SitesBLAST
Comparing WP_012673571.1 NCBI__GCF_000021545.1:WP_012673571.1 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)
38% identity, 87% coverage: 35:313/319 of query aligns to 36:315/334 of 5aovA
- active site: L100 (≠ S98), R241 (= R235), D265 (= D259), E270 (= E264), H288 (= H286)
- binding glyoxylic acid: M52 (≠ N51), L53 (vs. gap), L53 (vs. gap), Y74 (≠ A72), A75 (= A73), V76 (≠ T74), G77 (= G75), R241 (= R235), H288 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T74), T104 (≠ V102), F158 (≠ L155), G159 (= G156), R160 (≠ T157), I161 (= I158), S180 (= S177), R181 (≠ T178), A211 (≠ H205), V212 (≠ A206), P213 (= P207), T218 (= T212), I239 (≠ L233), A240 (≠ G234), R241 (= R235), H288 (= H286), G290 (≠ A288)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 93% coverage: 17:312/319 of query aligns to 14:304/304 of 1wwkA
- active site: S96 (= S98), R230 (= R235), D254 (= D259), E259 (= E264), H278 (= H286)
- binding nicotinamide-adenine-dinucleotide: V100 (= V102), G146 (= G154), F147 (≠ L155), G148 (= G156), R149 (≠ T157), I150 (= I158), Y168 (= Y176), D169 (vs. gap), P170 (vs. gap), V201 (≠ A206), P202 (= P207), T207 (= T212), T228 (≠ L233), S229 (≠ G234), D254 (= D259), H278 (= H286), G280 (≠ A288)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
36% identity, 87% coverage: 35:313/319 of query aligns to 35:314/332 of 6biiA
- active site: L99 (≠ S98), R240 (= R235), D264 (= D259), E269 (= E264), H287 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ T74), T103 (≠ V102), G156 (= G154), F157 (≠ L155), G158 (= G156), R159 (≠ T157), I160 (= I158), A179 (≠ S177), R180 (≠ T178), S181 (= S179), K183 (= K181), V211 (≠ A206), P212 (= P207), E216 (≠ Y211), T217 (= T212), V238 (≠ L233), A239 (≠ G234), R240 (= R235), D264 (= D259), H287 (= H286), G289 (≠ A288)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
32% identity, 88% coverage: 31:312/319 of query aligns to 32:320/334 of 3kb6B
- active site: S97 (= S98), R231 (= R235), D255 (= D259), E260 (= E264), H294 (= H286)
- binding lactic acid: F49 (≠ I48), S72 (≠ A73), V73 (≠ T74), G74 (= G75), Y96 (= Y97), R231 (= R235), H294 (= H286)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ T74), Y96 (= Y97), V101 (= V102), G150 (= G156), R151 (≠ T157), I152 (= I158), D171 (≠ S177), V172 (≠ T178), P203 (= P207), T229 (≠ L233), A230 (≠ G234), R231 (= R235), H294 (= H286), A296 (= A288), Y297 (≠ W289)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
37% identity, 96% coverage: 9:313/319 of query aligns to 17:315/334 of O58320
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
37% identity, 96% coverage: 9:313/319 of query aligns to 17:315/333 of 2dbqA
- active site: L100 (≠ S98), R241 (= R235), D265 (= D259), E270 (= E264), H288 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ T74), T104 (≠ V102), L158 (= L155), G159 (= G156), R160 (≠ T157), I161 (= I158), S180 (= S177), R181 (≠ T178), T182 (≠ S179), A211 (≠ H205), V212 (≠ A206), P213 (= P207), T218 (= T212), I239 (≠ L233), A240 (≠ G234), R241 (= R235), D265 (= D259), H288 (= H286), G290 (≠ A288)
4lceA Ctbp1 in complex with substrate mtob (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 4:325/327 of 4lceA
- active site: S98 (= S98), R240 (= R235), D264 (= D259), E269 (= E264), H289 (= H286)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ V71), G73 (≠ A73), S74 (≠ T74), G75 (= G75), R240 (= R235), H289 (= H286), W292 (= W289)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), G155 (= G154), G157 (= G156), R158 (≠ T157), V159 (≠ I158), Y177 (= Y176), D178 (vs. gap), P179 (vs. gap), Y180 (vs. gap), H210 (= H205), C211 (≠ A206), N214 (= N209), N217 (≠ T212), T238 (≠ L233), A239 (≠ G234), R240 (= R235), W292 (= W289)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 5:326/332 of 6v89A
