SitesBLAST
Comparing BWI76_RS02840 FitnessBrowser__Koxy:BWI76_RS02840 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)
P42412 Malonate-semialdehyde dehydrogenase; MSA dehydrogenase; Methylmalonate-semialdehyde dehydrogenase; MMSA dehydrogenase; MMSDH; MSDH; EC 1.2.1.27 from Bacillus subtilis (strain 168) (see 3 papers)
44% identity, 96% coverage: 1:485/503 of query aligns to 1:481/487 of P42412
- C36 (≠ A36) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-160; A-287; A-351 and A-413.
- R107 (≠ K107) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ V150) binding
- F152 (= F152) binding
- C160 (≠ M160) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-287; A-351 and A-413.
- K176 (= K177) binding
- E179 (≠ S180) binding
- R180 (≠ M181) binding
- S229 (= S230) binding
- T251 (≠ C252) binding
- R283 (= R284) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ L288) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-351 and A-413.
- C351 (≠ L352) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-413.
- E382 (= E386) binding
- C413 (≠ V417) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
44% identity, 96% coverage: 4:485/503 of query aligns to 2:479/484 of 1t90A
- active site: N151 (= N153), K174 (= K177), L248 (= L251), C282 (= C285), E380 (= E386), A460 (≠ C466)
- binding nicotinamide-adenine-dinucleotide: I147 (= I149), A148 (≠ V150), P149 (= P151), F150 (= F152), N151 (= N153), W159 (= W162), K174 (= K177), E177 (≠ S180), R178 (≠ M181), H207 (≠ R210), V225 (= V228), G226 (= G229), S227 (= S230), V230 (= V233), L248 (= L251), T249 (≠ C252), C282 (= C285), E380 (= E386), F382 (= F388)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
45% identity, 96% coverage: 1:485/503 of query aligns to 1:481/489 of 4zz7A
- active site: N149 (= N153), K172 (= K177), L246 (= L251), C280 (= C285), E382 (= E386), A462 (≠ C466)
- binding nicotinamide-adenine-dinucleotide: T146 (≠ V150), P147 (= P151), F148 (= F152), N149 (= N153), K172 (= K177), E175 (≠ S180), K205 (≠ R210), V208 (≠ A213), F222 (= F227), V223 (= V228), G224 (= G229), S225 (= S230), I228 (≠ V233), L246 (= L251), G247 (≠ C252), C280 (= C285), E382 (= E386), F384 (= F388)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
43% identity, 95% coverage: 7:485/503 of query aligns to 3:455/468 of 5tjrD
- active site: N144 (= N153), K167 (= K177), L241 (= L251), C270 (= C280), E356 (= E386), A436 (≠ C466)
- binding adenosine-5'-diphosphate: I140 (= I149), T141 (≠ V150), F143 (= F152), K167 (= K177), E170 (≠ S180), K200 (≠ R210), F217 (= F227), S220 (= S230), I223 (≠ V233)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
41% identity, 95% coverage: 7:485/503 of query aligns to 7:485/491 of 4iymC
- active site: N153 (= N153), K176 (= K177), F250 (≠ L251), C284 (= C285), E386 (= E386), Q466 (≠ C466)
- binding nicotinamide-adenine-dinucleotide: I149 (= I149), T150 (≠ V150), P151 (= P151), F152 (= F152), N153 (= N153), F154 (= F154), K176 (= K177), K209 (≠ R210), V212 (≠ A213), F226 (= F227), V227 (= V228), G228 (= G229), S229 (= S230), I232 (≠ V233), G251 (≠ C252), C284 (= C285), E386 (= E386), F388 (= F388)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
32% identity, 92% coverage: 27:491/503 of query aligns to 32:493/494 of P49189
- C116 (≠ G111) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
32% identity, 92% coverage: 27:491/503 of query aligns to 31:492/493 of 6vr6D
- active site: N156 (= N153), E253 (≠ L251), C287 (= C285), E467 (≠ L464)
- binding nicotinamide-adenine-dinucleotide: I152 (= I149), G153 (≠ V150), W155 (≠ F152), K179 (= K177), A212 (≠ R210), G215 (≠ A213), Q216 (≠ D214), F229 (= F227), G231 (= G229), S232 (= S230), T235 (≠ V233), I239 (≠ V237)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
32% identity, 91% coverage: 26:481/503 of query aligns to 40:492/503 of 1bpwA
