SitesBLAST
Comparing WP_012383190.1 NCBI__GCF_000019845.1:WP_012383190.1 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)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
60% identity, 95% coverage: 15:500/509 of query aligns to 4:489/489 of 4zz7A
- active site: N149 (= N161), K172 (= K184), L246 (= L258), C280 (= C292), E382 (= E394), A462 (≠ M474)
- binding nicotinamide-adenine-dinucleotide: T146 (= T158), P147 (= P159), F148 (= F160), N149 (= N161), K172 (= K184), E175 (= E187), K205 (= K217), V208 (= V220), F222 (= F234), V223 (= V235), G224 (= G236), S225 (= S237), I228 (= I240), L246 (= L258), G247 (= G259), C280 (= C292), E382 (= E394), F384 (= F396)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
62% identity, 94% coverage: 15:494/509 of query aligns to 3:456/468 of 5tjrD
- active site: N144 (= N161), K167 (= K184), L241 (= L258), C270 (= C292), E356 (= E394), A436 (≠ M474)
- binding adenosine-5'-diphosphate: I140 (= I157), T141 (= T158), F143 (= F160), K167 (= K184), E170 (= E187), K200 (= K217), F217 (= F234), S220 (= S237), I223 (= I240)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
57% identity, 96% coverage: 9:498/509 of query aligns to 1:490/491 of 4iymC
- active site: N153 (= N161), K176 (= K184), F250 (≠ L258), C284 (= C292), E386 (= E394), Q466 (≠ M474)
- binding nicotinamide-adenine-dinucleotide: I149 (= I157), T150 (= T158), P151 (= P159), F152 (= F160), N153 (= N161), F154 (= F162), K176 (= K184), K209 (= K217), V212 (= V220), F226 (= F234), V227 (= V235), G228 (= G236), S229 (= S237), I232 (= I240), G251 (= G259), C284 (= C292), E386 (= E394), F388 (= F396)
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)
46% identity, 95% coverage: 12:494/509 of query aligns to 4:482/487 of P42412
- C36 (≠ R44) 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 (= R115) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T158) binding NAD(+)
- F152 (= F160) binding NAD(+)
- C160 (≠ M168) 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 (= K184) binding NAD(+)
- E179 (= E187) binding NAD(+)
- R180 (= R188) binding NAD(+)
- S229 (= S237) binding NAD(+)
- T251 (≠ G259) binding NAD(+)
- R283 (= R291) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I295) 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 (≠ V360) 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 (= E394) binding NAD(+)
- C413 (≠ A425) 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
46% identity, 95% coverage: 12:494/509 of query aligns to 2:480/484 of 1t90A
- active site: N151 (= N161), K174 (= K184), L248 (= L258), C282 (= C292), E380 (= E394), A460 (≠ M474)
- binding nicotinamide-adenine-dinucleotide: I147 (= I157), A148 (≠ T158), P149 (= P159), F150 (= F160), N151 (= N161), W159 (= W169), K174 (= K184), E177 (= E187), R178 (= R188), H207 (≠ K217), V225 (= V235), G226 (= G236), S227 (= S237), V230 (≠ I240), L248 (= L258), T249 (≠ G259), C282 (= C292), E380 (= E394), F382 (= F396)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
38% identity, 90% coverage: 19:475/509 of query aligns to 15:473/494 of 4pz2B
- active site: N159 (= N161), K182 (= K184), E258 (≠ L258), C292 (= C292), E392 (= E394), D469 (= D471)
- binding nicotinamide-adenine-dinucleotide: I155 (= I157), I156 (≠ T158), P157 (= P159), W158 (≠ F160), N159 (= N161), M164 (≠ V166), K182 (= K184), A184 (≠ S186), E185 (= E187), G215 (≠ D216), G219 (≠ V220), F233 (= F234), T234 (≠ V235), G235 (= G236), S236 (= S237), V239 (≠ I240), E258 (≠ L258), L259 (≠ G259), C292 (= C292), E392 (= E394), F394 (= F396)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
35% identity, 93% coverage: 14:488/509 of query aligns to 26:500/515 of 2d4eC
- active site: N173 (= N161), K196 (= K184), E271 (≠ L258), C305 (= C292), E409 (= E394), E486 (≠ M474)
- binding nicotinamide-adenine-dinucleotide: I169 (= I157), T170 (= T158), P171 (= P159), W172 (≠ F160), K196 (= K184), A198 (≠ S186), G229 (≠ D216), G233 (≠ V220), A234 (≠ D221), T248 (≠ V235), G249 (= G236), E250 (≠ S237), T253 (≠ I240), E271 (≠ L258), L272 (≠ G259), C305 (= C292), E409 (= E394), F411 (= F396), F475 (= F461)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
