SitesBLAST
Comparing 206855 MicrobesOnline__882:206855 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
35% identity, 90% coverage: 34:325/326 of query aligns to 35:329/334 of 5aovA
- active site: L100 (≠ G98), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H285)
- binding glyoxylic acid: M52 (≠ N51), L53 (vs. gap), L53 (vs. gap), Y74 (≠ L72), A75 (= A73), V76 (≠ T74), G77 (= G75), R241 (= R237), H288 (= H285)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T74), T104 (≠ V102), F158 (= F155), G159 (= G156), R160 (≠ N157), I161 (≠ T158), S180 (≠ A177), R181 (= R179), A211 (≠ H207), V212 (≠ C208), P213 (= P209), T218 (= T214), I239 (≠ T235), A240 (= A236), R241 (= R237), H288 (= H285), G290 (≠ A287)
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
40% identity, 78% coverage: 65:319/326 of query aligns to 75:336/336 of 5z20F
- active site: S108 (≠ G98), R241 (= R237), D265 (= D261), E270 (= E266), H302 (= H285)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y97), G160 (= G156), Q161 (≠ N157), I162 (≠ T158), Y180 (= Y176), D181 (≠ A177), P182 (= P178), C212 (= C208), P213 (= P209), T218 (= T214), T239 (= T235), G240 (≠ A236), R241 (= R237), H302 (= H285), A304 (= A287)
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
36% identity, 85% coverage: 36:311/326 of query aligns to 38:315/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), G155 (= G154), G157 (= G156), R158 (≠ N157), T159 (= T158), D178 (≠ A177), P179 (= P178), Y180 (≠ R179), H210 (= H207), C211 (= C208), N212 (≠ P209), A238 (≠ T235), R240 (= R237), H289 (= H285), A291 (= A287), W292 (= W288)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
36% identity, 85% coverage: 36:311/326 of query aligns to 38:315/330 of 4lcjA
- active site: A98 (≠ G98), R240 (= R237), D264 (= D261), E269 (= E266), H289 (= H285)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ T50), H51 (≠ N51), I72 (≠ L72), G73 (≠ A73), S74 (≠ T74), G75 (= G75), R240 (= R237), H289 (= H285), W292 (= W288)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), I154 (≠ V153), G155 (= G154), G157 (= G156), R158 (≠ N157), T159 (= T158), D178 (≠ A177), Y180 (≠ R179), H210 (= H207), C211 (= C208), N212 (≠ P209), N214 (≠ T211), N217 (≠ T214), A238 (≠ T235), A239 (= A236), R240 (= R237), H289 (= H285), W292 (= W288)
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
35% identity, 85% coverage: 36:311/326 of query aligns to 70:347/445 of P56545
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
35% identity, 88% coverage: 36:322/326 of query aligns to 39:331/331 of 1hl3A
- active site: S99 (≠ G98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V102), G158 (= G156), R159 (≠ N157), V160 (≠ T158), D179 (≠ A177), Y181 (≠ R179), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), D265 (= D261), H290 (= H285)
- binding : E39 (≠ D36), L331 (= L322)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
35% identity, 88% coverage: 36:322/326 of query aligns to 39:331/331 of 1hkuA
- active site: S99 (≠ G98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T74), T103 (≠ V102), G156 (= G154), G158 (= G156), R159 (≠ N157), V160 (≠ T158), Y178 (= Y176), D179 (≠ A177), P180 (= P178), Y181 (≠ R179), C212 (= C208), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H285), W293 (= W288), L331 (= L322)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
32% identity, 77% coverage: 60:311/326 of query aligns to 59:320/334 of 3kb6B
- active site: S97 (≠ G98), R231 (= R237), D255 (= D261), E260 (= E266), H294 (= H285)
- binding lactic acid: S72 (≠ A73), V73 (≠ T74), G74 (= G75), Y96 (= Y97), R231 (= R237), H294 (= H285)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ T74), Y96 (= Y97), V101 (= V102), G150 (= G156), R151 (≠ N157), I152 (≠ T158), D171 (≠ A177), V172 (≠ P178), P203 (= P209), T229 (= T235), A230 (= A236), R231 (= R237), H294 (= H285), A296 (= A287), Y297 (≠ W288)
Sites not aligning to the query:
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)
35% identity, 88% coverage: 36:322/326 of query aligns to 53:345/430 of Q9Z2F5
- V55 (≠ I38) mutation to R: Strongly reduces interaction with E1A.
- S89 (≠ T74) binding
- IGLGRV 169:174 (≠ VGFGNT 153:158) binding
- G172 (= G156) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ A177) binding
- 226:232 (vs. 208:214, 29% identical) binding
- TAR 253:255 (= TAR 235:237) binding
- D279 (= D261) binding
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
35% identity, 88% coverage: 36:322/326 of query aligns to 39:331/332 of 6v89A
6cdfA Human ctbp1 (28-378) (see paper)
35% identity, 88% coverage: 36:322/326 of query aligns to 40:332/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V102), G157 (= G154), R160 (≠ N157), V161 (≠ T158), Y179 (= Y176), D180 (≠ A177), P181 (= P178), Y182 (≠ R179), H212 (= H207), C213 (= C208), N219 (≠ T214), T240 (= T235), A241 (= A236), R242 (= R237), H291 (= H285), W294 (= W288)
6p2iA Acyclic imino acid reductase (bsp5) in complex with NADPH and d-arg (see paper)
33% identity, 97% coverage: 1:317/326 of query aligns to 1:306/307 of 6p2iA
- binding d-arginine: E51 (≠ N51), T73 (≠ A73), T74 (= T74), S75 (≠ G75), Y97 (= Y97), W277 (= W288)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: S98 (≠ G98), V102 (= V102), G149 (= G154), I150 (≠ F155), G151 (= G156), Q152 (≠ N157), I153 (≠ T158), N172 (≠ A177), K173 (≠ P178), S174 (≠ R179), R176 (= R181), H199 (= H207), I200 (≠ C208), P201 (= P209), T206 (= T214), T227 (= T235), C228 (≠ A236), W277 (= W288)
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
35% identity, 88% coverage: 36:322/326 of query aligns to 64:356/440 of Q13363
- V66 (≠ I38) mutation to R: Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3.
