SitesBLAST
Comparing HSERO_RS13420 FitnessBrowser__HerbieS:HSERO_RS13420 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)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
41% identity, 88% coverage: 36:308/310 of query aligns to 37:309/313 of Q65CJ7
3bazA Structure of hydroxyphenylpyruvate reductase from coleus blumei in complex with NADP+ (see paper)
41% identity, 88% coverage: 36:308/310 of query aligns to 35:307/311 of 3bazA
- active site: L98 (≠ N99), R230 (= R230), A251 (= A251), D254 (= D254), E259 (= E259), H277 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V74 (≠ A75), G149 (= G149), L150 (≠ M150), G151 (= G151), R152 (≠ N152), I153 (= I153), S172 (≠ N172), R173 (= R173), S174 (≠ K174), C201 (≠ A201), P202 (= P202), T207 (= T207), I228 (= I228), G229 (= G229), R230 (= R230), D254 (= D254), H277 (= H277), G279 (≠ A279)
5v7nA Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADP and 2-keto-d-gluconic acid (see paper)
44% identity, 79% coverage: 61:305/310 of query aligns to 57:304/319 of 5v7nA
- active site: L95 (≠ N99), R229 (= R230), D253 (= D254), E258 (= E259), H276 (= H277)
- binding 2-keto-D-gluconic acid: G70 (= G74), V71 (≠ A75), G72 (= G76), R229 (= R230), H276 (= H277), S279 (≠ G280), R285 (≠ I286)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V71 (≠ A75), V99 (= V103), L149 (≠ M150), G150 (= G151), R151 (≠ N152), I152 (= I153), T171 (≠ N172), R172 (= R173), V200 (≠ A201), P201 (= P202), S205 (≠ Q206), T206 (= T207), V227 (≠ I228), G228 (= G229), R229 (= R230), H276 (= H277), A278 (= A279)
5v6qB Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADP and malonate (see paper)
44% identity, 79% coverage: 61:305/310 of query aligns to 58:305/319 of 5v6qB
- active site: L96 (≠ N99), R230 (= R230), D254 (= D254), E259 (= E259), H277 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V72 (≠ A75), V100 (= V103), F148 (≠ V148), L150 (≠ M150), G151 (= G151), R152 (≠ N152), I153 (= I153), T172 (≠ N172), R173 (= R173), V201 (≠ A201), P202 (= P202), S206 (≠ Q206), T207 (= T207), V228 (≠ I228), G229 (= G229), R230 (= R230), H277 (= H277), A279 (= A279)
5v7gA Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with NADPH and oxalate (see paper)
44% identity, 79% coverage: 61:305/310 of query aligns to 56:303/317 of 5v7gA
- active site: L94 (≠ N99), R228 (= R230), D252 (= D254), E257 (= E259), H275 (= H277)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V70 (≠ A75), V98 (= V103), F146 (≠ V148), L148 (≠ M150), G149 (= G151), R150 (≠ N152), I151 (= I153), T170 (≠ N172), R171 (= R173), V199 (≠ A201), P200 (= P202), S204 (≠ Q206), T205 (= T207), V226 (≠ I228), G227 (= G229), R228 (= R230), H275 (= H277), A277 (= A279)
- binding oxalate ion: G69 (= G74), V70 (≠ A75), G71 (= G76), R228 (= R230), H275 (= H277)
5j23A Crystal structure of NADPH-dependent glyoxylate/hydroxypyruvate reductase smc04462 (smghrb) from sinorhizobium meliloti in complex with 2'-phospho-adp-ribose (see paper)
44% identity, 79% coverage: 61:305/310 of query aligns to 56:303/318 of 5j23A
- active site: L94 (≠ N99), R228 (= R230), D252 (= D254), E257 (= E259), H275 (= H277)
- binding [(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl [(2r,3s,4r,5r)-3,4,5-trihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate: V70 (≠ A75), L148 (≠ M150), G149 (= G151), R150 (≠ N152), I151 (= I153), T170 (≠ N172), R171 (= R173), P200 (= P202), S204 (≠ Q206), T205 (= T207), R228 (= R230)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
37% identity, 85% coverage: 36:297/310 of query aligns to 37:308/334 of 5aovA
- active site: L100 (≠ N99), R241 (= R230), D265 (= D254), E270 (= E259), H288 (= H277)
