SitesBLAST
Comparing WP_012755375.1 NCBI__GCF_000023185.1:WP_012755375.1 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)
35% identity, 88% coverage: 33:316/324 of query aligns to 37:327/334 of 5aovA
- active site: L100 (≠ N94), R241 (= R229), D265 (= D253), E270 (≠ Q258), H288 (= H277)
- binding glyoxylic acid: M52 (vs. gap), L53 (≠ I47), L53 (≠ I47), Y74 (≠ H68), A75 (≠ G69), V76 (≠ A70), G77 (= G71), R241 (= R229), H288 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A70), T104 (≠ V98), F158 (≠ M148), G159 (= G149), R160 (≠ N150), I161 (≠ V151), S180 (= S171), R181 (= R172), A211 (≠ C199), V212 (≠ C200), P213 (= P201), T218 (= T206), I239 (≠ V227), A240 (≠ S228), R241 (= R229), H288 (= H277), G290 (≠ A279)
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
35% identity, 91% coverage: 9:303/324 of query aligns to 8:304/304 of 1wwkA
- active site: S96 (≠ N94), R230 (= R229), D254 (= D253), E259 (≠ Q258), H278 (= H277)
- binding nicotinamide-adenine-dinucleotide: V100 (= V98), G146 (= G147), F147 (≠ M148), G148 (= G149), R149 (≠ N150), I150 (≠ V151), Y168 (≠ T170), D169 (≠ S171), P170 (≠ R172), V201 (≠ C200), P202 (= P201), T207 (= T206), T228 (≠ V227), S229 (= S228), D254 (= D253), H278 (= H277), G280 (≠ A279)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
36% identity, 88% coverage: 33:316/324 of query aligns to 36:326/332 of 6biiA
- active site: L99 (≠ N94), R240 (= R229), D264 (= D253), E269 (≠ Q258), H287 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (≠ A70), T103 (≠ V98), G156 (= G147), F157 (≠ M148), G158 (= G149), R159 (≠ N150), I160 (≠ V151), A179 (≠ S171), R180 (= R172), S181 (= S173), K183 (vs. gap), V211 (≠ C200), P212 (= P201), E216 (= E205), T217 (= T206), V238 (= V227), A239 (≠ S228), R240 (= R229), D264 (= D253), H287 (= H277), G289 (≠ A279)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
34% identity, 96% coverage: 1:311/324 of query aligns to 2:312/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
34% identity, 96% coverage: 1:311/324 of query aligns to 1:311/526 of 3dc2A
Sites not aligning to the query:
7arzA Ternary complex of NAD-dependent formate dehydrogenase from physcomitrium patens
35% identity, 89% coverage: 15:302/324 of query aligns to 42:340/361 of 7arzA
- binding azide ion: T77 (≠ R48), P79 (= P50), F80 (≠ I51), L99 (≠ A65), V100 (≠ I66), T101 (≠ R67), G103 (= G69), V104 (≠ A70), R267 (= R229), H315 (= H277)
- binding nicotinamide-adenine-dinucleotide: V104 (≠ A70), N128 (= N94), V132 (= V98), G182 (= G149), R183 (≠ N150), I184 (≠ V151), D204 (≠ S171), R205 (= R172), T238 (≠ C200), P239 (= P201), Q243 (≠ E205), N265 (≠ V227), A266 (≠ S228), R267 (= R229), D291 (= D253), H315 (= H277), S317 (≠ A279), G318 (= G280)
Sites not aligning to the query:
6ttbA Crystal structure of NAD-dependent formate dehydrogenase from staphylococcus aureus in complex with NAD
35% identity, 77% coverage: 45:292/324 of query aligns to 57:307/331 of 6ttbA
- binding nicotinamide-adenine-dinucleotide: V87 (≠ A70), N111 (= N94), V115 (= V98), F162 (≠ V146), G165 (= G149), R166 (≠ N150), I167 (≠ V151), Y185 (≠ R172), D186 (≠ S173), P187 (= P174), H214 (≠ C199), A215 (≠ C200), P216 (= P201), T221 (= T206), T242 (≠ V227), A243 (≠ S228), R244 (= R229), H292 (= H277), S294 (≠ A279), G295 (= G280)
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
31% identity, 93% coverage: 4:303/324 of query aligns to 5:305/305 of 6plfA
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)
30% identity, 96% coverage: 4:315/324 of query aligns to 9:321/533 of O43175
- T78 (≠ A70) binding
- R135 (≠ A130) 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 (≠ NV 150:151) binding
- D175 (≠ S171) binding
- T207 (≠ C200) binding
- CAR 234:236 (≠ VSR 227:229) binding
- D260 (= D253) binding
- V261 (= V254) 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 (≠ HLAG 277:280) binding
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
7dkmA Phgdh covalently linked to oridonin (see paper)