34% identity, 93% coverage: 19:491/509 of query aligns to 11:481/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 158:161) binding NADPH
- K162 (≠ M170) active site, Charge relay system
- KPSE 176:179 (= KPSE 184:187) binding NADPH
- G209 (vs. gap) binding NADPH
- GTST 230:233 (≠ STPI 237:240) binding NADPH
- E252 (≠ L258) active site, Proton acceptor
- C286 (= C292) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E394) binding NADPH
- E464 (≠ H472) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 93% coverage: 19:491/509 of query aligns to 10:480/489 of 4cazA
- active site: N152 (= N161), K175 (= K184), E251 (≠ L258), C285 (= C292), E386 (= E394), E463 (≠ H472)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I157), G149 (≠ T158), W151 (≠ F160), N152 (= N161), K175 (= K184), E178 (= E187), G208 (vs. gap), G212 (≠ V220), F226 (= F234), T227 (≠ V235), G228 (= G236), G229 (≠ S237), T232 (≠ I240), V236 (≠ I244), E251 (≠ L258), L252 (≠ G259), C285 (= C292), E386 (= E394), F388 (= F396)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 93% coverage: 19:491/509 of query aligns to 10:480/489 of 2woxA
- active site: N152 (= N161), K175 (= K184), E251 (≠ L258), C285 (= C292), E386 (= E394), E463 (≠ H472)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I157), G149 (≠ T158), W151 (≠ F160), N152 (= N161), K175 (= K184), S177 (= S186), E178 (= E187), G208 (vs. gap), G212 (≠ V220), F226 (= F234), T227 (≠ V235), G228 (= G236), G229 (≠ S237), T232 (≠ I240), V236 (≠ I244), E251 (≠ L258), L252 (≠ G259), C285 (= C292), E386 (= E394), F388 (= F396)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 93% coverage: 19:491/509 of query aligns to 10:480/489 of 2wmeA
- active site: N152 (= N161), K175 (= K184), E251 (≠ L258), C285 (= C292), E386 (= E394), E463 (≠ H472)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T158), W151 (≠ F160), K175 (= K184), S177 (= S186), E178 (= E187), G208 (vs. gap), G212 (≠ V220), F226 (= F234), G228 (= G236), G229 (≠ S237), T232 (≠ I240), V236 (≠ I244)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
34% identity, 97% coverage: 3:494/509 of query aligns to 26:514/518 of O94788
- E50 (≠ Q27) to G: in dbSNP:rs34266719
- A110 (≠ R84) to V: in dbSNP:rs35365164
- Q182 (≠ G156) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPF 158:160) binding NAD(+)
- KPAE 210:213 (≠ KPSE 184:187) binding NAD(+)
- STE 264:266 (≠ STP 237:239) binding NAD(+)
- C320 (= C292) active site, Nucleophile
- R347 (≠ L320) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K321) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ QHLDK 339:343) binding NAD(+)
- A383 (= A356) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E394) binding NAD(+)
- E436 (≠ G413) to K: in dbSNP:rs34744827
- S461 (≠ L438) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
35% identity, 94% coverage: 19:494/509 of query aligns to 16:488/492 of 6b5hA
- active site: N161 (= N161), E260 (≠ L258), C294 (= C292), E468 (≠ M474)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G111), G116 (≠ R115), F162 (= F162), W169 (= W169), Q284 (≠ G282), F288 (≠ G286), T295 (≠ M293), N449 (≠ I452), L451 (≠ V454), N452 (≠ M456), F457 (= F461)
- binding nicotinamide-adenine-dinucleotide: I157 (= I157), I158 (≠ T158), W160 (≠ F160), N161 (= N161), K184 (= K184), G217 (≠ D216), G221 (≠ V220), F235 (= F234), T236 (≠ V235), G237 (= G236), S238 (= S237), V241 (≠ I240), E260 (≠ L258), L261 (≠ G259), C294 (= C292), F393 (= F396)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
35% identity, 94% coverage: 19:494/509 of query aligns to 16:488/492 of 6b5gA
- active site: N161 (= N161), E260 (≠ L258), C294 (= C292), E468 (≠ M474)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F162), L165 (≠ M165), W169 (= W169), F288 (≠ G286), C293 (≠ R291), C294 (= C292), T295 (≠ M293), N449 (≠ I452), L451 (≠ V454)
- binding nicotinamide-adenine-dinucleotide: I157 (= I157), I158 (≠ T158), P159 (= P159), W160 (≠ F160), N161 (= N161), M166 (≠ V166), K184 (= K184), E187 (= E187), G217 (≠ D216), G221 (≠ V220), F235 (= F234), T236 (≠ V235), G237 (= G236), S238 (= S237), V241 (≠ I240), E260 (≠ L258), L261 (≠ G259), C294 (= C292), E391 (= E394), F393 (= F396)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
