SitesBLAST
Comparing Ga0059261_0219 FitnessBrowser__Korea:Ga0059261_0219 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)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
53% identity, 97% coverage: 1:327/336 of query aligns to 1:326/330 of 4cukA
- active site: S101 (= S101), R234 (= R235), D258 (= D259), E263 (= E264), H295 (= H296)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y100), G153 (= G153), K154 (= K154), I155 (= I155), F173 (≠ S174), D174 (= D175), P175 (≠ V176), H204 (= H205), C205 (= C206), P206 (= P207), N211 (≠ T212), T232 (= T233), Y260 (= Y261), H295 (= H296), A297 (= A298)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
53% identity, 96% coverage: 1:322/336 of query aligns to 8:328/336 of 5z20F
- active site: S108 (= S101), R241 (= R235), D265 (= D259), E270 (= E264), H302 (= H296)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y100), G160 (= G153), Q161 (≠ K154), I162 (= I155), Y180 (≠ S174), D181 (= D175), P182 (≠ V176), C212 (= C206), P213 (= P207), T218 (= T212), T239 (= T233), G240 (≠ S234), R241 (= R235), H302 (= H296), A304 (= A298)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
45% identity, 98% coverage: 2:329/336 of query aligns to 3:329/331 of 5z21B
- active site: S101 (= S101), R235 (= R235), D259 (= D259), E264 (= E264), H296 (= H296)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y100), I105 (≠ V105), G153 (= G153), K154 (= K154), I155 (= I155), D174 (= D175), L175 (≠ V176), P207 (= P207), T212 (= T212), T233 (= T233), G234 (≠ S234), R235 (= R235), H296 (= H296), Y299 (≠ F299)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
46% identity, 98% coverage: 2:329/336 of query aligns to 12:344/346 of 4zgsA
- active site: S111 (= S101), R244 (= R235), D268 (= D259), E273 (= E264), H311 (= H296)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y100), G163 (= G153), A164 (≠ K154), I165 (= I155), D184 (= D175), C215 (= C206), P216 (= P207), L218 (≠ T209), S220 (≠ V211), T221 (= T212), S243 (= S234), H311 (= H296), F314 (= F299)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
38% identity, 96% coverage: 1:323/336 of query aligns to 3:325/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V105), G154 (= G153), N155 (≠ K154), I156 (= I155), D176 (= D175), I177 (≠ V176), I178 (≠ V177), T208 (≠ C206), P209 (= P207), T214 (= T212), V235 (≠ T233), H298 (= H296), A300 (= A298), W301 (≠ F299)
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, 90% coverage: 2:305/336 of query aligns to 3:306/333 of P26297
- HI 156:157 (≠ KI 154:155) binding
- D176 (= D175) binding
- H206 (= H205) mutation to Q: Increase of activity.
- VP 207:208 (≠ CP 206:207) binding
- N213 (≠ T212) binding
- R236 (= R235) mutation to K: Decrease of activity.
- D260 (= D259) binding ; mutation to N: Decrease of activity.
- E265 (= E264) mutation to Q: Decrease of activity.
- H297 (= H296) mutation to Q: 90% loss of activity.
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
37% identity, 90% coverage: 2:305/336 of query aligns to 3:306/337 of 2dldA
- active site: S103 (= S101), R236 (= R235), D260 (= D259), E265 (= E264), H297 (= H296)
- binding 1,4-dihydronicotinamide adenine dinucleotide: T154 (= T152), G155 (= G153), H156 (≠ K154), I157 (= I155), D176 (= D175), I177 (≠ V176), V207 (≠ C206), P208 (= P207), N213 (≠ T212), C234 (≠ T233), S235 (= S234), H297 (= H296)
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)
37% identity, 90% coverage: 2:305/336 of query aligns to 3:306/337 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)
36% identity, 90% coverage: 2:305/336 of query aligns to 3:306/332 of 1j49A
- active site: S103 (= S101), R236 (= R235), D260 (= D259), E265 (= E264), H297 (= H296)
- binding nicotinamide-adenine-dinucleotide: Y102 (= Y100), I107 (≠ V105), G153 (= G151), G155 (= G153), I157 (= I155), Y175 (≠ S174), D176 (= D175), I177 (≠ V176), V207 (≠ C206), P208 (= P207), N213 (≠ T212), V234 (≠ T233), S235 (= S234), R236 (= R235), H297 (= H296), A299 (= A298), F300 (= F299)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
30% identity, 93% coverage: 1:313/336 of query aligns to 1:312/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V154 (≠ T152), G155 (= G153), H156 (≠ K154), I157 (= I155), Y175 (≠ S174), D176 (= D175), H205 (= H205), T206 (≠ C206), P207 (= P207), A233 (≠ T233), A234 (≠ S234), D259 (= D259), H295 (= H296), A297 (= A298)
