SitesBLAST
Comparing BPHYT_RS03835 FitnessBrowser__BFirm:BPHYT_RS03835 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)
71% identity, 99% coverage: 1:330/332 of query aligns to 8:336/336 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 (≠ M154), I162 (= I155), Y180 (= Y173), D181 (= D174), P182 (= P175), C212 (= C206), P213 (= P207), T218 (= T212), T239 (= T233), G240 (= G234), R241 (= R235), H302 (= H296), A304 (= A298)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
52% identity, 97% coverage: 1:322/332 of query aligns to 1:321/330 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 (≠ M154), I155 (= I155), F173 (≠ Y173), D174 (= D174), P175 (= P175), H204 (= H205), C205 (= C206), P206 (= P207), N211 (≠ T212), T232 (= T233), Y260 (= Y261), H295 (= H296), A297 (= A298)
5z21B The ternary structure of d-lactate dehydrogenase from fusobacterium nucleatum with nadh and oxamate (see paper)
49% identity, 97% coverage: 2:324/332 of query aligns to 3:324/331 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 (≠ M154), I155 (= I155), D174 (= D174), L175 (vs. gap), P207 (= P207), T212 (= T212), T233 (= T233), G234 (= G234), R235 (= R235), H296 (= H296), Y299 (≠ F299)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
49% identity, 97% coverage: 2:324/332 of query aligns to 12:339/346 of 4zgsA
- active site: S111 (= S101), R244 (= R235), D268 (= D259), E273 (= E264), H311 (= H296)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y100), G163 (= G153), A164 (≠ M154), I165 (= I155), D184 (= D174), C215 (= C206), P216 (= P207), L218 (≠ V209), S220 (≠ D211), T221 (= T212), S243 (≠ G234), H311 (= H296), F314 (= F299)
8grvA Dictyostelium discoideum lactate dehydrogenase (dicldha)with NAD
41% identity, 100% coverage: 1:331/332 of query aligns to 3:335/336 of 8grvA
- binding nicotinamide-adenine-dinucleotide: V106 (= V105), G154 (= G153), N155 (≠ M154), I156 (= I155), D176 (= D174), I177 (≠ P175), I178 (≠ G176), 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, 98% coverage: 2:327/332 of query aligns to 3:332/333 of P26297
- HI 156:157 (≠ MI 154:155) binding
- D176 (= D174) 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.
1j49A Insights into domain closure, substrate specificity and catalysis of d-lactate dehydrogenase from lactobacillus bulgaricus (see paper)
35% identity, 98% coverage: 2:327/332 of query aligns to 3:332/332 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 (= Y173), D176 (= D174), I177 (≠ P175), V207 (≠ C206), P208 (= P207), N213 (≠ T212), V234 (≠ T233), S235 (≠ G234), R236 (= R235), H297 (= H296), A299 (= A298), F300 (= F299)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
39% identity, 83% coverage: 46:322/332 of query aligns to 44:320/334 of 3kb6B
- active site: S97 (= S101), R231 (= R235), D255 (= D259), E260 (= E264), H294 (= H296)
- binding lactic acid: F49 (= F51), S72 (= S76), V73 (≠ A77), G74 (= G78), Y96 (= Y100), R231 (= R235), H294 (= H296)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ A77), Y96 (= Y100), V101 (= V105), G150 (= G153), R151 (≠ M154), I152 (= I155), D171 (= D174), V172 (≠ P175), P203 (= P207), T229 (= T233), A230 (≠ G234), R231 (= R235), H294 (= H296), A296 (= A298), Y297 (≠ F299)
2dldA D-lactate dehydrogenase complexed with nadh and oxamate
35% identity, 95% coverage: 2:315/332 of query aligns to 3:316/337 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 (≠ M154), I157 (= I155), D176 (= D174), I177 (≠ P175), V207 (≠ C206), P208 (= P207), N213 (≠ T212), C234 (≠ T233), S235 (≠ G234), 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)
35% identity, 95% coverage: 2:315/332 of query aligns to 3:316/337 of P30901
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P17584 D-2-hydroxyisocaproate dehydrogenase; D-HICDH; EC 1.1.1.- from Lacticaseibacillus paracasei (Lactobacillus paracasei) (see paper)
33% identity, 100% coverage: 1:332/332 of query aligns to 1:332/333 of P17584
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
