SitesBLAST
Comparing WP_012706517.1 NCBI__GCF_000018545.1:WP_012706517.1 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)
34% identity, 87% coverage: 41:326/327 of query aligns to 37:332/334 of 5aovA
- active site: L100 (≠ N103), R241 (= R235), D265 (= D259), E270 (= E264), H288 (= H282)
- binding glyoxylic acid: M52 (≠ S56), L53 (vs. gap), L53 (vs. gap), Y74 (≠ V77), A75 (≠ G78), V76 (= V79), G77 (= G80), R241 (= R235), H288 (= H282)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V79), T104 (≠ V107), F158 (≠ A155), G159 (= G156), R160 (≠ I157), I161 (= I158), S180 (vs. gap), R181 (vs. gap), A211 (≠ H205), V212 (≠ A206), P213 (= P207), T218 (= T212), I239 (≠ T233), A240 (≠ S234), R241 (= R235), H288 (= H282), G290 (= G284)
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
34% identity, 88% coverage: 34:320/327 of query aligns to 32:321/533 of O43175
- T78 (≠ V79) binding NAD(+)
- R135 (= R136) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ II 157:158) binding NAD(+)
- D175 (= D177) binding NAD(+)
- T207 (≠ A206) binding NAD(+)
- CAR 234:236 (≠ TSR 233:235) binding NAD(+)
- D260 (= D259) binding NAD(+)
- V261 (= V260) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HIGG 282:285) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
34% identity, 84% coverage: 34:308/327 of query aligns to 28:305/305 of 6plfA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 27:289/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 27:289/303 of 6plgA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 27:289/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I153), G147 (= G154), L148 (≠ A155), G149 (= G156), R150 (≠ I157), I151 (= I158), G152 (= G159), D170 (= D177), H201 (= H205), T202 (≠ A206), P203 (= P207)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 27:289/302 of 6rihA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 26:288/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N103), A100 (≠ V107), R149 (≠ I157), I150 (= I158), Y168 (≠ F176), D169 (= D177), P170 (≠ A178), I171 (≠ M179), H200 (= H205), T201 (≠ A206), P202 (= P207), T207 (= T212), C228 (≠ T233), A229 (≠ S234), R230 (= R235), H277 (= H282), G279 (= G284)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 26:288/297 of 6rj3A
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 24:286/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G156), I148 (= I158), Y166 (≠ F176), D167 (= D177), P168 (≠ A178), I169 (≠ M179), I170 (vs. gap), H198 (= H205), T199 (≠ A206), L208 (= L215), R228 (= R235)
7dkmA Phgdh covalently linked to oridonin (see paper)
35% identity, 80% coverage: 34:293/327 of query aligns to 28:290/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V79), A102 (≠ V107), G148 (= G154), R151 (≠ I157), I152 (= I158), Y170 (≠ F176), D171 (= D177), P172 (≠ A178), I173 (≠ M179), H202 (= H205), T203 (≠ A206), P204 (= P207), T209 (= T212), C230 (≠ T233), A231 (≠ S234), R232 (= R235), H279 (= H282), G281 (= G284)
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, 293
6cdfA Human ctbp1 (28-378) (see paper)
36% identity, 82% coverage: 52:320/327 of query aligns to 49:332/333 of 6cdfA
- binding 1,4-dihydronicotinamide adenine dinucleotide: T104 (≠ V107), G157 (= G154), R160 (≠ I157), V161 (≠ I158), Y179 (≠ F176), D180 (= D177), P181 (≠ A178), Y182 (≠ M179), H212 (= H205), C213 (≠ A206), N219 (≠ T212), T240 (= T233), A241 (≠ S234), R242 (= R235), H291 (= H282), W294 (≠ G285)
6v89A Human ctbp1 (28-375) in complex with amp (see paper)
36% identity, 82% coverage: 52:320/327 of query aligns to 48:331/332 of 6v89A
4u6sA Ctbp1 in complex with substrate phenylpyruvate (see paper)
36% identity, 81% coverage: 52:316/327 of query aligns to 48:324/328 of 4u6sA
- active site: S99 (≠ N103), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H282)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V107), G156 (= G154), G158 (= G156), R159 (≠ I157), V160 (≠ I158), Y178 (≠ F176), D179 (= D177), P180 (≠ A178), Y181 (≠ M179), H211 (= H205), C212 (≠ A206), G213 (≠ P207), N218 (≠ T212), T239 (= T233), A240 (≠ S234), R241 (= R235), H290 (= H282), W293 (≠ G285)
- binding 3-phenylpyruvic acid: Y51 (≠ V55), H52 (≠ S56), I73 (≠ V77), G74 (= G78), S75 (≠ V79), G76 (= G80), R241 (= R235), W293 (≠ G285), M302 (= M294)
4u6qA Ctbp1 bound to inhibitor 2-(hydroxyimino)-3-phenylpropanoic acid (see paper)