- binding glyoxylic acid: M52 (≠ N51), L53 (≠ G52), L53 (≠ G52), Y74 (≠ L73), A75 (≠ G74), V76 (≠ A75), G77 (= G76), R241 (= R230), H288 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A75), T104 (≠ V103), F158 (≠ M150), G159 (= G151), R160 (≠ N152), I161 (= I153), S180 (≠ N172), R181 (= R173), A211 (= A200), V212 (≠ A201), P213 (= P202), T218 (= T207), I239 (= I228), A240 (≠ G229), R241 (= R230), H288 (= H277), G290 (≠ A279)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
36% identity, 78% coverage: 36:278/310 of query aligns to 36:288/332 of 6biiA
- active site: L99 (≠ N99), R240 (= R230), D264 (= D254), E269 (= E259), H287 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ A75), T103 (≠ V103), G156 (= G149), F157 (≠ M150), G158 (= G151), R159 (≠ N152), I160 (= I153), A179 (≠ N172), R180 (= R173), S181 (≠ K174), K183 (≠ R176), V211 (≠ A201), P212 (= P202), E216 (≠ Q206), T217 (= T207), V238 (≠ I228), A239 (≠ G229), R240 (= R230), D264 (= D254), H287 (= H277)
Sites not aligning to the query:
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
32% identity, 91% coverage: 1:282/310 of query aligns to 1:293/333 of 2dbqA
- active site: L100 (≠ N99), R241 (= R230), D265 (= D254), E270 (= E259), H288 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A75), T104 (≠ V103), L158 (≠ M150), G159 (= G151), R160 (≠ N152), I161 (= I153), S180 (≠ N172), R181 (= R173), T182 (≠ K174), A211 (= A200), V212 (≠ A201), P213 (= P202), T218 (= T207), I239 (= I228), A240 (≠ G229), R241 (= R230), D265 (= D254), H288 (= H277), G290 (≠ A279)
O58320 Glyoxylate reductase; EC 1.1.1.26 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
32% identity, 91% coverage: 1:282/310 of query aligns to 1:293/334 of O58320
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 85% coverage: 21:285/310 of query aligns to 20:286/304 of 1wwkA
- active site: S96 (≠ N99), R230 (= R230), D254 (= D254), E259 (= E259), H278 (= H277)
- binding nicotinamide-adenine-dinucleotide: V100 (= V103), G146 (= G149), F147 (≠ M150), G148 (= G151), R149 (≠ N152), I150 (= I153), Y168 (vs. gap), D169 (vs. gap), P170 (vs. gap), V201 (≠ A201), P202 (= P202), T207 (= T207), T228 (≠ I228), S229 (≠ G229), D254 (= D254), H278 (= H277), G280 (≠ A279)
6ttbA Crystal structure of NAD-dependent formate dehydrogenase from staphylococcus aureus in complex with NAD
31% identity, 81% coverage: 56:306/310 of query aligns to 68:320/331 of 6ttbA
- binding nicotinamide-adenine-dinucleotide: V87 (≠ A75), N111 (= N99), V115 (= V103), F162 (≠ V148), G165 (= G151), R166 (≠ N152), I167 (= I153), Y185 (≠ C171), D186 (≠ N172), P187 (≠ R173), H214 (≠ A200), A215 (= A201), P216 (= P202), T221 (= T207), T242 (≠ I228), A243 (≠ G229), R244 (= R230), H292 (= H277), S294 (≠ A279), G295 (= G280)
2gsdA NAD-dependent formate dehydrogenase from bacterium moraxella sp.C2 in complex with NAD and azide (see paper)
33% identity, 73% coverage: 56:282/310 of query aligns to 103:337/399 of 2gsdA
- active site: N146 (= N99), R284 (= R230), D308 (= D254), Q313 (≠ E259), H332 (= H277)
- binding azide ion: I122 (≠ A75), R284 (= R230), H332 (= H277)
- binding nicotinamide-adenine-dinucleotide: I122 (≠ A75), N146 (= N99), V150 (= V103), A198 (≠ G149), G200 (= G151), R201 (≠ N152), I202 (= I153), D221 (≠ N172), R222 (= R173), P256 (= P202), H258 (≠ G204), T261 (= T207), T282 (≠ I228), A283 (≠ G229), R284 (= R230), D308 (= D254), H332 (= H277), S334 (≠ A279), G335 (= G280)
Sites not aligning to the query:
4xyeA Granulicella m. Formate dehydrogenase (fdh) in complex with NAD(+) (see paper)
34% identity, 73% coverage: 56:282/310 of query aligns to 103:337/384 of 4xyeA
- active site: N146 (= N99), R284 (= R230), D308 (= D254), Q313 (≠ E259), H332 (= H277)