- C134 (≠ A108) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ E112) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R115) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (= RR 115:116) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ I124) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ F137) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ E144) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G154) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G156) 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 (= G159) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ A177) 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 (= R237) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D261) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E266) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H285) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295.
Sites not aligning to the query:
- 52 A→E: Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3.
- 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)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
35% identity, 85% coverage: 36:311/326 of query aligns to 39:316/328 of 4u6sA
- active site: S99 (≠ G98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V102), G156 (= G154), G158 (= G156), R159 (≠ N157), V160 (≠ T158), Y178 (= Y176), D179 (≠ A177), P180 (= P178), Y181 (≠ R179), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H285), W293 (= W288)
- binding 3-phenylpyruvic acid: Y51 (≠ T50), H52 (≠ N51), I73 (≠ L72), G74 (≠ A73), S75 (≠ T74), G76 (= G75), R241 (= R237), W293 (= W288), M302 (≠ L297)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
35% identity, 85% coverage: 36:311/326 of query aligns to 39:316/328 of 4u6qA
- active site: S99 (≠ G98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ T50), I73 (≠ L72), G74 (≠ A73), S75 (≠ T74), G76 (= G75), R241 (= R237), H290 (= H285), W293 (= W288), M302 (≠ L297)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T74), T103 (≠ V102), G156 (= G154), R159 (≠ N157), V160 (≠ T158), Y178 (= Y176), D179 (≠ A177), P180 (= P178), Y181 (≠ R179), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (≠ T214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H285), W293 (= W288)
4lceA Ctbp1 in complex with substrate mtob (see paper)
35% identity, 85% coverage: 36:311/326 of query aligns to 38:315/327 of 4lceA
- active site: S98 (≠ G98), R240 (= R237), D264 (= D261), E269 (= E266), H289 (= H285)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ V71), G73 (≠ A73), S74 (≠ T74), G75 (= G75), R240 (= R237), H289 (= H285), W292 (= W288)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), G155 (= G154), G157 (= G156), R158 (≠ N157), V159 (≠ T158), Y177 (= Y176), D178 (≠ A177), P179 (= P178), Y180 (≠ R179), H210 (= H207), C211 (= C208), N214 (≠ T211), N217 (≠ T214), T238 (= T235), A239 (= A236), R240 (= R237), W292 (= W288)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
33% identity, 87% coverage: 28:311/326 of query aligns to 24:304/304 of 1wwkA
- active site: S96 (≠ G98), R230 (= R237), D254 (= D261), E259 (= E266), H278 (= H285)
- binding nicotinamide-adenine-dinucleotide: V100 (= V102), G146 (= G154), F147 (= F155), G148 (= G156), R149 (≠ N157), I150 (≠ T158), Y168 (= Y176), D169 (≠ A177), P170 (= P178), V201 (≠ C208), P202 (= P209), T207 (= T214), T228 (= T235), S229 (≠ A236), D254 (= D261), H278 (= H285), G280 (≠ A287)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
33% identity, 90% coverage: 34:325/326 of query aligns to 34:328/332 of 6biiA
- active site: L99 (≠ G98), R240 (= R237), D264 (= D261), E269 (= E266), H287 (= H285)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ T74), T103 (≠ V102), G156 (= G154), F157 (= F155), G158 (= G156), R159 (≠ N157), I160 (≠ T158), A179 (≠ P178), R180 (= R179), S181 (= S180), K183 (vs. gap), V211 (≠ C208), P212 (= P209), E216 (= E213), T217 (= T214), V238 (≠ T235), A239 (= A236), R240 (= R237), D264 (= D261), H287 (= H285), G289 (≠ A287)
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, 87% coverage: 36:318/326 of query aligns to 89:378/466 of P87228
- S258 (≠ T211) modified: Phosphoserine
Sites not aligning to the query:
- 87 modified: Phosphoserine
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
33% identity, 79% coverage: 56:314/326 of query aligns to 58:308/313 of Q65CJ7
Query Sequence
>206855 MicrobesOnline__882:206855
MRIVALDGYTLNPGDISWAPIEELGELVVHPRTPSDKIIERAAGAHVVLTNKVPLDMSAL
QALPGLRFVSVLATGYDKVDVAAAGVLGIPVSNVPGYGTDSVAQHVFALLLELCRRTALH
DHRIRAGAWTQSPDWCFWDSTQEELTGKTMGIVGFGNTGRRVGRIANALGMNVIAYAPRS
RFDPDYRPFEHVGLDELFTSADVVSLHCPLTPETEGLVDARRLASMRPGSYLINTARGPL
LDERAVAEALDSGRLAGAGLDVLSQEPPAADNPLLSAKNCLITPHLAWASRTARRTLMDS
TAANIRSFIEGTPVNVVNAAHLRTKG
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