SitesBLAST
Comparing WP_051939384.1 NCBI__GCF_000744815.1:WP_051939384.1 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)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
35% identity, 79% coverage: 57:312/325 of query aligns to 54:306/525 of 3ddnB
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
33% identity, 72% coverage: 55:287/325 of query aligns to 51:282/304 of 1wwkA
- active site: S96 (≠ N100), R230 (= R236), D254 (= D259), E259 (≠ D264), H278 (= H283)
- binding nicotinamide-adenine-dinucleotide: V100 (= V104), G146 (≠ S152), F147 (≠ A153), G148 (≠ S154), R149 (≠ G155), I150 (= I156), Y168 (≠ H174), D169 (= D175), P170 (= P176), V201 (≠ T207), P202 (= P208), T207 (= T213), T228 (= T234), S229 (≠ A235), D254 (= D259), H278 (= H283), G280 (≠ A285)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
35% identity, 79% coverage: 57:312/325 of query aligns to 53:305/526 of 3dc2A
Sites not aligning to the query:
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 53:281/297 of 6rj3A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 53:281/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N100), A100 (≠ V104), R149 (≠ G155), I150 (= I156), Y168 (≠ H174), D169 (= D175), P170 (= P176), I171 (≠ F177), H200 (= H206), T201 (= T207), P202 (= P208), T207 (= T213), C228 (≠ T234), A229 (= A235), R230 (= R236), H277 (= H283), G279 (≠ A285)
7dkmA Phgdh covalently linked to oridonin (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 55:283/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ G76), A102 (≠ V104), G148 (≠ S152), R151 (≠ G155), I152 (= I156), Y170 (≠ H174), D171 (= D175), P172 (= P176), I173 (≠ F177), H202 (= H206), T203 (= T207), P204 (= P208), T209 (= T213), C230 (≠ T234), A231 (= A235), R232 (= R236), H279 (= H283), G281 (≠ A285)
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
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 55:283/305 of 6plfA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 54:282/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 54:282/303 of 6plgA
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 54:282/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (= L151), G147 (≠ S152), L148 (≠ A153), G149 (≠ S154), R150 (≠ G155), I151 (= I156), G152 (= G157), D170 (= D175), H201 (= H206), T202 (= T207), P203 (= P208)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 54:282/302 of 6rihA
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
31% identity, 71% coverage: 57:287/325 of query aligns to 51:279/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (≠ S154), I148 (= I156), Y166 (≠ H174), D167 (= D175), P168 (= P176), I169 (≠ F177), I170 (≠ V178), H198 (= H206), T199 (= T207), L208 (= L216), R228 (= R236)
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)
31% identity, 71% coverage: 57:287/325 of query aligns to 59:287/533 of O43175
- T78 (≠ G76) binding NAD(+)
- R135 (≠ A137) 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 (≠ GI 155:156) binding NAD(+)
- D175 (= D175) binding NAD(+)
- T207 (= T207) binding NAD(+)
- CAR 234:236 (≠ TAR 234:236) 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 (≠ HVAG 283:286) 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
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
31% identity, 70% coverage: 59:287/325 of query aligns to 47:273/292 of 6plfB
- binding 4-{(1S)-1-[(5-chloro-6-{[(5S)-2-oxo-1,3-oxazolidin-5-yl]methoxy}-1H-indole-2-carbonyl)amino]-2-hydroxyethyl}benzoic acid: R141 (≠ G155), Y160 (≠ H174), D161 (= D175), P162 (= P176), I164 (≠ V178), L179 (≠ I193), T193 (= T207), P194 (= P208), S198 (≠ Q212), L202 (= L216)
O13437 Formate dehydrogenase; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Candida boidinii (Yeast) (see 4 papers)
33% identity, 86% coverage: 35:315/325 of query aligns to 51:342/364 of O13437
- F69 (≠ G53) mutation to A: 2-fold decrease in substrate affinity for formate, but no significant change in affinity for NAD. A significant reduction in catalytic activity compared to the wild-type.
- N119 (= N100) mutation to A: 94-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type; when associated with A-311.; mutation to H: 80-fold decrease in substrate affinity for formate and a 1250-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type.
- I175 (= I156) mutation to A: 2-fold decrease in substrate affinity for formate and a 12-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type.
- Q197 (≠ F177) mutation to L: 4-fold decrease in substrate affinity for formate but no significant change in affinity for NAD compared to the wild-type.
- R258 (= R236) mutation to A: No catalytic activity.
- C262 (≠ V240) mutation to A: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, greater stability at a higher pH compared to the wild-type; when associated with S-23.; mutation to V: Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type; when associated with S-23. Great increase in substrate affinity for formate and NAD and 8 degrees Celsius decrease in thermal stability compared to the wild-type.
- Q287 (≠ D264) mutation to A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-311.; mutation to E: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with T-288. No significant decrease in substrate affinity for formate but a 4-fold decrease in substrate affinity for NAD and a significant reduction in catalytic activity compared to the wild-type, a more acidic pH is seen than in the wild-type, preventing formate binding by a single ionization of a group compared to that of the wild-type.
- P288 (= P265) mutation to T: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with E-287.
- H311 (= H283) mutation to A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-287. 93-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD, and a significant reduction in catalytic activity compared to the wild-type; when associated with A-119.; mutation to Q: 10-fold decrease in substrate affinity for formate and significant reduction in the catalytic activity compared to the wild-type.
