SitesBLAST
Comparing HSERO_RS05330 FitnessBrowser__HerbieS:HSERO_RS05330 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)
5jo9A Structural characterization of the thermostable bradyrhizobium japonicum d-sorbitol dehydrogenase (see paper)
64% identity, 98% coverage: 5:241/243 of query aligns to 2:238/239 of 5jo9A
4nbuB Crystal structure of fabg from bacillus sp (see paper)
31% identity, 91% coverage: 5:224/243 of query aligns to 5:226/244 of 4nbuB
- active site: G18 (= G18), N111 (= N112), S139 (= S140), Q149 (≠ E150), Y152 (= Y153), K156 (= K157)
- binding acetoacetyl-coenzyme a: D93 (≠ G94), K98 (≠ D99), S139 (= S140), N146 (≠ T147), V147 (≠ Y148), Q149 (≠ E150), Y152 (= Y153), F184 (≠ P185), M189 (≠ L190), K200 (= K201)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G14 (= G14), N17 (≠ S17), G18 (= G18), I19 (= I19), D38 (= D38), F39 (≠ W39), V59 (≠ T60), D60 (≠ N61), V61 (≠ L62), N87 (= N88), A88 (= A89), G89 (= G90), I90 (≠ T91), T137 (= T138), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), F184 (≠ P185), T185 (≠ V186), T187 (≠ S188), M189 (≠ L190)
4bmsF Short chain alcohol dehydrogenase from ralstonia sp. Dsm 6428 in complex with NADPH
32% identity, 89% coverage: 5:221/243 of query aligns to 4:227/249 of 4bmsF
- active site: S137 (= S140), H147 (≠ E150), Y150 (= Y153), K154 (= K157), Q195 (≠ W194)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G14), N15 (≠ A16), S16 (= S17), I18 (= I19), R38 (≠ W39), R39 (≠ N40), A59 (≠ P57), D60 (≠ Q58), V61 (= V59), N87 (= N88), S88 (≠ A89), G89 (= G90), V110 (≠ L111), S137 (= S140), Y150 (= Y153), K154 (= K157), G181 (= G184), I183 (vs. gap), T185 (vs. gap), I187 (≠ V186)
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)
30% identity, 98% coverage: 3:239/243 of query aligns to 9:257/267 of Q05016
- N102 (= N88) binding
- Y168 (= Y153) binding
- K172 (= K157) binding
3rkuA Substrate fingerprint and the structure of NADP+ dependent serine dehydrogenase from saccharomyces cerevisiae complexed with NADP+
30% identity, 98% coverage: 3:239/243 of query aligns to 10:258/268 of 3rkuA
- active site: A107 (≠ Y92), N128 (= N112), S156 (= S140), Y169 (= Y153), K173 (= K157), N214 (≠ P195)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G14), S23 (≠ A16), G25 (= G18), I26 (= I19), R49 (≠ W39), R50 (≠ N40), D76 (≠ N61), I77 (≠ L62), N103 (= N88), A104 (= A89), G105 (= G90), K106 (≠ T91), S156 (= S140), Y169 (= Y153), K173 (= K157), P199 (= P183), G200 (= G184), V202 (= V186), T204 (vs. gap), E205 (vs. gap), F206 (≠ I187)
6ihhA Crystal structure of rasadh f12 from ralstonia.Sp in complex with NADPH and a6o
