SitesBLAST
Comparing 207249 MicrobesOnline__882:207249 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)
3asvA The closed form of serine dehydrogenase complexed with NADP+ (see paper)
60% identity, 97% coverage: 5:249/253 of query aligns to 3:247/248 of 3asvA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G7 (= G9), T9 (= T11), G11 (= G13), F12 (= F14), R32 (= R34), R33 (= R35), D54 (= D57), V55 (= V58), N81 (= N84), G83 (= G86), I132 (≠ L135), S134 (= S137), Y147 (= Y150), K151 (= K154), G178 (= G181), V180 (vs. gap), T183 (≠ S185), E184 (= E186), F185 (= F187)
- binding phosphate ion: S134 (= S137), Y147 (= Y150), G178 (= G181), F185 (= F187)
6ixjA The crystal structure of sulfoacetaldehyde reductase from klebsiella oxytoca (see paper)
52% identity, 97% coverage: 5:249/253 of query aligns to 4:250/251 of 6ixjA
- binding 2-hydroxyethylsulfonic acid: S138 (= S137), Y145 (= Y144), Y151 (= Y150)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G8 (= G9), T10 (= T11), S11 (≠ A12), G12 (= G13), F13 (= F14), R33 (= R34), R34 (= R35), D57 (= D57), V58 (= V58), N84 (= N84), A85 (= A85), G86 (= G86), T108 (= T108), I136 (≠ L135), S138 (= S137), Y151 (= Y150), K155 (= K154), P181 (= P180), G182 (= G181), A184 (= A183), T186 (≠ S185), E187 (= E186), F188 (= F187)
Q9P7B4 NADP-dependent 3-hydroxy acid dehydrogenase; L-allo-threonine dehydrogenase; EC 1.1.1.381 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
45% identity, 98% coverage: 4:252/253 of query aligns to 8:259/259 of Q9P7B4
- S42 (≠ E37) modified: Phosphoserine
- T43 (≠ R38) modified: Phosphothreonine
Q05016 NADP-dependent 3-hydroxy acid dehydrogenase; L-allo-threonine dehydrogenase; EC 1.1.1.-; EC 1.1.1.381 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
37% identity, 95% coverage: 2:241/253 of query aligns to 13:259/267 of Q05016
- N102 (= N84) binding
- Y168 (= Y150) binding
- K172 (= K154) binding
3rkuA Substrate fingerprint and the structure of NADP+ dependent serine dehydrogenase from saccharomyces cerevisiae complexed with NADP+
37% identity, 95% coverage: 2:241/253 of query aligns to 14:260/268 of 3rkuA
- active site: A107 (= A88), N128 (= N109), S156 (= S137), Y169 (= Y150), K173 (= K154), N214 (≠ D195)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G9), S23 (≠ T11), G25 (= G13), I26 (≠ F14), R49 (= R34), R50 (= R35), D76 (= D57), I77 (≠ V58), N103 (= N84), A104 (= A85), G105 (= G86), K106 (≠ L87), S156 (= S137), Y169 (= Y150), K173 (= K154), P199 (= P180), G200 (= G181), V202 (≠ A183), T204 (≠ S185), E205 (= E186), F206 (= F187)
2ehdB Crystal structure analysis of oxidoreductase
36% identity, 94% coverage: 1:238/253 of query aligns to 3:213/213 of 2ehdB
2japA Clavulanic acid dehydrogenase: structural and biochemical analysis of the final step in the biosynthesis of the beta- lactamase inhibitor clavulanic acid (see paper)
42% identity, 93% coverage: 6:240/253 of query aligns to 9:244/245 of 2japA
- active site: S140 (= S137), Y153 (= Y150), K157 (= K154), A198 (= A200)
- binding (2r,3z,5r)-3-(2-hydroxyethylidene)-7-oxo-4-oxa-1-azabicyclo[3.2.0]heptane-2-carboxylic acid: M93 (≠ A88), S140 (= S137), A142 (= A139), Y153 (= Y150), T185 (≠ L182), Y203 (= Y203), R206 (vs. gap)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G12 (= G9), S14 (≠ T11), S15 (≠ A12), G16 (= G13), I17 (≠ F14), A36 (≠ G33), R37 (= R34), R38 (= R35), L61 (≠ F56), D62 (= D57), V63 (= V58), N89 (= N84), A90 (= A85), G91 (= G86), T112 (= T108), M138 (≠ L135), S139 (≠ G136), S140 (= S137), Y153 (= Y150), K157 (= K154), P183 (= P180), T185 (≠ L182), T186 (≠ A183), T188 (≠ S185), E189 (= E186), L190 (≠ F192)
