SitesBLAST
Comparing WP_015887821.1 NCBI__GCF_000018545.1:WP_015887821.1 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)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
38% identity, 77% coverage: 74:338/345 of query aligns to 45:303/526 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)
38% identity, 77% coverage: 74:338/345 of query aligns to 46:304/525 of 3ddnB
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 83% coverage: 51:338/345 of query aligns to 21:304/304 of 1wwkA
- active site: S96 (≠ N125), R230 (= R264), D254 (≠ E288), E259 (= E293), H278 (= H312)
- binding nicotinamide-adenine-dinucleotide: V100 (= V129), G146 (= G179), F147 (≠ Y180), G148 (= G181), R149 (≠ N182), I150 (= I183), Y168 (≠ H201), D169 (= D202), P170 (= P203), V201 (≠ P235), P202 (≠ R236), T207 (= T241), T228 (= T262), S229 (≠ A263), D254 (≠ E288), H278 (= H312), G280 (≠ A314)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
34% identity, 81% coverage: 62:341/345 of query aligns to 35:318/334 of 5aovA
- active site: L100 (≠ N125), R241 (= R264), D265 (≠ E288), E270 (= E293), H288 (= H312)
- binding glyoxylic acid: M52 (≠ Q78), L53 (= L79), L53 (= L79), Y74 (≠ S99), A75 (≠ R100), V76 (≠ G101), G77 (= G102), R241 (= R264), H288 (= H312)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ G101), T104 (≠ V129), F158 (≠ Y180), G159 (= G181), R160 (≠ N182), I161 (= I183), S180 (≠ D202), R181 (≠ P203), A211 (≠ H234), V212 (≠ P235), P213 (≠ R236), T218 (= T241), I239 (≠ T262), A240 (= A263), R241 (= R264), H288 (= H312), G290 (≠ A314)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
32% identity, 74% coverage: 82:338/345 of query aligns to 54:320/334 of 3kb6B
- active site: S97 (≠ N125), R231 (= R264), D255 (≠ E288), E260 (= E293), H294 (= H312)
- binding lactic acid: S72 (≠ R100), V73 (≠ G101), G74 (= G102), Y96 (≠ R124), R231 (= R264), H294 (= H312)
- binding nicotinamide-adenine-dinucleotide: V73 (≠ G101), Y96 (≠ R124), V101 (= V129), G150 (= G181), R151 (≠ N182), I152 (= I183), D171 (= D202), V172 (≠ P203), P203 (≠ R236), T229 (= T262), A230 (= A263), R231 (= R264), H294 (= H312), A296 (= A314), Y297 (≠ G315)
Sites not aligning to the query:
2gsdA NAD-dependent formate dehydrogenase from bacterium moraxella sp.C2 in complex with NAD and azide (see paper)
31% identity, 85% coverage: 48:340/345 of query aligns to 52:360/399 of 2gsdA
- active site: N146 (= N125), R284 (= R264), D308 (≠ E288), Q313 (≠ E293), H332 (= H312)
- binding azide ion: P97 (≠ L79), F98 (vs. gap), I122 (≠ G101), R284 (= R264), H332 (= H312)
- binding nicotinamide-adenine-dinucleotide: I122 (≠ G101), N146 (= N125), V150 (= V129), A198 (≠ G179), G200 (= G181), R201 (≠ N182), I202 (= I183), D221 (= D202), R222 (≠ P203), P256 (≠ R236), H258 (≠ T238), T261 (= T241), T282 (= T262), A283 (= A263), R284 (= R264), D308 (≠ E288), H332 (= H312), S334 (≠ A314), G335 (= G315)
Sites not aligning to the query:
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 49:319/332 of 6v89A
6cdfA Human ctbp1 (28-378) (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 50:320/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V129), G157 (= G179), R160 (≠ N182), V161 (≠ I183), Y179 (≠ H201), D180 (= D202), P181 (= P203), Y182 (= Y204), H212 (= H234), C213 (≠ P235), N219 (≠ T241), T240 (= T262), A241 (= A263), R242 (= R264), H291 (= H312), W294 (≠ G315)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 49:319/331 of 1hl3A
- active site: S99 (≠ N125), R241 (= R264), D265 (≠ E288), E270 (= E293), H290 (= H312)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V129), G158 (= G181), R159 (≠ N182), V160 (≠ I183), D179 (= D202), Y181 (= Y204), H211 (= H234), C212 (≠ P235), G213 (≠ R236), N218 (≠ T241), T239 (= T262), A240 (= A263), R241 (= R264), D265 (≠ E288), H290 (= H312)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 49:319/331 of 1hkuA
- active site: S99 (≠ N125), R241 (= R264), D265 (≠ E288), E270 (= E293), H290 (= H312)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ G101), T103 (≠ V129), G156 (= G179), G158 (= G181), R159 (≠ N182), V160 (≠ I183), Y178 (≠ H201), D179 (= D202), P180 (= P203), Y181 (= Y204), C212 (≠ P235), N218 (≠ T241), T239 (= T262), A240 (= A263), R241 (= R264), H290 (= H312), W293 (≠ G315)