31% identity, 89% coverage: 5:221/243 of query aligns to 4:227/249 of 6ihhA
- binding (2R,3S)-2-ethyl-2-[(2E)-2-(6-methoxy-3,4-dihydro-2H-naphthalen-1-ylidene)ethyl]-3-oxidanyl-cyclopentan-1-one: S137 (= S140), H147 (≠ E150), Y150 (= Y153), L188 (≠ I187)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G13 (= G14), N15 (≠ A16), S16 (= S17), G17 (= G18), I18 (= I19), R38 (≠ W39), R39 (≠ N40), D60 (≠ Q58), V61 (= V59), N87 (= N88), S88 (≠ A89), G89 (= G90), V110 (≠ L111), T135 (= T138), S137 (= S140), Y150 (= Y153), K154 (= K157), P180 (= P183), G181 (= G184), A182 (vs. gap), I183 (vs. gap), T185 (vs. gap), S187 (≠ V186)
Sites not aligning to the query:
3rkrA Crystal structure of a metagenomic short-chain oxidoreductase (sdr) in complex with NADP (see paper)
30% identity, 97% coverage: 3:238/243 of query aligns to 1:219/221 of 3rkrA
- active site: G16 (= G18), S142 (= S140), Y155 (= Y153), K159 (= K157)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G12 (= G14), R15 (≠ S17), A36 (≠ D38), R37 (≠ W39), D38 (≠ N40), C61 (≠ T60), D62 (≠ N61), L63 (= L62), A90 (= A89), G91 (= G90), V92 (≠ T91), G93 (vs. gap)
6vspA Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
29% identity, 89% coverage: 8:223/243 of query aligns to 6:224/251 of 6vspA
- active site: G16 (= G18), S138 (= S140), Y151 (= Y153)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), N15 (≠ S17), G16 (= G18), M17 (≠ I19), D36 (= D38), W37 (= W39), W37 (= W39), A38 (≠ N40), I59 (≠ T60), D60 (≠ N61), V61 (≠ L62), N87 (= N88), A88 (= A89), G89 (= G90), V90 (≠ T91), V110 (≠ L111), T136 (= T138), S138 (= S140), Y151 (= Y153), K155 (= K157), P181 (= P183), S182 (≠ G184), L183 (≠ P185), V184 (= V186), T186 (≠ S188), N187 (≠ A189), M188 (≠ L190), T189 (≠ L191)
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)
29% identity, 89% coverage: 8:223/243 of query aligns to 6:224/251 of H9XP47
- N15 (≠ S17) binding
- M17 (≠ I19) binding
- D36 (= D38) binding
- D60 (≠ N61) binding
- V61 (≠ L62) binding
- N87 (= N88) binding
- S138 (= S140) binding ; binding
- V139 (= V141) mutation to Q: Retains 50% of activity with acetoin as substrate; when associated with A-247.
- S140 (≠ A142) binding
- Y151 (= Y153) binding ; binding ; binding
- K155 (= K157) binding
- V184 (= V186) binding
- T186 (≠ S188) binding
- RDK 197:199 (≠ LRK 199:201) mutation to SEAAGKPLGYGTET: Mimics longer alpha6 helix. Retains 3% of activity with acetoin as substrate.
Sites not aligning to the query:
- 247 Q→A: Retains 10% of activity with acetoin as substrate. Retains 50% of activity with acetoin as substrate; when associated with Q-139.