2jahC Biochemical and structural analysis of the clavulanic acid dehydeogenase (cad) from streptomyces clavuligerus (see paper)
42% identity, 93% coverage: 6:240/253 of query aligns to 10:245/246 of 2jahC
- active site: S141 (= S137), Y154 (= Y150), K158 (= K154), A199 (= A200)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), S15 (≠ T11), S16 (≠ A12), G17 (= G13), I18 (≠ F14), A37 (≠ G33), R38 (= R34), R39 (= R35), D63 (= D57), V64 (= V58), N90 (= N84), A91 (= A85), G92 (= G86), T113 (= T108), M139 (≠ L135), S141 (= S137), Y154 (= Y150), K158 (= K154), P184 (= P180), G185 (= G181), T186 (≠ L182), T187 (≠ A183), T189 (≠ S185), E190 (= E186), L191 (≠ F192)
A0A1U8QWA2 Glycine betaine reductase ATRR; Nonribosomal peptide synthetase-like protein ATRR; EC 1.2.1.-; EC 1.1.1.- from Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) (see paper)
35% identity, 92% coverage: 6:237/253 of query aligns to 1033:1265/1270 of A0A1U8QWA2
- G1036 (= G9) mutation to A: Compromises binding of the cosubstrate NADPH to aldehyde reductase domain R2. Decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
- Y1178 (= Y150) mutation to F: Does not substantially affect carboxylic acid reductase activity but results to a 150-fold loss of aldehyde reductase activity and the accumulation of glycine betaine aldehyde intermediate. Further decreases the aldehyde reductase activity by 4,000-fold; when associated with F-1178.
Sites not aligning to the query:
- 14:418 Adenylation (A) domain
- 643:937 Carboxylic acid reductase domain R1
- 812 Y→F: Abolishes overall carboxylic acid reductase activity but does nor affect aldehyde reductase activity.
- 1026:1256 Aldehyde reductase domain R2
1xg5C Structure of human putative dehydrogenase mgc4172 in complex with nadp
32% identity, 92% coverage: 7:238/253 of query aligns to 15:255/257 of 1xg5C
- active site: S150 (= S137), Y165 (= Y150), K169 (= K154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G9), S19 (≠ T11), G21 (= G13), I22 (≠ F14), A41 (≠ G33), R42 (= R34), T43 (≠ R35), D69 (= D57), L70 (≠ V58), N96 (= N84), G98 (= G86), I148 (≠ L135), S150 (= S137), Y165 (= Y150), K169 (= K154), G198 (= G181), V200 (≠ A183), T202 (≠ S185), F204 (= F187), K207 (≠ I190)
3p19A Improved NADPH-dependent blue fluorescent protein (see paper)
33% identity, 95% coverage: 1:241/253 of query aligns to 1:238/239 of 3p19A
- active site: S132 (= S137), Y145 (= Y150), K149 (= K154)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G9 (= G9), S11 (≠ T11), S12 (≠ A12), G13 (= G13), I14 (≠ F14), A33 (≠ G33), R34 (= R34), R35 (= R35), D53 (= D57), V54 (= V58), N80 (= N84), A81 (= A85), G82 (= G86), I130 (≠ L135), S132 (= S137), Y145 (= Y150), K149 (= K154), P175 (= P180), A177 (≠ L182), V178 (≠ A183), T180 (≠ S185), E181 (= E186), L182 (≠ F187)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
34% identity, 73% coverage: 4:188/253 of query aligns to 7:189/251 of 6vspA
- active site: G16 (= G13), S138 (= S137), Y151 (= Y150)