- active site: N166 (= N153), K189 (= K177), E263 (≠ L251), C297 (= C285), E400 (= E386), E477 (≠ L464)
- binding nicotinamide-adenine-dinucleotide: I162 (= I149), L163 (≠ V150), W165 (≠ F152), N166 (= N153), K189 (= K177), G221 (≠ S209), G225 (≠ A213), T240 (≠ V228), G241 (= G229), S242 (= S230), T245 (≠ V233), E263 (≠ L251), L264 (≠ C252), C297 (= C285), E400 (= E386), F402 (= F388), F466 (= F453)
P56533 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABADH; Aldehyde dehydrogenase family 9 member A1; Betaine aldehyde dehydrogenase; BADH; EC 1.2.1.47; EC 1.2.1.3 from Gadus morhua subsp. callarias (Baltic cod) (Gadus callarias) (see paper)
32% identity, 91% coverage: 26:481/503 of query aligns to 40:492/503 of P56533
7radA Crystal structure analysis of aldh1b1
32% identity, 95% coverage: 4:482/503 of query aligns to 10:485/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I149), I159 (≠ V150), P160 (= P151), W161 (≠ F152), N162 (= N153), M167 (≠ P159), K185 (= K177), E188 (≠ S180), G218 (≠ R210), G222 (≠ D214), A223 (≠ I215), T237 (≠ V228), G238 (= G229), S239 (= S230), V242 (= V233), E261 (≠ L251), L262 (≠ C252), C295 (= C285), E392 (= E386), F394 (= F388)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ K107), F163 (= F154), E285 (≠ N275), F289 (≠ G279), N450 (≠ I444), V452 (= V446)
7mjdA Crystal structure analysis of aldh1b1
32% identity, 95% coverage: 4:482/503 of query aligns to 10:485/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I149), I159 (≠ V150), P160 (= P151), W161 (≠ F152), N162 (= N153), M167 (≠ P159), K185 (= K177), E188 (≠ S180), G218 (≠ R210), G222 (≠ D214), F236 (= F227), T237 (≠ V228), G238 (= G229), S239 (= S230), V242 (= V233), E261 (≠ L251), L262 (≠ C252), C295 (= C285), E392 (= E386), F394 (= F388)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ K107), E285 (≠ N275), F289 (≠ G279), N450 (≠ I444), V452 (= V446)
7mjcA Crystal structure analysis of aldh1b1
32% identity, 95% coverage: 4:482/503 of query aligns to 10:485/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I149), I159 (≠ V150), P160 (= P151), W161 (≠ F152), N162 (= N153), K185 (= K177), E188 (≠ S180), G218 (≠ R210), G222 (≠ D214), T237 (≠ V228), G238 (= G229), S239 (= S230), V242 (= V233), E261 (≠ L251), L262 (≠ C252), C295 (= C285), E392 (= E386), F394 (= F388)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
29% identity, 95% coverage: 6:481/503 of query aligns to 16:486/491 of 5gtlA
- active site: N165 (= N153), K188 (= K177), E263 (≠ L251), C297 (= C285), E394 (= E386), E471 (≠ C466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I149), P163 (= P151), K188 (= K177), A190 (= A179), E191 (≠ S180), Q192 (≠ M181), G221 (≠ R210), G225 (≠ D214), G241 (= G229), S242 (= S230), T245 (≠ V233), L264 (≠ C252), C297 (= C285), E394 (= E386), F396 (= F388)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
29% identity, 95% coverage: 6:481/503 of query aligns to 16:486/491 of 5gtkA
- active site: N165 (= N153), K188 (= K177), E263 (≠ L251), C297 (= C285), E394 (= E386), E471 (≠ C466)
- binding nicotinamide-adenine-dinucleotide: I161 (= I149), I162 (≠ V150), P163 (= P151), W164 (≠ F152), K188 (= K177), E191 (≠ S180), G221 (≠ R210), G225 (≠ D214), A226 (≠ I215), F239 (= F227), G241 (= G229), S242 (= S230), T245 (≠ V233), Y248 (≠ H236), L264 (≠ C252), C297 (= C285), Q344 (≠ H332), R347 (≠ S335), E394 (= E386), F396 (= F388)
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 95% coverage: 2:481/503 of query aligns to 18:493/503 of O14293
- S248 (= S230) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
7rluA Structure of aldh1l1 (10-formyltetrahydrofolate dehydrogenase) in complex with NADP (see paper)
31% identity, 95% coverage: 8:485/503 of query aligns to 104:583/583 of 7rluA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: K278 (= K177), S310 (= S209), G311 (≠ R210), G315 (≠ D214), G331 (= G229), S332 (= S230), V335 (= V233)