6xewA Structure of serratia marcescens 2,3-butanediol dehydrogenase (see paper)
29% identity, 89% coverage: 8:223/243 of query aligns to 6:224/251 of 6xewA
- active site: G16 (= G18), S138 (= S140), Y151 (= Y153)
- binding r,3-hydroxybutan-2-one: S138 (= S140), S140 (≠ A142), Y151 (= Y153)
- binding s,3-hydroxybutan-2-one: S138 (= S140), Y151 (= Y153), S182 (≠ G184)
- binding nicotinamide-adenine-dinucleotide: G12 (= G14), N15 (≠ S17), G16 (= G18), M17 (≠ I19), D36 (= D38), W37 (= W39), W37 (= W39), A38 (≠ N40), I59 (≠ T60), D60 (≠ N61), V61 (≠ L62), N87 (= N88), A88 (= A89), G89 (= G90), V110 (≠ L111), T136 (= T138), S138 (= S140), Y151 (= Y153), K155 (= K157), S182 (≠ G184), L183 (≠ P185), V184 (= V186), T186 (≠ S188), N187 (≠ A189), M188 (≠ L190), T189 (≠ L191)
6vspB Structure of serratia marcescens 2,3-butanediol dehydrogenase mutant q247a (see paper)
29% identity, 89% coverage: 8:223/243 of query aligns to 8:226/252 of 6vspB
8cwlA Cryo-em structure of human 15-pgdh in complex with small molecule sw222746 (see paper)
32% identity, 88% coverage: 7:220/243 of query aligns to 4:215/255 of 8cwlA
- binding 1,4-dihydronicotinamide adenine dinucleotide: G11 (= G14), Q14 (≠ S17), G15 (= G18), I16 (= I19), D35 (= D38), W36 (= W39), C62 (vs. gap), V64 (≠ A65), N90 (= N88), G92 (= G90), V93 (≠ T91), S137 (= S140), Y150 (= Y153), K154 (= K157), G183 (= G184), V185 (= V186), T187 (≠ S188), I189 (≠ L190)
- binding 2-methyl-6-[7-(piperidine-1-carbonyl)quinoxalin-2-yl]isoquinolin-1(2H)-one: S137 (= S140), L138 (≠ V141), A139 (= A142), M142 (≠ F145), Q147 (≠ E150), Y150 (= Y153), F184 (≠ P185), I193 (≠ L199), M212 (≠ A217)
Sites not aligning to the query:
P15428 15-hydroxyprostaglandin dehydrogenase [NAD(+)]; 15-PGDH; Eicosanoid/docosanoid dehydrogenase [NAD(+)]; Prostaglandin dehydrogenase 1; Short chain dehydrogenase/reductase family 36C member 1; EC 1.1.1.141; EC 1.1.1.-; EC 1.1.1.232 from Homo sapiens (Human) (see 5 papers)
32% identity, 88% coverage: 7:220/243 of query aligns to 5:216/266 of P15428
- 12:20 (vs. 14:22, 78% identical) binding
- DW 36:37 (= DW 38:39) binding
- CDV 63:65 (≠ -DA 64:65) binding
- N91 (= N88) binding
- A140 (= A142) to P: in COA; inactive; dbSNP:rs121434480
- Q148 (≠ E150) mutation to A: Loss of activity.; mutation Q->E,H,N: Reduced affinity for NAD and prostaglandin E2.
- Y151 (= Y153) mutation to A: Loss of activity.; mutation to F: Loss 15-hydroxyprostaglandin dehydrogenase activity.
- YCASK 151:155 (≠ YAGSK 153:157) binding
- K155 (= K157) mutation to Q: Loss 15-hydroxyprostaglandin dehydrogenase activity.
- VNT 186:188 (≠ VIS 186:188) binding
8cvnA Cryo-em structure of human 15-pgdh in complex with small molecule sw209415 (see paper)
32% identity, 88% coverage: 7:220/243 of query aligns to 5:216/256 of 8cvnA
- binding 1,4-dihydronicotinamide adenine dinucleotide: Q15 (≠ S17), I17 (= I19), D36 (= D38), W37 (= W39), V65 (≠ A65), N91 (= N88), G93 (= G90), V94 (≠ T91), S138 (= S140), K155 (= K157), P183 (= P183), V186 (= V186), T188 (≠ S188)