- binding nicotinamide-adenine-dinucleotide: G12 (= G9), N15 (≠ A12), G16 (= G13), M17 (≠ F14), D36 (≠ G33), W37 (≠ R34), W37 (≠ R34), A38 (≠ R35), I59 (≠ F56), D60 (= D57), V61 (= V58), N87 (= N84), A88 (= A85), G89 (= G86), V90 (≠ L87), V110 (≠ T108), T136 (≠ L135), S138 (= S137), Y151 (= Y150), K155 (= K154), P181 (= P180), S182 (≠ G181), L183 (= L182), V184 (≠ A183), T186 (≠ S185), N187 (≠ E186), M188 (≠ F187), T189 (≠ S188)
H9XP47 Meso-2,3-butanediol dehydrogenase; BDH; meso-2,3-BDH; (R,S)-butane-2,3-diol dehydrogenase; NAD(H)-dependent meso-2,3-BDH; SmBdh; EC 1.1.1.- from Serratia marcescens (see paper)
34% identity, 73% coverage: 4:188/253 of query aligns to 7:189/251 of H9XP47
- N15 (≠ A12) binding
- M17 (≠ F14) binding
- D36 (≠ G33) binding
- D60 (= D57) binding
- V61 (= V58) binding
- N87 (= N84) binding
- S138 (= S137) binding ; binding
- V139 (≠ I138) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A139) binding
- Y151 (= Y150) binding ; binding ; binding
- K155 (= K154) binding
- V184 (≠ A183) binding
- T186 (≠ S185) binding
Sites not aligning to the query:
- 197:199 RDK→SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
34% identity, 73% coverage: 4:188/253 of query aligns to 9:191/252 of 6vspB
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
34% identity, 73% coverage: 4:188/253 of query aligns to 7:189/251 of 6xewA
- active site: G16 (= G13), S138 (= S137), Y151 (= Y150)
- binding r,3-hydroxybutan-2-one: S138 (= S137), S140 (≠ A139), Y151 (= Y150)
- binding s,3-hydroxybutan-2-one: S138 (= S137), Y151 (= Y150), S182 (≠ G181)
- binding nicotinamide-adenine-dinucleotide: G12 (= G9), N15 (≠ A12), G16 (= G13), M17 (≠ F14), D36 (≠ G33), W37 (≠ R34), W37 (≠ R34), A38 (≠ R35), I59 (≠ F56), D60 (= D57), V61 (= V58), N87 (= N84), A88 (= A85), G89 (= G86), V110 (≠ T108), T136 (≠ L135), S138 (= S137), Y151 (= Y150), K155 (= K154), S182 (≠ G181), L183 (= L182), V184 (≠ A183), T186 (≠ S185), N187 (≠ E186), M188 (≠ F187), T189 (≠ S188)
2cfcA Structural basis for stereo selectivity in the (r)- and (s)-hydroxypropylethane thiosulfonate dehydrogenases (see paper)
34% identity, 76% coverage: 1:192/253 of query aligns to 1:197/250 of 2cfcA
- active site: G13 (= G13), S142 (= S137), Y155 (= Y150), K159 (= K154)
- binding (2-[2-ketopropylthio]ethanesulfonate: F149 (≠ Y144), R152 (≠ G147), Y155 (= Y150), W195 (≠ I190), R196 (= R191)
- binding nicotinamide-adenine-dinucleotide: G9 (= G9), S12 (≠ A12), G13 (= G13), N14 (≠ F14), D33 (≠ G33), L34 (≠ R34), A59 (≠ F56), D60 (= D57), V61 (= V58), N87 (= N84), A88 (= A85), G89 (= G86), I140 (≠ L135), P185 (= P180), G186 (= G181), M187 (≠ L182), I188 (≠ A183), T190 (≠ S185), P191 (≠ E186), M192 (≠ F187), T193 (≠ S188)
Q56840 2-(R)-hydroxypropyl-CoM dehydrogenase; R-HPCDH; 2-[(R)-2-hydroxypropylthio]ethanesulfonate dehydrogenase; Aliphatic epoxide carboxylation component III; Epoxide carboxylase component III; RHPCDH1; EC 1.1.1.268 from Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2) (see 4 papers)
34% identity, 76% coverage: 1:192/253 of query aligns to 1:197/250 of Q56840
- M1 (= M1) modified: Initiator methionine, Removed
- SGN 12:14 (≠ AGF 12:14) binding
- D33 (≠ G33) binding
- DV 60:61 (= DV 57:58) binding
- N87 (= N84) binding
- S142 (= S137) mutation to A: Retains weak activity. 120-fold decrease in kcat.; mutation to C: Loss of activity.
