SitesBLAST
Comparing WP_018125039.1 NCBI__GCF_000375485.1:WP_018125039.1 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)
37% identity, 89% coverage: 34:318/321 of query aligns to 35:322/334 of 5aovA
- active site: L100 (≠ S98), R241 (= R237), D265 (= D261), E270 (= E266), H288 (= H285)
- binding glyoxylic acid: M52 (≠ N51), L53 (≠ K52), L53 (≠ K52), 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 (≠ G157), I161 (= I158), S180 (≠ A177), R181 (≠ P178), A211 (≠ H207), V212 (≠ C208), P213 (= P209), T218 (≠ N214), 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)
37% identity, 79% coverage: 67:318/321 of query aligns to 77:335/336 of 5z20F
- active site: S108 (= S98), R241 (= R237), D265 (= D261), E270 (= E266), H302 (= H285)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y107 (= Y97), G160 (= G156), Q161 (≠ G157), I162 (= I158), Y180 (≠ H176), D181 (≠ A177), P182 (= P178), C212 (= C208), P213 (= P209), T218 (≠ N214), T239 (= T235), G240 (≠ A236), R241 (= R237), H302 (= H285), A304 (= A287)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
36% identity, 89% coverage: 34:318/321 of query aligns to 34:321/332 of 6biiA
- active site: L99 (≠ S98), 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 (≠ G157), I160 (= I158), A179 (= A175), R180 (≠ H176), S181 (≠ A177), K183 (≠ R179), V211 (≠ C208), P212 (= P209), E216 (= E213), T217 (≠ N214), V238 (≠ T235), A239 (= A236), R240 (= R237), D264 (= D261), H287 (= H285), G289 (≠ A287)
3kb6B Crystal structure of d-lactate dehydrogenase from aquifex aeolicus complexed with NAD and lactic acid (see paper)
32% identity, 87% coverage: 32:311/321 of query aligns to 34:320/334 of 3kb6B
- active site: S97 (= S98), R231 (= R237), D255 (= D261), E260 (= E266), H294 (= H285)
- binding lactic acid: F49 (≠ I48), 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 (≠ G157), I152 (= I158), D171 (≠ A177), V172 (≠ P178), P203 (= P209), T229 (= T235), A230 (= A236), R231 (= R237), H294 (= H285), A296 (= A287), Y297 (≠ W288)
6p2iA Acyclic imino acid reductase (bsp5) in complex with NADPH and d-arg (see paper)
34% identity, 99% coverage: 1:317/321 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 (= S98), V102 (= V102), G149 (= G154), I150 (≠ F155), G151 (= G156), Q152 (≠ G157), I153 (= I158), N172 (≠ P180), K173 (= K181), S174 (≠ P182), R176 (≠ P184), H199 (= H207), I200 (≠ C208), P201 (= P209), T206 (≠ N214), T227 (= T235), C228 (≠ A236), W277 (= W288)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
36% identity, 83% coverage: 47:311/321 of query aligns to 45:304/304 of 1wwkA
- active site: S96 (= S98), R230 (= R237), D254 (= D261), E259 (= E266), H278 (= H285)
- binding nicotinamide-adenine-dinucleotide: V100 (= V102), G146 (= G154), F147 (= F155), G148 (= G156), R149 (≠ G157), I150 (= I158), Y168 (≠ H176), D169 (≠ A177), P170 (= P178), V201 (≠ C208), P202 (= P209), T207 (≠ N214), T228 (= T235), S229 (≠ A236), D254 (= D261), H278 (= H285), G280 (≠ A287)
8atiA Human ctbp2(31-364) in complex with rai2 peptide(315-322)
33% identity, 89% coverage: 35:321/321 of query aligns to 37:326/330 of 8atiA
- binding nicotinamide-adenine-dinucleotide: S74 (≠ T74), T102 (≠ V102), G155 (= G154), G157 (= G156), R158 (≠ G157), T159 (≠ I158), D178 (≠ A177), P179 (= P178), Y180 (≠ R179), H210 (= H207), C211 (= C208), N212 (≠ P209), A238 (≠ T235), R240 (= R237), H289 (= H285), A291 (= A287), W292 (= W288)
- binding : H37 (= H35)
Sites not aligning to the query:
4lcjA Ctbp2 in complex with substrate mtob (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 37:326/330 of 4lcjA
- active site: A98 (≠ S98), 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 (= I153), G155 (= G154), G157 (= G156), R158 (≠ G157), T159 (≠ I158), D178 (≠ A177), Y180 (≠ R179), H210 (= H207), C211 (= C208), N212 (≠ P209), N214 (≠ T211), N217 (= N214), A238 (≠ T235), A239 (= A236), R240 (= R237), H289 (= H285), W292 (= W288)
6cdfA Human ctbp1 (28-378) (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 39:328/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V102), G157 (= G154), R160 (≠ G157), V161 (≠ I158), Y179 (≠ H176), D180 (≠ A177), P181 (= P178), Y182 (≠ R179), H212 (= H207), C213 (= C208), N219 (= N214), T240 (= T235), A241 (= A236), R242 (= R237), H291 (= H285), W294 (= W288)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 38:327/332 of 6v89A
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 38:327/328 of 4u6sA