Sites not aligning to the query:
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 49:319/328 of 4u6sA
- active site: S99 (≠ N125), R241 (= R264), D265 (≠ E288), E270 (= E293), H290 (= H312)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V129), G156 (= G179), G158 (= G181), R159 (≠ N182), V160 (≠ I183), Y178 (≠ H201), D179 (= D202), P180 (= P203), Y181 (= Y204), H211 (= H234), C212 (≠ P235), G213 (≠ R236), N218 (≠ T241), T239 (= T262), A240 (= A263), R241 (= R264), H290 (= H312), W293 (≠ G315)
- binding 3-phenylpyruvic acid: Y51 (≠ T77), H52 (≠ Q78), I73 (≠ S99), G74 (≠ R100), S75 (≠ G101), G76 (= G102), R241 (= R264), W293 (≠ G315), M302 (≠ A324)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 49:319/328 of 4u6qA
- active site: S99 (≠ N125), R241 (= R264), D265 (≠ E288), E270 (= E293), H290 (= H312)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ T77), I73 (≠ S99), G74 (≠ R100), S75 (≠ G101), G76 (= G102), R241 (= R264), H290 (= H312), W293 (≠ G315), M302 (≠ A324)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ G101), T103 (≠ V129), G156 (= G179), R159 (≠ N182), V160 (≠ I183), Y178 (≠ H201), D179 (= D202), P180 (= P203), Y181 (= Y204), H211 (= H234), C212 (≠ P235), G213 (≠ R236), N218 (≠ T241), T239 (= T262), A240 (= A263), R241 (= R264), H290 (= H312), W293 (≠ G315)
1dxyA Structure of d-2-hydroxyisocaproate dehydrogenase (see paper)
32% identity, 69% coverage: 78:314/345 of query aligns to 52:297/330 of 1dxyA
- active site: S101 (≠ N125), R234 (= R264), D258 (≠ E288), E263 (= E293), H295 (= H312)
- binding 2-oxo-4-methylpentanoic acid: V77 (≠ G101), Y100 (≠ R124)
- binding nicotinamide-adenine-dinucleotide: Y100 (≠ R124), G152 (= G179), G154 (= G181), H155 (≠ N182), I156 (= I183), Y174 (≠ H201), D175 (= D202), P176 (= P203), H204 (= H234), V205 (≠ P235), P206 (≠ R236), N211 (≠ T241), T232 (= T262), A233 (= A263), R234 (= R264), H295 (= H312)
Sites not aligning to the query:
4lceA Ctbp1 in complex with substrate mtob (see paper)
34% identity, 77% coverage: 75:341/345 of query aligns to 48:318/327 of 4lceA
- active site: S98 (≠ N125), R240 (= R264), D264 (≠ E288), E269 (= E293), H289 (= H312)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (≠ V98), G73 (≠ R100), S74 (≠ G101), G75 (= G102), R240 (= R264), H289 (= H312), W292 (≠ G315)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ G101), T102 (≠ V129), G155 (= G179), G157 (= G181), R158 (≠ N182), V159 (≠ I183), Y177 (≠ H201), D178 (= D202), P179 (= P203), Y180 (= Y204), H210 (= H234), C211 (≠ P235), N214 (≠ T238), N217 (≠ T241), T238 (= T262), A239 (= A263), R240 (= R264), W292 (≠ G315)
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
34% identity, 75% coverage: 82:341/345 of query aligns to 81:344/440 of Q13363
- C134 (≠ G135) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ A139) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R142) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ RL 142:143) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (= L151) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ D164) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ E172) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G179) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G181) 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 (= G184) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (= D202) 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 (= R264) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (≠ E288) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E293) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H312) 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)
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)
34% identity, 77% coverage: 75:341/345 of query aligns to 63:333/430 of Q9Z2F5
- S89 (≠ G101) binding NAD(+)
- IGLGRV 169:174 (≠ IGYGNI 178:183) binding NAD(+)
- G172 (= G181) mutation to E: Loss dimerization and of NAD binding.