31% identity, 92% coverage: 4:302/324 of query aligns to 5:304/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ A70), A102 (≠ V98), G148 (= G147), R151 (≠ N150), I152 (≠ V151), Y170 (≠ T170), D171 (≠ S171), P172 (vs. gap), I173 (vs. gap), H202 (≠ C199), T203 (≠ C200), P204 (= P201), T209 (= T206), C230 (≠ V227), A231 (≠ S228), R232 (= R229), H279 (= H277), G281 (≠ A279)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ A13), K17 (≠ S16), I18 (≠ M17), E293 (≠ T291)
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
31% identity, 92% coverage: 4:302/324 of query aligns to 4:303/303 of 6plgA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
32% identity, 89% coverage: 4:290/324 of query aligns to 4:291/301 of 6rj5A
2gsdA NAD-dependent formate dehydrogenase from bacterium moraxella sp.C2 in complex with NAD and azide (see paper)
33% identity, 86% coverage: 15:292/324 of query aligns to 60:347/399 of 2gsdA
- active site: N146 (= N94), R284 (= R229), D308 (= D253), Q313 (= Q258), H332 (= H277)
- binding azide ion: P97 (= P50), F98 (≠ I51), I122 (≠ A70), R284 (= R229), H332 (= H277)
- binding nicotinamide-adenine-dinucleotide: I122 (≠ A70), N146 (= N94), V150 (= V98), A198 (≠ G147), G200 (= G149), R201 (≠ N150), I202 (≠ V151), D221 (≠ A169), R222 (≠ T170), P256 (= P201), H258 (≠ T203), T261 (= T206), T282 (≠ V227), A283 (≠ S228), R284 (= R229), D308 (= D253), H332 (= H277), S334 (≠ A279), G335 (= G280)
Sites not aligning to the query:
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
32% identity, 89% coverage: 4:290/324 of query aligns to 4:291/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ V146), G147 (= G147), L148 (≠ M148), G149 (= G149), R150 (≠ N150), I151 (≠ V151), G152 (= G152), D170 (≠ S171), H201 (≠ C199), T202 (≠ C200), P203 (= P201)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
32% identity, 89% coverage: 4:290/324 of query aligns to 4:291/302 of 6rihA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
32% identity, 89% coverage: 4:290/324 of query aligns to 3:290/297 of 6rj3A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
32% identity, 89% coverage: 4:290/324 of query aligns to 3:290/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N94), A100 (≠ V98), R149 (≠ N150), I150 (≠ V151), Y168 (≠ T170), D169 (≠ S171), P170 (vs. gap), I171 (vs. gap), H200 (≠ C199), T201 (≠ C200), P202 (= P201), T207 (= T206), C228 (≠ V227), A229 (≠ S228), R230 (= R229), H277 (= H277), G279 (≠ A279)
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
32% identity, 89% coverage: 4:290/324 of query aligns to 1:288/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G149), I148 (≠ V151), Y166 (≠ T170), D167 (≠ S171), P168 (vs. gap), I169 (vs. gap), I170 (≠ R172), H198 (≠ C199), T199 (≠ C200), L208 (= L209), R228 (= R229)
2dbqA Crystal structure of glyoxylate reductase (ph0597) from pyrococcus horikoshii ot3, complexed with NADP (i41) (see paper)
33% identity, 97% coverage: 4:316/324 of query aligns to 5:327/333 of 2dbqA
- active site: L100 (≠ N94), R241 (= R229), D265 (= D253), E270 (≠ Q258), H288 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (≠ A70), T104 (≠ V98), L158 (≠ M148), G159 (= G149), R160 (≠ N150), I161 (≠ V151), S180 (= S171), R181 (= R172), T182 (≠ S173), A211 (≠ C199), V212 (≠ C200), P213 (= P201), T218 (= T206), I239 (≠ V227), A240 (≠ S228), R241 (= R229), D265 (= D253), 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)
33% identity, 97% coverage: 4:316/324 of query aligns to 5:327/334 of O58320
Query Sequence
>WP_012755375.1 NCBI__GCF_000023185.1:WP_012755375.1
MSFIFSTHPLHPAARSMLEAAGDLRVASAPDPETLLREGRGAGILVIRAPIPPAYFEDAP
ALRAAIRHGAGLDMVPMDAATRAGVLVANVPGANASTVAEHVFLVTLALLRRFRLMDREL
RQNGWVAGRARSDAAVDLAGRTIGIVGMGNVGKAIFKIAKFGFGLEVVATSRSPESVPDG
VRFLTIDELVATADIVVLCCPLTPETTGLLNAGRIGRMKPAAILVNVSRGPVIDDAALVE
ALRDGRVGGAALDVFATQPLPLDHPYFGFDNVIVTPHLAGLTEESMMRMGTGAASEALRV
IKGDLPVNLCNPEVVEHYRRRFPA
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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