35% identity, 94% coverage: 19:494/509 of query aligns to 16:488/492 of 6aljA
- active site: N161 (= N161), E260 (≠ L258), C294 (= C292), E468 (≠ M474)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ R115), F162 (= F162), L165 (≠ M165), M166 (≠ V166), W169 (= W169), E260 (≠ L258), C293 (≠ R291), C294 (= C292), L451 (≠ V454), N452 (≠ M456), A453 (= A457)
- binding nicotinamide-adenine-dinucleotide: I157 (= I157), I158 (≠ T158), P159 (= P159), W160 (≠ F160), N161 (= N161), K184 (= K184), E187 (= E187), G217 (≠ D216), G221 (≠ V220), F235 (= F234), G237 (= G236), S238 (= S237), V241 (≠ I240), Q341 (≠ H340), K344 (= K343), E391 (= E394), F393 (= F396)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 93% coverage: 19:492/509 of query aligns to 8:478/489 of 4o6rA
- active site: N150 (= N161), K173 (= K184), E248 (≠ L258), C282 (= C292), E383 (= E394), E460 (≠ H472)
- binding adenosine monophosphate: I146 (= I157), V147 (≠ T158), K173 (= K184), G206 (≠ D216), G210 (≠ V220), Q211 (≠ D221), F224 (= F234), G226 (= G236), S227 (= S237), T230 (≠ I240), R233 (≠ Y243)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
34% identity, 97% coverage: 3:494/509 of query aligns to 26:514/518 of Q63639
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
33% identity, 96% coverage: 3:492/509 of query aligns to 9:495/501 of P00352
- N121 (≠ G111) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ TPFN 158:161) binding NAD(+)
- I177 (≠ M168) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPSE 184:187) binding NAD(+)
- GP 226:227 (≠ DK 216:217) binding NAD(+)
- GS 246:247 (= GS 236:237) binding NAD(+)
- E269 (≠ L258) active site, Proton acceptor
- ELG 269:271 (≠ LGG 258:260) binding NAD(+)
- C302 (≠ R291) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C292) active site, Nucleophile
- EQYDK 349:353 (≠ QHLDK 339:343) binding NAD(+)
- EIF 400:402 (= EIF 394:396) binding NAD(+)
- G458 (≠ P453) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
- 336:501 Mediates interaction with PRMT3
4wb9A Human aldh1a1 complexed with nadh (see paper)
33% identity, 96% coverage: 3:492/509 of query aligns to 1:487/493 of 4wb9A
- active site: N162 (= N161), K185 (= K184), E261 (≠ L258), C295 (= C292), E392 (= E394), E469 (≠ M474)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I157), I159 (≠ T158), P160 (= P159), W161 (≠ F160), N162 (= N161), K185 (= K184), E188 (= E187), G218 (≠ D216), G222 (≠ V220), F236 (= F234), T237 (≠ V235), G238 (= G236), S239 (= S237), V242 (≠ I240), G263 (= G260), C295 (= C292), Q342 (≠ H340), K345 (= K343), E392 (= E394), F394 (= F396)
5teiA Structure of human aldh1a1 with inhibitor cm039
33% identity, 96% coverage: 3:492/509 of query aligns to 1:487/493 of 5teiA
- active site: N162 (= N161), K185 (= K184), E261 (≠ L258), C295 (= C292), E392 (= E394), E469 (≠ M474)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-5-(2-methylphenyl)-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: S113 (≠ G111), F163 (= F162), H285 (≠ G282), G286 (≠ A283), Y289 (≠ G286), C295 (= C292), G450 (≠ P453), V452 (≠ P455), F458 (= F461)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I157), I159 (≠ T158), P160 (= P159), W161 (≠ F160), N162 (= N161), K185 (= K184), E188 (= E187), G218 (≠ D216), G222 (≠ V220), A223 (≠ D221), F236 (= F234), T237 (≠ V235), G238 (= G236), S239 (= S237), V242 (≠ I240), C295 (= C292), Q342 (≠ H340), K345 (= K343), E392 (= E394), F394 (= F396)
Query Sequence
>WP_012383190.1 NCBI__GCF_000019845.1:WP_012383190.1
MTLPVTPAQTTIEPIPHVINGQLTEGQSGRFGEVFNPALGSVVRRVPLATREEVGQAVEA
AATAFPAWAATPPHVRARVLFRFRDLVEQQADRLAALITSEHGKVFSDAKGELTRGLEVV
EFACGIPQLLKGEFSEQVGRGIDAVSMRQPLGVVAGITPFNFPAMVPMWMFPVALACGNT
FVLKPSERDPSLGVALAQLLREAGLPDGVFNVIHGDKEAVDALLEHEKVEAISFVGSTPI
AEYIYQQGTARGKRVQALGGAKNHMIVMPDADLDQAVDALMGAAFGSAGERCMAISVVVP
VGEKTAEALIERLVPRIQALKVAPGTDPSAEMGPLVTRQHLDKVTAYIETGLAEGAKLRV
DGRGLAVEGHAEGFFLGGSLFDHVTSSMRIYKEEIFGPVLCMVRAKSFEEGLGLINDHAF
GNGTALFTRDGDAAQSFLSRVRAGMVGVNVPIPVPMAFHSFGGWKRSLFGDHHMHGPEGV
RFYTRLKTATVRWPTGIRAGAEFTMPTLG
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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