- binding 4'-phosphopantetheine: K201 (= K107), F382 (≠ G279), N387 (≠ R284), C388 (= C285), N545 (≠ I444)
4go2A Crystal structure of thE C-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with thio-NADP (see paper)
31% identity, 95% coverage: 8:485/503 of query aligns to 19:498/498 of 4go2A
- active site: N170 (= N153), K193 (= K177), E269 (≠ L251), C303 (= C285), E400 (= E386), D479 (≠ C466)
- binding 7-thionicotinamide-adenine-dinucleotide phosphate: V166 (≠ I149), I167 (≠ V150), P168 (= P151), W169 (≠ F152), K193 (= K177), A195 (= A179), Q196 (≠ S180), S225 (= S209), G226 (≠ R210), G230 (≠ D214), Q231 (≠ I215), F244 (= F227), G246 (= G229), S247 (= S230), V250 (= V233), I254 (≠ V237), E269 (≠ L251), G271 (≠ E253), C303 (= C285), E400 (= E386), F402 (= F388)
2o2rA Crystal structure of thE C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase in complex with NADPH (see paper)
31% identity, 95% coverage: 8:485/503 of query aligns to 19:498/498 of 2o2rA
- active site: N170 (= N153), K193 (= K177), E269 (≠ L251), C303 (= C285), E400 (= E386), D479 (≠ C466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V166 (≠ I149), I167 (≠ V150), W169 (≠ F152), K193 (= K177), A195 (= A179), Q196 (≠ S180), S225 (= S209), G226 (≠ R210), G230 (≠ D214), Q231 (≠ I215), F244 (= F227), S247 (= S230), V250 (= V233), I254 (≠ V237)
P28037 Cytosolic 10-formyltetrahydrofolate dehydrogenase; 10-FTHFDH; FDH; Aldehyde dehydrogenase family 1 member L1; FBP-CI; EC 1.5.1.6 from Rattus norvegicus (Rat) (see 5 papers)
31% identity, 95% coverage: 8:485/503 of query aligns to 423:902/902 of P28037
- IPW 571:573 (≠ VPF 150:152) binding
- KPAQ 597:600 (≠ KAAS 177:180) binding
- GSLVGQ 630:635 (≠ RNEADI 210:215) binding
- GS 650:651 (= GS 229:230) binding
- E673 (≠ L251) mutation to A: Loss of aldehyde dehydrogenase activity.
- EL 673:674 (≠ LC 251:252) binding
- C707 (= C285) mutation to A: Loss of formyltetrahydrofolate dehydrogenase activity. No effect on formyltetrahydrofolate hydrolase activity. No effect on NADP binding. No effect on homotetramerization.
- K757 (≠ S335) binding
- ESF 804:806 (≠ EIF 386:388) binding
Sites not aligning to the query:
- 142 Essential for catalytic activity; D→A: Loss of formyltetrahydrofolate dehydrogenase activity. Loss of formyltetrahydrofolate hydrolase activity. No effect on aldehyde dehydrogenase activity.
- 354 modified: O-(pantetheine 4'-phosphoryl)serine; S→A: Loss of phosphopantetheinylation. Loss of formyltetrahydrofolate dehydrogenase activity. No effect on hydrolase and aldehyde dehydrogenase activities in vitro.
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
29% identity, 87% coverage: 8:445/503 of query aligns to 4:440/494 of 5izdA
- active site: N149 (= N153), K172 (= K177), E247 (≠ L251), C281 (= C285), E381 (= E386)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I149), T146 (≠ V150), W148 (≠ F152), K172 (= K177), P173 (≠ A178), S174 (≠ A179), S175 (= S180), R204 (≠ S209), G205 (≠ R210), G209 (≠ A213), D210 (= D214), G225 (= G229), S226 (= S230), T229 (≠ V233)
Sites not aligning to the query:
Query Sequence
>BWI76_RS02840 FitnessBrowser__Koxy:BWI76_RS02840
MTTVPRLKYFVDGQWRVSQTERYMDVYNPSTGEVMAQAPCCTEQEVLDAVAAARKAFPAW
SDTPAIKRSQIMFRVRELLIQHQDRLTELVAKENGKAWGDAQGDVLKAKEGTELACSIPT
LMAGENLMDASAGIDTNLYREPIGVFAGIVPFNFPAMIPMGWMAPLCVASGNTMVIKAAS
MTPMTCMEITKLYQEAGVPDGVINVVTCSRNEADILLTHPDVNGVSFVGSTSVGLHVYSK
AAAHGKRVQALCEAKNHALVLADAPINRTAAGIINAAFGCAGERCMALPVVVVQEEIADK
LIAAVVEKAKQLKIGPGYLRDTDMGPVISKDHKRSVIGWINKGIEEGAKLVLDGRDIKVP
GQENGFYVGPTILDRVTEEMSVGTQEIFGPVLCFKRVKTFEEGLQLMNNNPFANGSVIFT
QSGYYAREFQKRTHGGMVGINVGIPVPVGVFPFSGHKQSFFGDLHCLGKDGVRFYTESKC
VTSRWFDEEEAKREKVDSWDGTI
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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