6cdfA Human ctbp1 (28-378) (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 6:327/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V102), G157 (= G154), R160 (≠ T157), V161 (≠ I158), Y179 (= Y176), D180 (vs. gap), P181 (vs. gap), Y182 (vs. gap), H212 (= H205), C213 (≠ A206), N219 (≠ T212), T240 (≠ L233), A241 (≠ G234), R242 (= R235), H291 (= H286), W294 (= W289)
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 5:326/328 of 4u6sA
- active site: S99 (= S98), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H286)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V102), G156 (= G154), G158 (= G156), R159 (≠ T157), V160 (≠ I158), Y178 (= Y176), D179 (vs. gap), P180 (vs. gap), Y181 (vs. gap), H211 (= H205), C212 (≠ A206), G213 (≠ P207), N218 (≠ T212), T239 (≠ L233), A240 (≠ G234), R241 (= R235), H290 (= H286), W293 (= W289)
- binding 3-phenylpyruvic acid: Y51 (≠ T50), H52 (≠ N51), I73 (≠ A72), G74 (≠ A73), S75 (≠ T74), G76 (= G75), R241 (= R235), W293 (= W289), M302 (≠ A294)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 5:326/328 of 4u6qA
- active site: S99 (= S98), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H286)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ T50), I73 (≠ A72), G74 (≠ A73), S75 (≠ T74), G76 (= G75), R241 (= R235), H290 (= H286), W293 (= W289), M302 (≠ A294)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ T74), T103 (≠ V102), G156 (= G154), R159 (≠ T157), V160 (≠ I158), Y178 (= Y176), D179 (vs. gap), P180 (vs. gap), Y181 (vs. gap), H211 (= H205), C212 (≠ A206), G213 (≠ P207), N218 (≠ T212), T239 (≠ L233), A240 (≠ G234), R241 (= R235), H290 (= H286), W293 (= W289)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 5:326/331 of 1hl3A
- active site: S99 (= S98), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H286)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V102), G158 (= G156), R159 (≠ T157), V160 (≠ I158), D179 (vs. gap), Y181 (vs. gap), H211 (= H205), C212 (≠ A206), G213 (≠ P207), N218 (≠ T212), T239 (≠ L233), A240 (≠ G234), R241 (= R235), D265 (= D259), H290 (= H286)
- binding : M17 (≠ L17), V26 (≠ I26), A27 (≠ E27), F28 (≠ Y29), C29 (≠ P30), E36 (= E37), H38 (≠ I39), E39 (= E40)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 5:326/331 of 1hkuA
- active site: S99 (= S98), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H286)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T74), T103 (≠ V102), G156 (= G154), G158 (= G156), R159 (≠ T157), V160 (≠ I158), Y178 (= Y176), D179 (vs. gap), P180 (vs. gap), Y181 (vs. gap), C212 (≠ A206), N218 (≠ T212), T239 (≠ L233), A240 (≠ G234), R241 (= R235), H290 (= H286), W293 (= W289)
Sites not aligning to the query:
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
33% identity, 81% coverage: 56:313/319 of query aligns to 58:306/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
33% identity, 81% coverage: 56:313/319 of query aligns to 56:304/311 of 3bazA
- active site: L98 (≠ S98), R230 (= R235), A251 (= A256), D254 (= D259), E259 (= E264), H277 (= H286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (≠ T74), G149 (= G154), L150 (= L155), G151 (= G156), R152 (≠ T157), I153 (= I158), S172 (= S177), R173 (≠ T178), S174 (= S179), C201 (≠ A206), P202 (= P207), T207 (= T212), I228 (≠ L233), G229 (= G234), R230 (= R235), D254 (= D259), H277 (= H286), G279 (≠ A288)
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)
29% identity, 99% coverage: 3:318/319 of query aligns to 19:340/430 of Q9Z2F5
- A41 (≠ E27) mutation to E: Strongly reduces interaction with E1A.
