SitesBLAST
Comparing WP_043458529.1 NCBI__GCF_000430725.1:WP_043458529.1 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)
38% identity, 74% coverage: 61:295/317 of query aligns to 56:303/334 of 5aovA
- active site: L100 (≠ C105), R241 (= R236), D265 (= D260), E270 (= E265), H288 (= H283)
- binding glyoxylic acid: Y74 (≠ I79), A75 (≠ G80), V76 (= V81), G77 (= G82), R241 (= R236), H288 (= H283)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V81), T104 (≠ V109), F158 (≠ Y156), G159 (= G157), R160 (= R158), I161 (= I159), S180 (≠ T178), R181 (≠ L179), A211 (≠ H206), V212 (≠ L207), P213 (= P208), T218 (≠ S213), I239 (≠ V234), A240 (≠ S235), R241 (= R236), H288 (= H283), G290 (≠ A285)
Sites not aligning to the query:
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
39% identity, 81% coverage: 61:317/317 of query aligns to 55:321/332 of 6biiA
- active site: L99 (≠ C105), R240 (= R236), D264 (= D260), E269 (= E265), H287 (= H283)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V81), T103 (≠ V109), G156 (= G155), F157 (≠ Y156), G158 (= G157), R159 (= R158), I160 (= I159), A179 (= A176), R180 (≠ N177), S181 (≠ T178), K183 (≠ T180), V211 (≠ L207), P212 (= P208), E216 (= E212), T217 (≠ S213), V238 (= V234), A239 (≠ S235), R240 (= R236), D264 (= D260), H287 (= H283), G289 (≠ A285)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
30% identity, 96% coverage: 6:308/317 of query aligns to 3:315/334 of 3kb6B
- active site: S97 (≠ C105), R231 (= R236), D255 (= D260), E260 (= E265), H294 (= H283)
- binding lactic acid: F49 (≠ L56), S72 (≠ G80), V73 (= V81), G74 (= G82), Y96 (= Y104), R231 (= R236), H294 (= H283)
- binding nicotinamide-adenine-dinucleotide: V73 (= V81), Y96 (= Y104), V101 (= V109), G150 (= G157), R151 (= R158), I152 (= I159), D171 (≠ T178), V172 (≠ L179), P203 (= P208), T229 (≠ V234), A230 (≠ S235), R231 (= R236), H294 (= H283), A296 (= A285), Y297 (≠ F286)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
38% identity, 71% coverage: 60:285/317 of query aligns to 55:281/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
38% identity, 71% coverage: 60:285/317 of query aligns to 53:279/311 of 3bazA
- active site: L98 (≠ C105), R230 (= R236), A251 (= A257), D254 (= D260), E259 (= E265), H277 (= H283)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (= V81), G149 (= G155), L150 (≠ Y156), G151 (= G157), R152 (= R158), I153 (= I159), S172 (≠ T178), R173 (≠ L179), S174 (≠ T180), C201 (≠ L207), P202 (= P208), T207 (≠ S213), I228 (≠ V234), G229 (≠ S235), R230 (= R236), D254 (= D260), H277 (= H283), G279 (≠ A285)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
39% identity, 77% coverage: 62:306/317 of query aligns to 53:299/526 of 3dc2A
Sites not aligning to the query:
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
39% identity, 77% coverage: 62:306/317 of query aligns to 54:300/525 of 3ddnB
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
38% identity, 68% coverage: 82:295/317 of query aligns to 88:323/346 of 4zgsA
- active site: S111 (≠ C105), R244 (= R236), D268 (= D260), E273 (= E265), H311 (= H283)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y104), G163 (= G157), A164 (≠ R158), I165 (= I159), D184 (≠ T178), C215 (≠ L207), P216 (= P208), L218 (≠ T210), S220 (≠ E212), T221 (≠ S213), S243 (= S235), H311 (= H283), F314 (= F286)
4lceA Ctbp1 in complex with substrate mtob (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 66:324/327 of 4lceA
- active site: S98 (≠ C105), R240 (= R236), D264 (= D260), E269 (= E265), H289 (= H283)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (= R78), G73 (= G80), S74 (≠ V81), G75 (= G82), R240 (= R236), H289 (= H283), W292 (≠ F286)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V81), T102 (≠ V109), G155 (= G155), G157 (= G157), R158 (= R158), V159 (≠ I159), Y177 (≠ T180), D178 (≠ P181), P179 (= P182), Y180 (≠ A183), H210 (= H206), C211 (≠ L207), N214 (≠ T210), N217 (≠ S213), T238 (≠ V234), A239 (≠ S235), R240 (= R236), W292 (≠ F286)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 67:325/332 of 6v89A
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 67:325/328 of 4u6sA
- active site: S99 (≠ C105), R241 (= R236), D265 (= D260), E270 (= E265), H290 (= H283)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V109), G156 (= G155), G158 (= G157), R159 (= R158), V160 (≠ I159), Y178 (≠ T180), D179 (≠ P181), P180 (= P182), Y181 (≠ A183), H211 (= H206), C212 (≠ L207), G213 (≠ P208), N218 (≠ S213), T239 (≠ V234), A240 (≠ S235), R241 (= R236), H290 (= H283), W293 (≠ F286)
- binding 3-phenylpyruvic acid: I73 (= I79), G74 (= G80), S75 (≠ V81), G76 (= G82), R241 (= R236), W293 (≠ F286), M302 (≠ L295)
Sites not aligning to the query:
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 67:325/328 of 4u6qA
- active site: S99 (≠ C105), R241 (= R236), D265 (= D260), E270 (= E265), H290 (= H283)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: I73 (= I79), G74 (= G80), S75 (≠ V81), G76 (= G82), R241 (= R236), H290 (= H283), W293 (≠ F286), M302 (≠ L295)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ V81), T103 (≠ V109), G156 (= G155), R159 (= R158), V160 (≠ I159), Y178 (≠ T180), D179 (≠ P181), P180 (= P182), Y181 (≠ A183), H211 (= H206), C212 (≠ L207), G213 (≠ P208), N218 (≠ S213), T239 (≠ V234), A240 (≠ S235), R241 (= R236), H290 (= H283), W293 (≠ F286)