- K328 (≠ L300) mutation to V: A 75% increase in substrate affinity for formate after 2 weeks and a 50% increase in affinity for NAD. However, after 4 months the affinity for formate increases 7-fold and affinity for NAD increases by 2 thirds. Retains 70% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius.
Sites not aligning to the query:
- 23 C→S: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, significantly more stable in the presence of CuCl(2); when associated with A-262. Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type, significantly more stable in the presence of CuCl(2); when associated with V-262. No significant change in affinity for formate or NAD, 5 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, and significantly more stable in the presence of CuCl(2).
- 47 K→E: Slight increase in substrate affinity for formate and also affinity for NAD increases by half after 2 weeks. Also after 4 months affinity for formate increases by more than half and affinity for NAD increases by more than half. Retains 84% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius.
- 360 K→A: Exhibits no change in substrate affinity for formate, but shows a 4-fold decrease in substrate affinity for NAD implying that L-360 side chain forms strong interactions with the cofactor. A higher reaction rate is observed at an acidic and basic pH values.
6d4bA Crystal structure of candida boidinii formate dehydrogenase v123a mutant complexed with NAD+ and azide
31% identity, 91% coverage: 19:315/325 of query aligns to 39:342/361 of 6d4bA
- binding azide ion: P68 (≠ W52), F69 (≠ G53), V93 (≠ T77), R258 (= R236), H311 (= H283)
- binding nicotinamide-adenine-dinucleotide: V93 (≠ T77), N119 (= N100), G173 (≠ S154), R174 (≠ G155), I175 (= I156), Y194 (≠ H174), D195 (= D175), Y196 (≠ P176), A229 (≠ T207), P230 (= P208), H232 (≠ L210), T235 (= T213), T256 (= T234), A257 (= A235), R258 (= R236), D282 (= D259), H311 (= H283), S313 (≠ A285), G314 (= G286)
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, 77% coverage: 37:287/325 of query aligns to 82:336/399 of 2gsdA
- active site: N146 (= N100), R284 (= R236), D308 (= D259), Q313 (≠ D264), H332 (= H283)
- binding azide ion: P97 (≠ W52), F98 (≠ G53), I122 (≠ T77), R284 (= R236), H332 (= H283)
- binding nicotinamide-adenine-dinucleotide: I122 (≠ T77), N146 (= N100), V150 (= V104), A198 (≠ S152), G200 (≠ S154), R201 (≠ G155), I202 (= I156), D221 (= D175), R222 (≠ P176), P256 (= P208), H258 (≠ L210), T261 (= T213), T282 (= T234), A283 (= A235), R284 (= R236), D308 (= D259), H332 (= H283), S334 (≠ A285), G335 (= G286)
Sites not aligning to the query:
7cvpA The crystal structure of human phgdh from biortus.
31% identity, 61% coverage: 90:287/325 of query aligns to 41:236/254 of 7cvpA
- binding nicotinamide-adenine-dinucleotide: G101 (≠ S152), G103 (≠ S154), R104 (≠ G155), I105 (= I156), Y123 (≠ H174), D124 (= D175), P125 (= P176), I126 (≠ F177), H155 (= H206), T156 (= T207), P157 (= P208), T162 (= T213), C183 (≠ T234), A184 (= A235), R185 (= R236), H232 (= H283), G234 (≠ A285)
7va1A Crystal structure of human 3-phosphoglycerate dehydrogenase in complex with gdd-04-35
31% identity, 58% coverage: 100:287/325 of query aligns to 1:186/193 of 7va1A
- binding 4-[(3-ethanoylphenyl)sulfamoyl]-~{N}-[4-(3-fluorophenyl)-1,3-thiazol-2-yl]benzamide: L50 (= L151), G53 (≠ S154), R57 (= R158), Y73 (≠ H174), D74 (= D175), P75 (= P176), I76 (≠ F177), I77 (≠ V178), T106 (= T207), P107 (= P208), L115 (= L216)
5ofwA Crystal structure of human 3-phosphoglycerate dehydrogenase in complex with 3-chloro-4-fluorobenzamide (see paper)
31% identity, 58% coverage: 99:287/325 of query aligns to 2:188/195 of 5ofwA
- active site: N3 (= N100), R137 (= R236), D161 (= D259), E166 (≠ D264), H184 (= H283)
- binding 3-chloranyl-4-fluoranyl-benzamide: G53 (≠ S152), Y75 (≠ H174), P77 (= P176), T108 (= T207), S113 (≠ Q212), T114 (= T213), L117 (= L216)
Query Sequence
>WP_051939384.1 NCBI__GCF_000744815.1:WP_051939384.1
MRGEVFGQLFPPTELARLRELVELTSEEALSGFGTPEARKALGEAELLITGWGCPPVDAE
ALAAAPRLRAVVHVAGTVRNHITEACWERGLRVSTAAAANGVPVAEYTLAMILLSQKRVL
ESARALRTEHRRPAWTADPRLGNFRRTVGILSASGIGRRVIGLLRPHDLEVLLHDPFVSP
EEAERLGARAVGIEELFAVSDTVSVHTPLLPQTVGLVSRELLALMPDGATLINTARGAVV
DQEALTAELLSGRLRAVLDVTVPDPLPPGSPLYGCPNVLLTPHVAGSLGGELLRMTELAL
GEIERLARGEEFAHRIRREDLGRTA
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