- V55 (= V42) mutation to R: Strongly reduces interaction with E1A.
- S89 (≠ T74) binding
- IGLGRV 169:174 (≠ IGLGTI 153:158) binding
- G172 (= G156) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ S177) binding
- 226:232 (vs. 206:212, 43% identical) binding
- TAR 253:255 (≠ LGR 233:235) binding
- D279 (= D259) binding
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
29% identity, 99% coverage: 3:318/319 of query aligns to 30:351/440 of Q13363
- A52 (≠ E27) mutation to E: Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3.
- V66 (= V42) 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 (≠ Y112) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (≠ E115) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ EN 115:116) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V124) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ T136) 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 (≠ S177) 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 (= R235) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D259) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E264) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H286) 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)
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
30% identity, 99% coverage: 3:318/319 of query aligns to 4:325/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), G155 (= G154), G157 (= G156), R158 (≠ T157), T159 (≠ I158), D178 (≠ S177), P179 (vs. gap), Y180 (vs. gap), H210 (= H205), C211 (≠ A206), N212 (≠ P207), A238 (≠ L233), R240 (= R235), H289 (= H286), A291 (= A288), W292 (= W289)
- binding : C12 (≠ L11), M16 (≠ L17), V25 (≠ I26), A26 (≠ I28), F27 (≠ Y29), C28 (≠ P30), E35 (= E37), H37 (≠ I39)
4lcjA Ctbp2 in complex with substrate mtob (see paper)
30% identity, 99% coverage: 3:318/319 of query aligns to 4:325/330 of 4lcjA
- active site: A98 (≠ S98), R240 (= R235), D264 (= D259), E269 (= E264), H289 (= H286)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: Y50 (≠ T50), H51 (≠ N51), I72 (≠ A72), G73 (≠ A73), S74 (≠ T74), G75 (= G75), R240 (= R235), H289 (= H286), W292 (= W289)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), I154 (= I153), G155 (= G154), G157 (= G156), R158 (≠ T157), T159 (≠ I158), D178 (≠ S177), Y180 (vs. gap), H210 (= H205), C211 (≠ A206), N212 (≠ P207), N214 (= N209), N217 (≠ T212), A238 (≠ L233), A239 (≠ G234), R240 (= R235), H289 (= H286), W292 (= W289)
4zgsA Identification of the pyruvate reductase of chlamydomonas reinhardtii (see paper)
33% identity, 77% coverage: 66:310/319 of query aligns to 79:335/346 of 4zgsA
- active site: S111 (= S98), R244 (= R235), D268 (= D259), E273 (= E264), H311 (= H286)
- binding nicotinamide-adenine-dinucleotide: Y110 (= Y97), G163 (= G156), A164 (≠ T157), I165 (= I158), D184 (≠ S177), C215 (≠ A206), P216 (= P207), L218 (≠ N209), S220 (≠ Y211), T221 (= T212), S243 (≠ G234), H311 (= H286), F314 (≠ W289)
Query Sequence
>WP_012673571.1 NCBI__GCF_000021545.1:WP_012673571.1
MKLAILDAKTLGDDIDLNIFRDFGYIEIYPITKTKEETIERVKDKNIIITNKVIIDKDVM
DNAPYLKLICVAATGYNNVDINYAKQKGIAVTNVAGYSTNSVVQHTFAMLFYLLENLRYY
DDYVKSGEYSKSPIFTHLDRPFWELNGKTWGVIGLGTIGKKVAQVAESFGCDVIYYSTSG
KNLDQTYPHKGLDELLSISDIVSIHAPLNEYTKNLITYDKIKLMKKTAILLNLGRGGIVN
ERDLAKALDEGLIAAAGLDVLEKEPIDPDNPLLFIKNKDRLLITPHIAWTSIEARQTLVK
EIYLNIEAFIRGKQRNRVC
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