34% identity, 95% coverage: 1:316/332 of query aligns to 1:315/330 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 (≠ M154), I156 (= I155), Y174 (= Y173), D175 (= D174), P176 (= P175), H204 (= H205), V205 (≠ C206), P206 (= P207), N211 (≠ T212), T232 (= T233), A233 (≠ G234), R234 (= R235), H295 (= H296), Y298 (≠ F299)
4xkjA A novel d-lactate dehydrogenase from sporolactobacillus sp
36% identity, 96% coverage: 1:318/332 of query aligns to 1:317/332 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 (≠ M154), I156 (= I155), D175 (= D174), I176 (≠ P175), R179 (≠ P178), H204 (= H205), V205 (≠ C206), P206 (= P207), T211 (= T212), A232 (≠ T233), R234 (= R235), H295 (= H296), G297 (≠ A298), F298 (= F299)
4prlA Crystal structure of d-lactate dehydrogenase with NAD+ from lactobacillus jensenii (see paper)
33% identity, 97% coverage: 1:322/332 of query aligns to 1:321/330 of 4prlA
- binding nicotinamide-adenine-dinucleotide: Y101 (= Y100), I106 (≠ V105), V154 (≠ T152), G155 (= G153), H156 (≠ M154), I157 (= I155), Y175 (= Y173), D176 (= D174), H205 (= H205), T206 (≠ C206), P207 (= P207), A233 (≠ T233), A234 (≠ G234), D259 (= D259), H295 (= H296), A297 (= A298)
2yq5C Crystal structure of d-isomer specific 2-hydroxyacid dehydrogenase from lactobacillus delbrueckii ssp. Bulgaricus: NAD complexed form (see paper)
34% identity, 92% coverage: 26:329/332 of query aligns to 26:331/331 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 (≠ M154), I158 (= I155), Y176 (= Y173), D177 (= D174), V178 (≠ P175), H206 (= H205), T207 (≠ C206), P208 (= P207), A235 (≠ G234), R236 (= R235), H297 (= H296), F300 (= F299)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
33% identity, 83% coverage: 46:322/332 of query aligns to 47:314/334 of 5aovA
- active site: L100 (≠ S101), R241 (= R235), D265 (= D259), E270 (= E264), H288 (= H296)
- binding glyoxylic acid: M52 (≠ F51), L53 (≠ V52), L53 (≠ V52), Y74 (≠ R75), A75 (≠ S76), V76 (≠ A77), G77 (= G78), R241 (= R235), H288 (= H296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A77), T104 (≠ V105), F158 (≠ T152), G159 (= G153), R160 (≠ M154), I161 (= I155), S180 (≠ D174), R181 (≠ P175), A211 (≠ H205), V212 (≠ C206), P213 (= P207), T218 (= T212), I239 (≠ T233), A240 (≠ G234), R241 (= R235), H288 (= H296), G290 (≠ A298)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
41% identity, 71% coverage: 70:306/332 of query aligns to 65:288/304 of 1wwkA
- active site: S96 (= S101), R230 (= R235), D254 (= D259), E259 (= E264), H278 (= H296)
- binding nicotinamide-adenine-dinucleotide: V100 (= V105), G146 (= G151), F147 (≠ T152), G148 (= G153), R149 (≠ M154), I150 (= I155), Y168 (= Y173), D169 (= D174), P170 (= P175), V201 (≠ C206), P202 (= P207), T207 (= T212), T228 (= T233), S229 (≠ G234), D254 (= D259), H278 (= H296), G280 (≠ A298)
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
34% identity, 70% coverage: 78:310/332 of query aligns to 71:289/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G153), I148 (= I155), Y166 (= Y173), D167 (= D174), P168 (= P175), I169 (≠ G176), I170 (≠ K177), H198 (= H205), T199 (≠ C206), L208 (= L215), R228 (= R235)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
34% identity, 70% coverage: 78:310/332 of query aligns to 74:292/301 of 6rj5A
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
34% identity, 70% coverage: 78:310/332 of query aligns to 74:292/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I150), G147 (= G151), L148 (≠ T152), G149 (= G153), R150 (≠ M154), I151 (= I155), G152 (= G156), D170 (= D174), H201 (= H205), T202 (≠ C206), P203 (= P207)
Query Sequence
>BPHYT_RS03835 FitnessBrowser__BFirm:BPHYT_RS03835
MRMILFSSRQYDRDTFTEANATHRYELHCQESHLDSETAILAQGYDVVCPFVNDNVDAAV
LARLHAGGTRMIALRSAGFNHVDLAAAERLGITVARVPAYSPHAVAEHAVGLILALNRRL
PRAVARTREGDFSLHGLLGFDLHGKTVGVIGTGMIGRVFGRIMAGFGMQVLAYDPGKPAA
DLLALGARYVPLDALLAESDVVSLHCPLVPDTYHLINGPALAKMKRGAMLINTGRGGLVE
SNALIGALKDGQLGHLGLDVYEEESGLFFEDHSNLPLQDDVLARLLMFPNVIVTAHQAFF
TREAMNEIAQTTLDNVAAWQAGTPRNVVRAPA
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