SitesBLAST
Comparing PP_0762 PP_0762 Glycerate dehydrogenase 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)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
33% identity, 86% coverage: 41:315/321 of query aligns to 37:315/334 of 5aovA
- active site: L100 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H288 (= H288)
- binding glyoxylic acid: M52 (≠ N56), L53 (vs. gap), L53 (vs. gap), Y74 (≠ A77), A75 (= A78), V76 (≠ T79), G77 (= G80), R241 (= R238), H288 (= H288)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T79), T104 (≠ V107), F158 (≠ H160), G159 (= G161), R160 (≠ E162), I161 (≠ L163), S180 (= S180), R181 (≠ G181), A211 (≠ H208), V212 (≠ C209), P213 (= P210), T218 (= T215), I239 (≠ T236), A240 (= A237), R241 (= R238), H288 (= H288), G290 (≠ A290)
P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 89% coverage: 22:306/321 of query aligns to 69:362/466 of P87228
- S87 (≠ P40) modified: Phosphoserine
- S258 (≠ N212) modified: Phosphoserine
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
32% identity, 82% coverage: 53:314/321 of query aligns to 46:304/304 of 1wwkA
- active site: S96 (≠ G103), R230 (= R238), D254 (= D262), E259 (= E267), H278 (= H288)
- binding nicotinamide-adenine-dinucleotide: V100 (= V107), G146 (= G159), F147 (≠ H160), G148 (= G161), R149 (≠ E162), I150 (≠ L163), Y168 (≠ G181), D169 (≠ Q182), P170 (≠ I183), V201 (≠ C209), P202 (= P210), T207 (= T215), T228 (= T236), S229 (≠ A237), D254 (= D262), H278 (= H288), G280 (≠ A290)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
34% identity, 89% coverage: 30:315/321 of query aligns to 21:305/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
34% identity, 89% coverage: 30:315/321 of query aligns to 20:304/526 of 3dc2A
Sites not aligning to the query:
6p2iA Acyclic imino acid reductase (bsp5) in complex with NADPH and d-arg (see paper)
30% identity, 92% coverage: 27:320/321 of query aligns to 21:306/307 of 6p2iA
- binding d-arginine: E51 (≠ N56), T73 (≠ A78), T74 (= T79), S75 (≠ G80), Y97 (= Y102), W277 (= W291)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S98 (≠ G103), V102 (= V107), G149 (= G159), I150 (≠ H160), G151 (= G161), Q152 (≠ E162), I153 (≠ L163), N172 (≠ Q182), K173 (≠ I183), S174 (≠ P184), R176 (= R186), H199 (= H208), I200 (≠ C209), P201 (= P210), T206 (= T215), T227 (= T236), C228 (≠ A237), W277 (= W291)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 48:304/331 of 1hl3A
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V107), G158 (= G161), R159 (≠ E162), V160 (≠ L163), D179 (≠ S180), Y181 (≠ Q182), H211 (= H208), C212 (= C209), G213 (≠ P210), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), D265 (= D262), H290 (= H288)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 48:304/331 of 1hkuA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T79), T103 (≠ V107), G156 (= G159), G158 (= G161), R159 (≠ E162), V160 (≠ L163), Y178 (vs. gap), D179 (≠ S180), P180 (≠ G181), Y181 (≠ Q182), C212 (= C209), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), H290 (= H288), W293 (= W291)
Sites not aligning to the query:
4lceA Ctbp1 in complex with substrate mtob (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 47:303/327 of 4lceA
- active site: S98 (≠ G103), R240 (= R238), D264 (= D262), E269 (= E267), H289 (= H288)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ V76), G73 (≠ A78), S74 (≠ T79), G75 (= G80), R240 (= R238), H289 (= H288), W292 (= W291)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), G155 (= G159), G157 (= G161), R158 (≠ E162), V159 (≠ L163), Y177 (vs. gap), D178 (≠ S180), P179 (≠ G181), Y180 (≠ Q182), H210 (= H208), C211 (= C209), N214 (= N212), N217 (≠ T215), T238 (= T236), A239 (= A237), R240 (= R238), W292 (= W291)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 48:304/328 of 4u6sA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V107), G156 (= G159), G158 (= G161), R159 (≠ E162), V160 (≠ L163), Y178 (vs. gap), D179 (≠ S180), P180 (≠ G181), Y181 (≠ Q182), H211 (= H208), C212 (= C209), G213 (≠ P210), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), H290 (= H288), W293 (= W291)
- binding 3-phenylpyruvic acid: Y51 (≠ S55), H52 (≠ N56), I73 (≠ A77), G74 (≠ A78), S75 (≠ T79), G76 (= G80), R241 (= R238), W293 (= W291), M302 (≠ S296)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 48:304/328 of 4u6qA
- active site: S99 (≠ G103), R241 (= R238), D265 (= D262), E270 (= E267), H290 (= H288)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ S55), I73 (≠ A77), G74 (≠ A78), S75 (≠ T79), G76 (= G80), R241 (= R238), H290 (= H288), W293 (= W291), M302 (≠ S296)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T79), T103 (≠ V107), G156 (= G159), R159 (≠ E162), V160 (≠ L163), Y178 (vs. gap), D179 (≠ S180), P180 (≠ G181), Y181 (≠ Q182), H211 (= H208), C212 (= C209), G213 (≠ P210), N218 (≠ T215), T239 (= T236), A240 (= A237), R241 (= R238), H290 (= H288), W293 (= W291)
