEQIVYTSLDELYHSSDIISLHCPLTEATKYLINDYSISKMKDGVMIINTGRGQL
IHTNALIEGLKNKKIGSAGLDVYEEESEYFYEDQSDRIIDDDVLARLLSFNNVIVTSHQA
FFTREAMGNIAMTTLQNIKDFINHKPLLNEVKR
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