SitesBLAST
Comparing WP_013644025.1 NCBI__GCF_000191585.1:WP_013644025.1 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)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
37% identity, 96% coverage: 5:507/525 of query aligns to 4:507/526 of 3dc2A
- active site: N96 (≠ T97), R230 (= R231), D254 (= D255), E259 (= E260), H277 (= H278)
- binding serine: Y458 (= Y458), D460 (= D460), R461 (≠ K461), P462 (= P462), G463 (= G463), A464 (≠ V464), L465 (≠ I465), L484 (≠ V484)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
37% identity, 96% coverage: 5:507/525 of query aligns to 5:506/525 of 3ddnB
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)
40% identity, 78% coverage: 3:413/525 of query aligns to 7:418/533 of O43175
- T78 (≠ V73) binding NAD(+)
- R135 (≠ K130) 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 (= RI 150:151) binding NAD(+)
- D175 (= D170) binding NAD(+)
- T207 (≠ V202) binding NAD(+)
- CAR 234:236 (= CAR 229:231) binding NAD(+)
- D260 (= D255) binding NAD(+)
- V261 (= V256) 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 (≠ HIAA 278:281) binding NAD(+)
- A373 (≠ M369) to T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- G377 (≠ E373) to S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 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
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
52% identity, 57% coverage: 4:304/525 of query aligns to 2:304/304 of 1wwkA
- active site: S96 (≠ T97), R230 (= R231), D254 (= D255), E259 (= E260), H278 (= H278)
- binding nicotinamide-adenine-dinucleotide: V100 (= V101), G146 (= G147), F147 (≠ M148), G148 (= G149), R149 (= R150), I150 (= I151), Y168 (= Y169), D169 (= D170), P170 (= P171), V201 (= V202), P202 (= P203), T207 (= T208), T228 (≠ C229), S229 (≠ A230), D254 (= D255), H278 (= H278), G280 (≠ A280)
7dkmA Phgdh covalently linked to oridonin (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 3:288/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ V73), A102 (≠ V101), G148 (= G147), R151 (= R150), I152 (= I151), Y170 (= Y169), D171 (= D170), P172 (= P171), I173 (≠ Y172), H202 (= H201), T203 (≠ V202), P204 (= P203), T209 (= T208), C230 (= C229), A231 (= A230), R232 (= R231), H279 (= H278), G281 (≠ A280)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ K14), K17 (≠ D17), I18 (≠ E18)
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: 293
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 3:288/305 of 6plfA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 1:286/297 of 6rj3A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 1:286/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (≠ T97), A100 (≠ V101), R149 (= R150), I150 (= I151), Y168 (= Y169), D169 (= D170), P170 (= P171), I171 (≠ Y172), H200 (= H201), T201 (≠ V202), P202 (= P203), T207 (= T208), C228 (= C229), A229 (= A230), R230 (= R231), H277 (= H278), G279 (≠ A280)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 2:287/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I146), G147 (= G147), L148 (≠ M148), G149 (= G149), R150 (= R150), I151 (= I151), G152 (= G152), D170 (= D170), H201 (= H201), T202 (≠ V202), P203 (= P203)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 2:287/302 of 6rihA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 2:287/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
47% identity, 54% coverage: 3:287/525 of query aligns to 2:287/303 of 6plgA
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
47% identity, 54% coverage: 5:287/525 of query aligns to 1:284/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G149), I148 (= I151), Y166 (= Y169), D167 (= D170), P168 (= P171), I169 (≠ Y172), I170 (= I173), H198 (= H201), T199 (≠ V202), L208 (= L211), R228 (= R231)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