- binding 2-[butyl(oxidanyl)-$l^{3}-sulfanyl]-4-(2,3-dimethylimidazol-4-yl)-6-(1,3-thiazol-2-yl)thieno[2,3-b]pyridin-3-amine: N95 (≠ T100), S138 (= S140), Q148 (≠ E150), Y151 (= Y153), F185 (≠ P185), M213 (≠ A217)
Sites not aligning to the query:
1gegE Cryatal structure analysis of meso-2,3-butanediol dehydrogenase (see paper)
28% identity, 94% coverage: 8:236/243 of query aligns to 3:249/256 of 1gegE
- active site: G13 (= G18), S139 (= S140), Y152 (= Y153), K156 (= K157), V197 (vs. gap)
- binding alpha-D-glucopyranose: R63 (≠ A65), D64 (≠ E66), F67 (≠ A69), E123 (≠ A124)
- binding nicotinamide-adenine-dinucleotide: G9 (= G14), Q12 (≠ S17), I14 (= I19), D33 (= D38), Y34 (≠ W39), V58 (≠ T60), D59 (≠ N61), V60 (≠ L62), N86 (= N88), A87 (= A89), I109 (≠ L111), S139 (= S140), Y152 (= Y153), K156 (= K157), P182 (= P183), V185 (= V186), T187 (≠ S188), M189 (≠ L190)
2gdzA Crystal structure of 15-hydroxyprostaglandin dehydrogenase type1, complexed with NAD+ (see paper)
32% identity, 88% coverage: 7:220/243 of query aligns to 6:217/266 of 2gdzA
- active site: G17 (= G18), N108 (= N112), S139 (= S140), Y152 (= Y153), K156 (= K157)
- binding nicotinamide-adenine-dinucleotide: G13 (= G14), Q16 (≠ S17), G17 (= G18), I18 (= I19), D37 (= D38), W38 (= W39), C64 (vs. gap), D65 (= D64), V66 (≠ A65), N92 (= N88), G94 (= G90), V95 (≠ T91), I107 (≠ L111), S139 (= S140), Y152 (= Y153), K156 (= K157), P184 (= P183), F186 (≠ P185), V187 (= V186), T189 (≠ S188), I191 (≠ L190)
Q48436 Diacetyl reductase [(S)-acetoin forming]; Acetoin(diacetyl) reductase; AR; Meso-2,3-butanediol dehydrogenase; EC 1.1.1.304 from Klebsiella pneumoniae (see paper)
28% identity, 94% coverage: 8:236/243 of query aligns to 3:249/256 of Q48436
- 6:33 (vs. 11:38, 39% identical) binding
- D59 (≠ N61) binding
- K156 (= K157) binding
5ha5D Crystal structure of an NAD-bound oxidoreductase from brucella ovis
30% identity, 88% coverage: 8:221/243 of query aligns to 7:222/244 of 5ha5D
- active site: G17 (= G18), S142 (= S140), Y155 (= Y153), K159 (= K157)
- binding nicotinamide-adenine-dinucleotide: G13 (= G14), R16 (≠ S17), G17 (= G18), L18 (≠ I19), D37 (= D38), I38 (≠ W39), L62 (≠ T60), D63 (≠ N61), V64 (≠ L62), N90 (= N88), A91 (= A89), S142 (= S140), Y155 (= Y153), K159 (= K157), G186 (= G184), M188 (≠ V186), S190 (= S188)
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)
28% identity, 97% coverage: 5:239/243 of query aligns to 1027:1267/1270 of A0A1U8QWA2
- G1036 (= G14) 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 (= Y153) 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
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)
28% identity, 97% coverage: 5:239/243 of query aligns to 4:247/259 of Q9P7B4
- S42 (≠ K42) modified: Phosphoserine
- T43 (≠ A43) modified: Phosphothreonine
Query Sequence
>HSERO_RS05330 FitnessBrowser__HerbieS:HSERO_RS05330
MTQSLAGKIAVITGAASGIGLATTEKLLANGVTVVMVDWNAKALDELAARLGPQVIPQVT
NLLDAESCAAMAPEILKKVDHIDILYCNAGTYIGGELVDTTPEAIDKMLNLNVNAVMKNV
HAVAPHMMERKSGDIIVTCSVAGHFPTYWEPVYAGSKWAITCFVQTMRRQMIPHGVRVGQ
VSPGPVISALLADWPEENLRKAKESGSLIEPSEVADAVEYMLTRNRNVTIRDMLVLPTNF
DRV
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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