- binding nicotinamide-adenine-dinucleotide: I122 (≠ A75), N146 (= N99), V150 (= V103), A198 (≠ G149), G200 (= G151), R201 (≠ N152), I202 (= I153), A221 (≠ N172), R222 (= R173), A255 (= A201), P256 (= P202), Y258 (≠ G204), R284 (= R230), H332 (= H277), G335 (= G280)
Sites not aligning to the query:
4xybA Granulicella m. Formate dehydrogenase (fdh) in complex with NADP(+) and nan3 (see paper)
34% identity, 73% coverage: 56:282/310 of query aligns to 103:337/384 of 4xybA
- active site: N146 (= N99), R284 (= R230), D308 (= D254), Q313 (≠ E259), H332 (= H277)
- binding azide ion: I122 (≠ A75), R284 (= R230), H332 (= H277)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I122 (≠ A75), N146 (= N99), V150 (= V103), A198 (≠ G149), G200 (= G151), R201 (≠ N152), I202 (= I153), R222 (= R173), H223 (≠ K174), P256 (= P202), Y258 (≠ G204), T261 (= T207), T282 (≠ I228), A283 (≠ G229), R284 (= R230), D308 (= D254), H332 (= H277), S334 (≠ A279), G335 (= G280)
Sites not aligning to the query:
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
32% identity, 91% coverage: 3:285/310 of query aligns to 3:286/525 of 3ddnB
Sites not aligning to the query:
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
32% identity, 91% coverage: 3:285/310 of query aligns to 2:285/526 of 3dc2A
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)
29% identity, 80% coverage: 56:304/310 of query aligns to 70:348/430 of Q9Z2F5
- S89 (≠ A75) binding
- IGLGRV 169:174 (≠ VGMGNI 148:153) binding
- G172 (= G151) mutation to E: Loss dimerization and of NAD binding.
- D193 (≠ N172) binding
- 226:232 (vs. 201:207, 0% identical) binding
- TAR 253:255 (≠ IGR 228:230) binding
- D279 (= D254) 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)
30% identity, 80% coverage: 56:304/310 of query aligns to 81:359/440 of Q13363
- C134 (≠ G109) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ A113) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R116) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (≠ RN 116:117) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ T125) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (= R131) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171.
- R171 (≠ Q139) mutation to A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163.
- G181 (= G149) mutation to V: Strongly reduces E1A binding; when associated with V-183 and A-204.
- G183 (= G151) 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 (= G154) mutation to A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183.
- D204 (≠ N172) 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 (= R230) mutation to A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315.
- D290 (= D254) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315.
- E295 (= E259) mutation to A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315.
- H315 (= H277) 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)
6cdfA Human ctbp1 (28-378) (see paper)
30% identity, 74% coverage: 56:285/310 of query aligns to 57:299/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V103), G157 (= G149), R160 (≠ N152), V161 (≠ I153), Y179 (≠ C171), D180 (≠ N172), P181 (≠ R173), Y182 (≠ K174), H212 (≠ A200), C213 (≠ A201), N219 (≠ T207), T240 (≠ I228), A241 (≠ G229), R242 (= R230), H291 (= H277), W294 (≠ G280)
Query Sequence
>HSERO_RS13420 FitnessBrowser__HerbieS:HSERO_RS13420
MKPPLLVLIHLSEESTATIAAHYDILYAPDRQRRDEMIAGPARKVAVVLTNGSTGLTAEE
MRALPHLQLVCTLGAGFENVDVAHAEAHGIEIATGAGTNEDCVADHALGLLLAILRNIPV
LDRYTRDGGWRETIPLQPQLAGKRVGIVGMGNIGKKIARRAAAFDAEIAYCNRKKRDDVD
YHYFPDVAQLAGWADCLIVAAPGGAQTRHLINARVLEELGPQGYLVNIGRGSIVDTDALG
AALSSGRLAGAGLDVYEGEPQPPAALIALPNVVLTPHIAGWSPEAIRASVTQFLRNCEEH
FAAAEPVLRA
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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