- R152 (≠ G147) binding ; mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
- Y155 (= Y150) mutation Y->E,F: Loss of activity.
- K159 (= K154) mutation to A: Loss of activity.
- R179 (= R174) mutation to A: Loss of activity.
- IETPM 188:192 (≠ AESEF 183:187) binding
- WR 195:196 (≠ IR 190:191) binding
- R196 (= R191) mutation to A: Almost loss of activity with the natural substrate 2-KPC, but does not affect activity with 2-butanone as substrate.
Sites not aligning to the query:
- 203 R→A: Slight decrease in catalytic efficiency.
- 209 R→A: Does not affect catalytic efficiency.
5t2uA Short chain dehydrogenase/reductase family protein (see paper)
36% identity, 70% coverage: 4:181/253 of query aligns to 8:179/241 of 5t2uA
- active site: G17 (= G13), T135 (≠ S137), T145 (≠ G147), Y148 (= Y150), K152 (= K154)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G9), G17 (= G13), R38 (= R34), D39 (≠ R35), R42 (= R38), D60 (= D57), L61 (≠ V58), N83 (= N84), A84 (= A85), Y87 (≠ E92), I133 (≠ L135), T135 (≠ S137), Y148 (= Y150), K152 (= K154), P178 (= P180)
Sites not aligning to the query:
4nbuB Crystal structure of fabg from bacillus sp (see paper)
34% identity, 71% coverage: 6:185/253 of query aligns to 11:187/244 of 4nbuB
- active site: G18 (= G13), N111 (= N109), S139 (= S137), Q149 (≠ G147), Y152 (= Y150), K156 (= K154)
- binding acetoacetyl-coenzyme a: D93 (≠ G90), K98 (≠ R96), S139 (= S137), N146 (≠ Y144), V147 (≠ P145), Q149 (≠ G147), Y152 (= Y150), F184 (≠ L182)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G9), N17 (≠ A12), G18 (= G13), I19 (≠ F14), D38 (≠ R34), F39 (≠ R35), V59 (= V55), D60 (= D57), V61 (= V58), N87 (= N84), A88 (= A85), G89 (= G86), I90 (≠ L87), T137 (≠ L135), S139 (= S137), Y152 (= Y150), K156 (= K154), P182 (= P180), F184 (≠ L182), T185 (≠ A183), T187 (≠ S185)
Sites not aligning to the query:
3op4A Crystal structure of putative 3-ketoacyl-(acyl-carrier-protein) reductase from vibrio cholerae o1 biovar eltor str. N16961 in complex with NADP+ (see paper)
30% identity, 72% coverage: 6:188/253 of query aligns to 12:192/247 of 3op4A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G15 (= G9), S17 (≠ T11), R18 (≠ A12), I20 (≠ F14), T40 (≠ R34), N62 (≠ D57), V63 (= V58), N89 (= N84), A90 (= A85), I92 (≠ L87), V139 (≠ L135), S141 (= S137), Y154 (= Y150), K158 (= K154), P184 (= P180), G185 (= G181), I187 (≠ A183), T189 (≠ S185), M191 (≠ F187)
Query Sequence
>207249 MicrobesOnline__882:207249
MQATICITGATAGFGEACARRFAAEGCRLIITGRRKERLEKLAAELGEDRCLPLVFDVRD
RKAVEAAFAALPEAFANVDVLINNAGLALGLEPAHRASLEDWETMIDTNLKGLMYCTRAL
LPGMVERGKGHVVNLGSIAGSYPYPGGNTYGATKAFVMQFSRNLRADLHGTGVRVTNIEP
GLAESEFSVIRFKGDASKAAGVYKGTEPLRPVDIADIIHFAVTCPAHVNINRIEVMPTCQ
SFGALPVHRTEAD
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