- D193 (= D202) binding NAD(+)
- 226:232 (vs. 235:241, 0% identical) binding NAD(+)
- TAR 253:255 (= TAR 262:264) binding NAD(+)
- D279 (≠ E288) binding NAD(+)
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
- 55 V→R: Strongly reduces interaction with E1A.
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
30% identity, 82% coverage: 56:338/345 of query aligns to 29:305/305 of 6plfA
5z20F The ternary structure of d-lactate dehydrogenase from pseudomonas aeruginosa with nadh and oxamate (see paper)
34% identity, 72% coverage: 94:340/345 of query aligns to 77:330/336 of 5z20F
- active site: S108 (≠ N125), R241 (= R264), D265 (≠ E288), E270 (= E293), H302 (= H312)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (≠ R124), G160 (= G181), Q161 (≠ N182), I162 (= I183), Y180 (≠ H201), D181 (= D202), P182 (= P203), C212 (≠ P235), P213 (≠ R236), T218 (= T241), T239 (= T262), G240 (≠ A263), R241 (= R264), H302 (= H312), A304 (= A314)
7dkmA Phgdh covalently linked to oridonin (see paper)
31% identity, 80% coverage: 56:332/345 of query aligns to 29:295/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ G101), A102 (≠ V129), G148 (= G179), R151 (≠ N182), I152 (= I183), Y170 (≠ H201), D171 (= D202), P172 (= P203), I173 (≠ Y204), H202 (= H234), T203 (≠ P235), P204 (≠ R236), T209 (= T241), C230 (≠ T262), A231 (= A263), R232 (= R264), H279 (= H312), G281 (= G315)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: E293 (= E330)
Sites not aligning to the query:
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: 14, 17, 18
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
31% identity, 80% coverage: 56:332/345 of query aligns to 27:293/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N125), A100 (≠ V129), R149 (≠ N182), I150 (= I183), Y168 (≠ H201), D169 (= D202), P170 (= P203), I171 (≠ Y204), H200 (= H234), T201 (≠ P235), P202 (≠ R236), T207 (= T241), C228 (≠ T262), A229 (= A263), R230 (= R264), H277 (= H312), G279 (= G315)
Query Sequence
>WP_015887821.1 NCBI__GCF_000018545.1:WP_015887821.1
MKKIAIIGDRFMLPDVFRDKIVAACGDGHDIRTLEQPWPDVPMEHGYAVEGMDGLKEYLG
KPKEIVDFIGDAEILVTQLAPLSRAMFSELPRLKLVAVSRGGPVNIDMDAARDAGVRVVN
TPGRNASAVAEFTIGAILAETRLIRVGHEALRKGEWRGDLYRADRTGRELSELTIGVIGY
GNIGTKVVRLLRAFGTEVLVHDPYVQLSAEDRNAGVEHVSRDDLLARSDVVTLHPRVTAE
TRNMMNAETFAKMKPGAVFVNTARGPLCDYEALYESLVSGHLSSAMLETFAVEPVPEDWP
LLKLPNVTLTPHIAGASVRTVTHAAEMAAEEVRRYIAGLPPVNPC
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