44% identity, 54% coverage: 3:287/525 of query aligns to 1:278/292 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 (= R150), Y160 (= Y169), D161 (= D170), P162 (= P171), I164 (= I173), L179 (= L188), T193 (≠ V202), P194 (= P203), S198 (≠ E207), L202 (= L211)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
38% identity, 60% coverage: 1:316/525 of query aligns to 1:326/334 of 5aovA
- active site: L100 (≠ T97), R241 (= R231), D265 (= D255), E270 (= E260), H288 (= H278)
- binding glyoxylic acid: M52 (≠ R49), L53 (≠ S50), L53 (≠ S50), Y74 (≠ A71), A75 (≠ G72), V76 (= V73), G77 (= G74), R241 (= R231), H288 (= H278)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V76 (= V73), T104 (≠ V101), F158 (≠ M148), G159 (= G149), R160 (= R150), I161 (= I151), S180 (≠ D170), R181 (≠ P171), A211 (≠ H201), V212 (= V202), P213 (= P203), T218 (= T208), I239 (≠ C229), A240 (= A230), R241 (= R231), H288 (= H278), G290 (≠ A280)
2eklA Structure of st1218 protein from sulfolobus tokodaii
41% identity, 55% coverage: 4:291/525 of query aligns to 6:295/312 of 2eklA
- active site: S100 (≠ T97), R232 (= R231), D256 (= D255), E261 (= E260), H282 (= H278)
- binding nicotinamide-adenine-dinucleotide: I76 (≠ V73), S100 (≠ T97), G148 (= G147), G150 (= G149), R151 (= R150), I152 (= I151), Y170 (= Y169), D171 (= D170), I172 (≠ P171), L173 (≠ Y172), H202 (= H201), V203 (= V202), T204 (≠ P203), I212 (≠ L211), T230 (≠ C229), S231 (≠ A230), D256 (= D255), G284 (≠ A280)
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
37% identity, 60% coverage: 4:316/525 of query aligns to 3:325/332 of 6biiA
- active site: L99 (≠ T97), R240 (= R231), D264 (= D255), E269 (= E260), H287 (= H278)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: V75 (= V73), T103 (≠ V101), G156 (= G147), F157 (≠ M148), G158 (= G149), R159 (= R150), I160 (= I151), A179 (≠ D170), R180 (≠ P171), S181 (≠ Y172), K183 (≠ T174), V211 (= V202), P212 (= P203), E216 (= E207), T217 (= T208), V238 (≠ C229), A239 (= A230), R240 (= R231), D264 (= D255), H287 (= H278), G289 (≠ A280)
7cvpA The crystal structure of human phgdh from biortus.
42% identity, 47% coverage: 39:287/525 of query aligns to 18:241/254 of 7cvpA
- binding nicotinamide-adenine-dinucleotide: G101 (= G147), G103 (= G149), R104 (= R150), I105 (= I151), Y123 (= Y169), D124 (= D170), P125 (= P171), I126 (≠ Y172), H155 (= H201), T156 (≠ V202), P157 (= P203), T162 (= T208), C183 (= C229), A184 (= A230), R185 (= R231), H232 (= H278), G234 (≠ A280)
P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
36% identity, 60% coverage: 2:314/525 of query aligns to 55:380/466 of P87228
- S87 (= S32) modified: Phosphoserine
- S258 (≠ T205) modified: Phosphoserine
6rj6A Crystal structure of phgdh in complex with bi-4924 (see paper)
46% identity, 36% coverage: 98:287/525 of query aligns to 3:192/204 of 6rj6A
- binding 2-[4-[(1~{S})-1-[[4,5-bis(chloranyl)-1,6-dimethyl-indol-2-yl]carbonylamino]-2-oxidanyl-ethyl]phenyl]sulfonylethanoic acid: G52 (= G147), R55 (= R150), I56 (= I151), Y74 (= Y169), D75 (= D170), P76 (= P171), I77 (≠ Y172), I78 (= I173), H106 (= H201), T107 (≠ V202), P108 (= P203), T113 (= T208)
Query Sequence
>WP_013644025.1 NCBI__GCF_000191585.1:WP_013644025.1
MDKKVLIADQINEKGIDELKDVAEIVSNFTISKEELVKEIADYDAIIVRSRTKVTREVIE
AADKLKIIARAGVGVDNVDVQAATERGIMVINAPESTSITVAEHTMGLILSLSRKISIAD
SSVKDGKWEKSRFMGIELNGKTLGVIGMGRIGSQVVTRSKAFGMETVVYDPYITEKSASE
LGVTVVDLETLLKESDVMTIHVPLTPETKHLISKPQFEIMKENAIIINCARGGIINEEDL
YEALSNNRIRGAGLDVYEVEPPENSPLFTLDNVVLTPHIAASTSEAQRDAAIIVANEIKK
VFQGRSPKNVLNMPVLDPETFSMVKPYFGLIEKIGKFMIQTAKGNIKEIDVTYCGDLSEL
RKHDILTRMILQEVLNPILTEPVNLVNATSVAEKRGIIVTEGKRCDAKGYKNLIKVEMKS
DFNDVSIEGIMADEPKIIMINGYQVDVETEGTMLISKYKDKPGVIGAIGTKIGKHNINIA
KMQVGRKELGGEAVMVLKVDQQVPLNVIEELKQLEDVNDAVAVNL
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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