Sites not aligning to the query:
6cdfA Human ctbp1 (28-378) (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 68:326/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V109), G157 (= G155), R160 (= R158), V161 (≠ I159), Y179 (≠ T180), D180 (≠ P181), P181 (= P182), Y182 (≠ A183), H212 (= H206), C213 (≠ L207), N219 (≠ S213), T240 (≠ V234), A241 (≠ S235), R242 (= R236), H291 (= H283), W294 (≠ F286)
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
38% identity, 76% coverage: 73:312/317 of query aligns to 66:318/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V81), T102 (≠ V109), G155 (= G155), G157 (= G157), R158 (= R158), T159 (≠ I159), D178 (≠ P181), P179 (= P182), Y180 (≠ A183), H210 (= H206), C211 (≠ L207), N212 (≠ P208), A238 (≠ V234), R240 (= R236), H289 (= H283), A291 (= A285), W292 (≠ F286)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
38% identity, 76% coverage: 73:312/317 of query aligns to 66:318/330 of 4lcjA
- active site: A98 (≠ C105), R240 (= R236), D264 (= D260), E269 (= E265), H289 (= H283)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: I72 (= I79), G73 (= G80), S74 (≠ V81), G75 (= G82), R240 (= R236), H289 (= H283), W292 (≠ F286)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V81), T102 (≠ V109), I154 (≠ V154), G155 (= G155), G157 (= G157), R158 (= R158), T159 (≠ I159), D178 (≠ P181), Y180 (≠ A183), H210 (= H206), C211 (≠ L207), N212 (≠ P208), N214 (≠ T210), N217 (≠ S213), A238 (≠ V234), A239 (≠ S235), R240 (= R236), H289 (= H283), W292 (≠ F286)
Sites not aligning to the query:
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 67:325/331 of 1hl3A
- active site: S99 (≠ C105), R241 (= R236), D265 (= D260), E270 (= E265), H290 (= H283)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V109), G158 (= G157), R159 (= R158), V160 (≠ I159), D179 (≠ P181), Y181 (≠ A183), H211 (= H206), C212 (≠ L207), G213 (≠ P208), N218 (≠ S213), T239 (≠ V234), A240 (≠ S235), R241 (= R236), D265 (= D260), H290 (= H283)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
38% identity, 77% coverage: 73:316/317 of query aligns to 67:325/331 of 1hkuA
- active site: S99 (≠ C105), R241 (= R236), D265 (= D260), E270 (= E265), H290 (= H283)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ V81), T103 (≠ V109), G156 (= G155), G158 (= G157), R159 (= R158), V160 (≠ I159), Y178 (≠ T180), D179 (≠ P181), P180 (= P182), Y181 (≠ A183), C212 (≠ L207), N218 (≠ S213), T239 (≠ V234), A240 (≠ S235), R241 (= R236), H290 (= H283), W293 (≠ F286)
Sites not aligning to the query:
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 91% coverage: 22:309/317 of query aligns to 16:304/304 of 1wwkA
- active site: S96 (≠ C105), R230 (= R236), D254 (= D260), E259 (= E265), H278 (= H283)
- binding nicotinamide-adenine-dinucleotide: V100 (= V109), G146 (= G155), F147 (≠ Y156), G148 (= G157), R149 (= R158), I150 (= I159), Y168 (≠ N177), D169 (≠ T178), P170 (≠ L179), V201 (≠ L207), P202 (= P208), T207 (≠ S213), T228 (≠ V234), S229 (= S235), D254 (= D260), H278 (= H283), G280 (≠ A285)
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)
38% identity, 77% coverage: 73:316/317 of query aligns to 81:339/430 of Q9Z2F5
- S89 (≠ V81) binding
- IGLGRV 169:174 (≠ VGYGRI 154:159) binding
- G172 (= G157) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ P181) binding
- 226:232 (vs. 207:213, 14% identical) binding
- TAR 253:255 (≠ VSR 234:236) binding
- D279 (= D260) binding
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
- 55 V→R: Strongly reduces interaction with E1A.
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
38% identity, 77% coverage: 73:316/317 of query aligns to 92:350/440 of Q13363
- C134 (≠ G115) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ A119) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R122) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ RG 122:123) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V131) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (= R144) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (= R145) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G155) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G157) 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 (= G160) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ P181) 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 (= R236) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D260) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E265) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H283) 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.
- 66 V→R: Loss of interaction with SIMC1. Reduced 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)
Query Sequence
>WP_043458529.1 NCBI__GCF_000430725.1:WP_043458529.1
MTASTVLVTDFAWPDLDIERDVLEGAGLRLVAGPASPAPADTIAALVREHQPSSILTCWA
QVNAQAVNASSRLQHVGRIGVGLDNIDVAACTARGLPVTNVPDYCVEEVSDHAVGFALAW
TRGLVAFDRDVHAGRWDPAKARLRRLSALTVGLVGYGRIGQASARKFAAFGCRVLANTLT
PPARSTGVEFTELDTLLTQSDIVVLHLPLTPESHHLINRSRINAMKPGALLVNVSRGGIV
DTDAVVEALASGHLGGAALDVIESEPQVPAALLAQPGALLTPHVAFSSDASLAELRRRAA
EETVRVLSGRAPLNRCN
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