6cdfA Human ctbp1 (28-378) (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 49:305/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V107), G157 (= G159), R160 (≠ E162), V161 (≠ L163), Y179 (vs. gap), D180 (≠ S180), P181 (≠ G181), Y182 (≠ Q182), H212 (= H208), C213 (= C209), N219 (≠ T215), T240 (= T236), A241 (= A237), R242 (= R238), H291 (= H288), W294 (= W291)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
36% identity, 77% coverage: 52:298/321 of query aligns to 48:304/332 of 6v89A
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
34% identity, 80% coverage: 52:307/321 of query aligns to 47:320/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), G155 (= G159), G157 (= G161), R158 (≠ E162), T159 (≠ L163), D178 (≠ Q182), P179 (= P184), Y180 (≠ G185), H210 (= H208), C211 (= C209), N212 (≠ P210), A238 (≠ T236), R240 (= R238), H289 (= H288), A291 (= A290), W292 (= W291)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
34% identity, 80% coverage: 52:307/321 of query aligns to 47:320/330 of 4lcjA
- active site: A98 (≠ G103), R240 (= R238), D264 (= D262), E269 (= E267), H289 (= H288)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ S55), H51 (≠ N56), I72 (≠ A77), G73 (≠ A78), S74 (≠ T79), G75 (= G80), R240 (= R238), H289 (= H288), W292 (= W291)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T79), T102 (≠ V107), I154 (≠ L158), G155 (= G159), G157 (= G161), R158 (≠ E162), T159 (≠ L163), D178 (≠ Q182), Y180 (≠ G185), H210 (= H208), C211 (= C209), N212 (≠ P210), N214 (= N212), N217 (≠ T215), A238 (≠ T236), A239 (= A237), R240 (= R238), H289 (= H288), W292 (= W291)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
33% identity, 84% coverage: 52:320/321 of query aligns to 79:371/445 of P56545
Q9Z2F5 C-terminal-binding protein 1; CtBP1; 50 kDa BFA-dependent ADP-ribosylation substrate; BARS-50; C-terminal-binding protein 3; CtBP3; EC 1.1.1.- from Rattus norvegicus (Rat) (see 3 papers)
36% identity, 77% coverage: 52:298/321 of query aligns to 62:318/430 of Q9Z2F5
- S89 (≠ T79) binding
- IGLGRV 169:174 (≠ LGHGEL 158:163) binding
- G172 (= G161) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ S180) binding
- 226:232 (vs. 209:215, 71% identical) binding
- TAR 253:255 (= TAR 236:238) binding
- D279 (= D262) binding
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
- 55 V→R: Strongly reduces interaction with E1A.
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
34% identity, 81% coverage: 41:300/321 of query aligns to 41:300/406 of 2p9eA
- active site: N104 (≠ G103), R236 (= R238), D260 (= D262), E265 (= E267), H288 (= H288)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G161), H157 (≠ E162), I158 (≠ L163), Y176 (≠ G181), D177 (≠ Q182), I178 (= I183), H206 (= H208), V207 (≠ C209), P208 (= P210), S212 (≠ H214), A234 (≠ T236), S235 (≠ A237), R236 (= R238), H288 (= H288), G290 (≠ A290)
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
33% identity, 86% coverage: 24:298/321 of query aligns to 43:329/440 of Q13363
- A52 (≠ E33) mutation to E: Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3.
- V66 (≠ L47) mutation to R: Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3.
- C134 (≠ A113) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ A117) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (≠ T120) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ TR 120:121) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V129) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ C141) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ E149) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G159) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G161) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-186.; mutation to V: Strongly reduces E1A binding; when associated with V-181 and A-204.
- G186 (= G164) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ S180) mutation to A: Strongly reduces E1A binding; when associated with V-181 and V-183.; mutation to L: Reduced proteolytic processing mediated by CAPN3.
- R266 (= R238) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D262) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E267) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H288) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295.
Sites not aligning to the query:
- 375:376 Cleavage; by CAPN1
- 387:388 Cleavage; by CAPN1
- 409:410 Cleavage; by CAPN1 and CAPN3
- 422 modified: Phosphoserine; by HIPK2; S→A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance.
- 428 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
35% identity, 72% coverage: 38:269/321 of query aligns to 33:263/305 of 6plfA
Query Sequence
>PP_0762 PP_0762 Glycerate dehydrogenase
MPSPRRAVFLDHQSLDLGDLDLSPLKQQFDQFELFAATRPEQVAERLQGAVAVVSNKVML
DAATLAANPQLKLILVAATGTNNVDLAAARAQGITVCNCQGYGTPSVAQHTLALLLALAT
RLCDYNQAVADGQWAKASQFCLLDFPIVELEGKTLGLLGHGELGGAVARLAEAFGMRVLS
GQIPGRPERADRLPLDELLPQVDALTLHCPLNEHTRHMLGARELALLKPNALVVNTARGG
LIDEQALADALRGGHLGGAATDVLSVEPPVNGNPLLEPGIPRLIITPHSAWGAVESRQRI
VGQLSENAQAFFAGQPRRVVS
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