36% identity, 81% coverage: 52:316/327 of query aligns to 48:324/328 of 4u6qA
- active site: S99 (≠ N103), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H282)
- binding (2E)-2-(hydroxyimino)-3-phenylpropanoic acid: Y51 (≠ V55), I73 (≠ V77), G74 (= G78), S75 (≠ V79), G76 (= G80), R241 (= R235), H290 (= H282), W293 (≠ G285), M302 (= M294)
- binding 1,4-dihydronicotinamide adenine dinucleotide: S75 (≠ V79), T103 (≠ V107), G156 (= G154), R159 (≠ I157), V160 (≠ I158), Y178 (≠ F176), D179 (= D177), P180 (≠ A178), Y181 (≠ M179), H211 (= H205), C212 (≠ A206), G213 (≠ P207), N218 (≠ T212), T239 (= T233), A240 (≠ S234), R241 (= R235), H290 (= H282), W293 (≠ G285)
4lceA Ctbp1 in complex with substrate mtob (see paper)
36% identity, 81% coverage: 52:316/327 of query aligns to 47:323/327 of 4lceA
- active site: S98 (≠ N103), R240 (= R235), D264 (= D259), E269 (= E264), H289 (= H282)
- binding 4-(methylsulfanyl)-2-oxobutanoic acid: R71 (= R76), G73 (= G78), S74 (≠ V79), G75 (= G80), R240 (= R235), H289 (= H282), W292 (≠ G285)
- binding nicotinamide-adenine-dinucleotide: S74 (≠ V79), T102 (≠ V107), G155 (= G154), G157 (= G156), R158 (≠ I157), V159 (≠ I158), Y177 (≠ F176), D178 (= D177), P179 (≠ A178), Y180 (≠ M179), H210 (= H205), C211 (≠ A206), N214 (≠ L209), N217 (≠ T212), T238 (= T233), A239 (≠ S234), R240 (= R235), W292 (≠ G285)
1hl3A Ctbp/bars in ternary complex with NAD(h) and pidlskk peptide (see paper)
35% identity, 81% coverage: 52:316/327 of query aligns to 48:324/331 of 1hl3A
- active site: S99 (≠ N103), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H282)
- binding nicotinamide-adenine-dinucleotide: T103 (≠ V107), G158 (= G156), R159 (≠ I157), V160 (≠ I158), D179 (= D177), Y181 (≠ M179), H211 (= H205), C212 (≠ A206), G213 (≠ P207), N218 (≠ T212), T239 (= T233), A240 (≠ S234), R241 (= R235), D265 (= D259), H290 (= H282)
Sites not aligning to the query:
1hkuA Ctbp/bars: a dual-function protein involved in transcription corepression and golgi membrane fission (see paper)
35% identity, 81% coverage: 52:316/327 of query aligns to 48:324/331 of 1hkuA
- active site: S99 (≠ N103), R241 (= R235), D265 (= D259), E270 (= E264), H290 (= H282)
- binding nicotinamide-adenine-dinucleotide: S75 (≠ V79), T103 (≠ V107), G156 (= G154), G158 (= G156), R159 (≠ I157), V160 (≠ I158), Y178 (≠ F176), D179 (= D177), P180 (≠ A178), Y181 (≠ M179), C212 (≠ A206), N218 (≠ T212), T239 (= T233), A240 (≠ S234), R241 (= R235), H290 (= H282), W293 (≠ G285)
Sites not aligning to the query:
Q13363 C-terminal-binding protein 1; CtBP1; EC 1.1.1.- from Homo sapiens (Human) (see 4 papers)
36% identity, 83% coverage: 46:316/327 of query aligns to 67:349/440 of Q13363
- C134 (≠ A113) mutation to A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150.
- N138 (≠ G117) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150.
- R141 (= R120) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150.
- RR 141:142 (= RR 120:121) mutation to AA: Strongly reduces E1A binding; when associated with A-163 and A-171.
- L150 (≠ V129) mutation to A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141.
- R163 (vs. gap) 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 (= D177) 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 (= H282) 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)
35% identity, 83% coverage: 46:316/327 of query aligns to 56:338/430 of Q9Z2F5
- S89 (≠ V79) binding NAD(+)
- IGLGRV 169:174 (≠ IGAGII 153:158) binding NAD(+)
- G172 (= G156) mutation to E: Loss dimerization and of NAD binding.
- D193 (= D177) binding NAD(+)
- 226:232 (vs. 206:212, 14% identical) binding NAD(+)
- TAR 253:255 (≠ TSR 233:235) binding NAD(+)
- D279 (= D259) binding NAD(+)
Sites not aligning to the query:
- 41 A→E: Strongly reduces interaction with E1A.
- 55 V→R: Strongly reduces interaction with E1A.
Query Sequence
>WP_012706517.1 NCBI__GCF_000018545.1:WP_012706517.1
MARVFISWPGYSPRDEDTGARLIAAGHELVLRPKRGNRTADELATLLEDCDAAIVSTDPF
TREVLAGDRNLKVIARVGVGTDSIDHDAAKEFGVGISVTPGMNAETVADQTLAMILGLMR
RVVTQDQAVKAGRWDRVGEATPTELYRKTVGLIGAGIIGKAVIRRLLGFGVRVLYFDAMV
EKVHGAERCGSLDQLLGSSDIVSLHAPLLADTRELMNAARIALMPKGSYLINTSRGGLVQ
QPAVFAALRSGHLAGAALDVFEVEPPGAEALADVPNLIASAHIGGISTESIARMTRSATT
SVLSVLNGEIPDTVINPDALRERLAGA
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