SitesBLAST
Comparing SMa1347 FitnessBrowser__Smeli:SMa1347 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)
5aovA Ternary crystal structure of pyrococcus furiosus glyoxylate hydroxypyruvate reductase in presence of glyoxylate (see paper)
35% identity, 85% coverage: 42:316/324 of query aligns to 48:327/334 of 5aovA
- active site: L100 (≠ N94), R241 (= R229), D265 (= D253), E270 (≠ Q258), H288 (= H277)
- binding glyoxylic acid: M52 (≠ I46), L53 (≠ V47), L53 (≠ V47), 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)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
36% identity, 94% coverage: 1:304/324 of query aligns to 2:304/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
36% identity, 94% coverage: 1:304/324 of query aligns to 1:303/526 of 3dc2A
Sites not aligning to the query:
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
34% identity, 91% coverage: 10:303/324 of query aligns to 9:304/304 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 (≠ N170), D169 (≠ S171), P170 (≠ R172), V201 (≠ C200), P202 (= P201), T207 (= T206), T228 (≠ V227), S229 (= S228), D254 (= D253), H278 (= H277), G280 (≠ A279)
2gsdA NAD-dependent formate dehydrogenase from bacterium moraxella sp.C2 in complex with NAD and azide (see paper)
32% identity, 83% coverage: 23:292/324 of query aligns to 69:347/399 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 (≠ N170), 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:
6biiA Crystal structure of pyrococcus yayanosii glyoxylate hydroxypyruvate reductase in complex with NADP and malonate (re-refinement of 5aow) (see paper)
35% identity, 85% coverage: 42:316/324 of query aligns to 47:326/332 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 (= A169), R180 (≠ N170), S181 (= S171), K183 (≠ S173), V211 (≠ C200), P212 (= P201), E216 (≠ K205), T217 (= T206), V238 (= V227), A239 (≠ S228), R240 (= R229), D264 (= D253), H287 (= H277), G289 (≠ A279)
7arzA Ternary complex of NAD-dependent formate dehydrogenase from physcomitrium patens
35% identity, 81% coverage: 29:292/324 of query aligns to 60:330/361 of 7arzA
- binding azide ion: T77 (≠ V47), P79 (= P50), F80 (≠ I51), L99 (≠ V65), V100 (= V66), 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 (≠ K205), N265 (≠ V227), A266 (≠ S228), R267 (= R229), D291 (= D253), H315 (= H277), S317 (≠ A279), G318 (= G280)
Sites not aligning to the query:
6t9wB Crystal structure of formate dehydrogenase fdh2 d222a/q223r enzyme from granulicella mallensis mp5actx8 in complex with NADP and azide.
34% identity, 79% coverage: 37:293/324 of query aligns to 85:348/383 of 6t9wB
- binding azide ion: P97 (= P50), F98 (≠ I51), G121 (= G69), I122 (≠ A70), H332 (= H277)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I122 (≠ A70), N146 (= N94), S147 (≠ A95), V150 (= V98), A198 (≠ G147), G200 (= G149), R201 (≠ N150), I202 (≠ V151), F220 (≠ V168), R222 (≠ N170), 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:
8bxxAA Formate dehydrogenase
33% identity, 79% coverage: 37:293/324 of query aligns to 85:348/370 of 8bxxAA
- 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), F220 (≠ V168), D221 (≠ A169), Q222 (≠ N170), P256 (= P201), H258 (≠ T203), T282 (≠ V227), A283 (≠ S228), R284 (= R229), D308 (= D253), H332 (= H277), S334 (≠ A279), G335 (= G280)
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
31% identity, 84% coverage: 33:303/324 of query aligns to 35:305/305 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)
31% identity, 84% coverage: 33:303/324 of query aligns to 39:309/533 of O43175
- T78 (≠ A70) binding
- R135 (≠ T127) 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 (≠ A169) 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
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
31% identity, 82% coverage: 33:298/324 of query aligns to 34:299/301 of 6rj5A
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
31% identity, 83% coverage: 33:302/324 of query aligns to 34:303/303 of 6plgA
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
32% identity, 81% coverage: 33:296/324 of query aligns to 33:296/297 of 6rj3A
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
31% identity, 82% coverage: 33:298/324 of query aligns to 34:299/302 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 (≠ N150), I151 (≠ V151), G152 (= G152), D170 (≠ A169), H201 (≠ C199), T202 (≠ C200), P203 (= P201)
7dkmA Phgdh covalently linked to oridonin (see paper)
31% identity, 83% coverage: 33:302/324 of query aligns to 35:304/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ A70), A102 (≠ V98), G148 (= G147), R151 (≠ N150), I152 (≠ V151), Y170 (≠ V168), D171 (≠ A169), P172 (≠ N170), I173 (≠ S171), 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: E293 (≠ K291)
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
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
31% identity, 82% coverage: 33:298/324 of query aligns to 34:299/302 of 6rihA
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
31% identity, 82% coverage: 33:298/324 of query aligns to 33:298/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N94), A100 (≠ V98), R149 (≠ N150), I150 (≠ V151), Y168 (≠ V168), D169 (≠ A169), P170 (≠ N170), I171 (≠ S171), 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)
31% identity, 82% coverage: 33:298/324 of query aligns to 31:296/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G149), I148 (≠ V151), Y166 (≠ V168), D167 (≠ A169), P168 (≠ N170), I169 (≠ S171), I170 (≠ R172), H198 (≠ C199), T199 (≠ C200), L208 (= L209), R228 (= R229)
Q65CJ7 Hydroxyphenylpyruvate reductase; HPPR; EC 1.1.1.237 from Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides) (see paper)
35% identity, 71% coverage: 59:289/324 of query aligns to 65:291/313 of Q65CJ7
Query Sequence
>SMa1347 FitnessBrowser__Smeli:SMa1347
MSFIFSTHRLHPDAEAMLKAASDLRVASAPDPETLLREGEGAEIVIVRAPIPPAFFGNVP
ALRAVVRHGAGLDMIPYDAATAAGVLIANVPAVNAPTVAEHVFMVTLALLRQFRPMDRDL
RNMGWSTGRAHSDRALDLAGRIMGVIGMGNVGKAVFRIAKYGFQLEIVANSRSPESLPDG
VRFLSVDDLLSTADIVVLCCPLTPKTTGLLSRERIARMKPGAILVNVSRGPVVDDAALIE
ALERGRIGGAALDVFSTQPLPPEHPYFRQDNVIVTPHLAGISEESMMRMGKGAAAEAIRV
MEGGLPVNLRNPEVVEHYRRRFPG
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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