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
30% identity, 98% coverage: 1:329/336 of query aligns to 1:328/330 of 1dxyA
- active site: S101 (= S101), R234 (= R235), D258 (= D259), E263 (= E264), H295 (= H296)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ A77), Y100 (= Y100), Y298 (≠ F299)
- binding nicotinamide-adenine-dinucleotide: Y100 (= Y100), G152 (= G151), G154 (= G153), H155 (≠ K154), I156 (= I155), Y174 (≠ S174), D175 (= D175), P176 (≠ V176), H204 (= H205), V205 (≠ C206), P206 (= P207), N211 (≠ T212), T232 (= T233), A233 (≠ S234), R234 (= R235), H295 (= H296), Y298 (≠ F299)
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
30% identity, 98% coverage: 1:329/336 of query aligns to 1:328/333 of P17584
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
34% identity, 94% coverage: 1:316/336 of query aligns to 1:315/332 of 4xkjA
- active site: S102 (= S101), R234 (= R235), D258 (= D259), E263 (= E264), H295 (= H296)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), V106 (= V105), G152 (= G151), G154 (= G153), R155 (≠ K154), I156 (= I155), D175 (= D175), I176 (≠ V176), R179 (≠ D179), H204 (= H205), V205 (≠ C206), P206 (= P207), T211 (= T212), A232 (≠ T233), R234 (= R235), H295 (= H296), G297 (≠ A298), F298 (= F299)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
34% identity, 85% coverage: 32:317/336 of query aligns to 36:315/334 of 3kb6B
- active site: S97 (= S101), R231 (= R235), D255 (= D259), E260 (= E264), H294 (= H296)
- binding lactic acid: F49 (= F51), S72 (≠ C76), V73 (≠ A77), G74 (= G78), Y96 (= Y100), R231 (= R235), H294 (= H296)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A77), Y96 (= Y100), V101 (= V105), G150 (= G153), R151 (≠ K154), I152 (= I155), D171 (= D175), V172 (= V176), P203 (= P207), T229 (= T233), A230 (≠ S234), R231 (= R235), H294 (= H296), A296 (= A298), Y297 (≠ F299)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
31% identity, 96% coverage: 2:323/336 of query aligns to 2:325/331 of 2yq5C
- active site: S102 (= S101), R236 (= R235), D260 (= D259), E265 (= E264), H297 (= H296)
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V155 (≠ T152), G156 (= G153), H157 (≠ K154), I158 (= I155), Y176 (≠ S174), D177 (= D175), V178 (= V176), H206 (= H205), T207 (≠ C206), P208 (= P207), A235 (≠ S234), R236 (= R235), H297 (= H296), F300 (= F299)
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, 76% coverage: 78:332/336 of query aligns to 79:319/533 of O43175
- R135 (≠ L134) 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 154:155) binding
- D175 (= D175) binding
- T207 (≠ C206) binding
- CAR 234:236 (≠ TSR 233:235) binding
- D260 (= D259) binding
- V261 (= V260) 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 296:299) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 78 binding
- 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
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
34% identity, 56% coverage: 78:264/336 of query aligns to 71:257/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G153), I148 (= I155), Y166 (≠ S174), D167 (= D175), P168 (≠ V176), I169 (≠ V177), I170 (≠ T178), H198 (= H205), T199 (≠ C206), L208 (= L215), R228 (= R235)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
34% identity, 56% coverage: 78:264/336 of query aligns to 74:260/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
34% identity, 56% coverage: 78:264/336 of query aligns to 74:260/303 of 6plgA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
34% identity, 56% coverage: 78:264/336 of query aligns to 73:259/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ S101), A100 (≠ V105), R149 (≠ K154), I150 (= I155), Y168 (≠ S174), D169 (= D175), P170 (≠ V176), I171 (≠ V177), H200 (= H205), T201 (≠ C206), P202 (= P207), T207 (= T212), C228 (≠ T233), A229 (≠ S234), R230 (= R235)
Sites not aligning to the query:
Query Sequence
>Ga0059261_0219 FitnessBrowser__Korea:Ga0059261_0219
MRVAVFGTKGYDRRFLSEANAAHAHELIFLEPRLDLSTAPLAAGCAAVCVFVNDCVDARV
LEALAGSGVRLVALRCAGFNNVDLAAAERLGIDVVRVPAYSPHAVAEFTIGLMLAVDRHI
PRAWARVRDNNFALDGLIGRNLHGRMVGVIGTGKIGALVARSLRAGFGCDVLASDVVTDP
ELERVGVRYVPRATLLEQAEIVTLHCPLTPVTRHLIDAAAISRAREGLLIVNTSRGALID
TAALIDGLKSRKIGGVALDVYEQEADLFFEDLSNEIVGDDVFQRLLTFPNVLVTGHQAFL
TEEALTAIAETTLASISDAEAGRELANRVGTERVAG
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