- active site: S99 (= S98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V102), G156 (= G154), G158 (= G156), R159 (≠ G157), V160 (≠ I158), Y178 (≠ H176), D179 (≠ A177), P180 (= P178), Y181 (≠ R179), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (= N214), 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)
33% identity, 89% coverage: 35:321/321 of query aligns to 38:327/328 of 4u6qA
- active site: S99 (= S98), 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 (≠ G157), V160 (≠ I158), Y178 (≠ H176), D179 (≠ A177), P180 (= P178), Y181 (≠ R179), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (= N214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H285), W293 (= W288)
4lceA Ctbp1 in complex with substrate mtob (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 37:326/327 of 4lceA
- active site: S98 (= S98), 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 (≠ G157), V159 (≠ I158), Y177 (≠ H176), D178 (≠ A177), P179 (= P178), Y180 (≠ R179), H210 (= H207), C211 (= C208), N214 (≠ T211), N217 (= N214), T238 (= T235), A239 (= A236), R240 (= R237), W292 (= W288)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 38:327/331 of 1hl3A
- active site: S99 (= S98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V102), G158 (= G156), R159 (≠ G157), V160 (≠ I158), D179 (≠ A177), Y181 (≠ R179), H211 (= H207), C212 (= C208), G213 (≠ P209), N218 (= N214), T239 (= T235), A240 (= A236), R241 (= R237), D265 (= D261), H290 (= H285)
- binding : H38 (= H35), E39 (≠ N36)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
33% identity, 89% coverage: 35:321/321 of query aligns to 38:327/331 of 1hkuA
- active site: S99 (= S98), R241 (= R237), D265 (= D261), E270 (= E266), H290 (= H285)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ T74), T103 (≠ V102), G156 (= G154), G158 (= G156), R159 (≠ G157), V160 (≠ I158), Y178 (≠ H176), D179 (≠ A177), P180 (= P178), Y181 (≠ R179), C212 (= C208), N218 (= N214), T239 (= T235), A240 (= A236), R241 (= R237), H290 (= H285), W293 (= W288)
Sites not aligning to the query:
P56545 C-terminal-binding protein 2; CtBP2 from Homo sapiens (Human)
33% identity, 89% coverage: 35:321/321 of query aligns to 69:358/445 of P56545
- IGFGRT 186:191 (≠ IGFGGI 153:158) binding NAD(+)
- D210 (≠ A177) binding NAD(+)
- 243:249 (vs. 208:214, 43% identical) binding NAD(+)
- AAR 270:272 (≠ TAR 235:237) binding NAD(+)
- D296 (= D261) binding NAD(+)
- HTAW 321:324 (≠ HVAW 285:288) binding NAD(+)
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)
33% identity, 89% coverage: 35:321/321 of query aligns to 52:341/430 of Q9Z2F5
- V55 (≠ I38) mutation to R: Strongly reduces interaction with E1A.
- S89 (≠ T74) binding NAD(+)
- IGLGRV 169:174 (≠ IGFGGI 153:158) binding NAD(+)
- G172 (= G156) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ A177) binding NAD(+)
- 226:232 (vs. 208:214, 43% identical) binding NAD(+)
- TAR 253:255 (= TAR 235:237) binding NAD(+)
- D279 (= D261) binding NAD(+)
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
33% identity, 89% coverage: 35:321/321 of query aligns to 63:352/440 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 (≠ S115) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ SR 115:116) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ T124) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (≠ C136) 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)
4cukA Structure of salmonella d-lactate dehydrogenase in complex with nadh
36% identity, 79% coverage: 59:311/321 of query aligns to 60:321/330 of 4cukA
- active site: S101 (= S98), R234 (= R237), D258 (= D261), E263 (= E266), H295 (= H285)
- binding 1,4-dihydronicotinamide adenine dinucleotide: Y100 (= Y97), G153 (= G156), K154 (≠ G157), I155 (= I158), F173 (≠ H176), D174 (≠ A177), P175 (= P178), H204 (= H207), C205 (= C208), P206 (= P209), N211 (= N214), T232 (= T235), Y260 (≠ L263), H295 (= H285), A297 (= A287)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
37% identity, 82% coverage: 45:306/321 of query aligns to 43:299/525 of 3ddnB
Query Sequence
>WP_018125039.1 NCBI__GCF_000375485.1:WP_018125039.1
MKIVVLDGYTLNPGDNPWDEIETLGTLEVHDRTPHNEIAQRAAGADVILTNKTKLPAEIL
DELPELKYISVLATGYDVVDVKAAAARGIAVSNVPGYSTPAVAQHVMALLLELASRPGDY
DTSTKNGDWSGQPDFCNIAFGQTELAGKTLGIIGFGGIGQEAARLGHAFGMRILAHAPRP
KPQPQWGTVEFADLGTVFAESDAISLHCPQTEENKEFVNAALLARMKPSAFIINTARGTL
INEGDLAKALEAGTIAGAGLDVLAQEPPAKDNPLMRAPNCLITPHVAWATLESRQRLMRM
TADNIRAFANGAPTNVVNGVS
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