SitesBLAST
Comparing WP_012404379.1 NCBI__GCF_000020045.1:WP_012404379.1 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)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
48% identity, 94% coverage: 15:492/509 of query aligns to 3:481/489 of 4zz7A
- active site: N149 (= N162), K172 (= K185), L246 (≠ M259), C280 (= C293), E382 (= E393), A462 (≠ P473)
- binding nicotinamide-adenine-dinucleotide: T146 (= T159), P147 (= P160), F148 (= F161), N149 (= N162), K172 (= K185), E175 (= E188), K205 (= K218), V208 (= V221), F222 (= F235), V223 (= V236), G224 (= G237), S225 (= S238), I228 (≠ V241), L246 (≠ M259), G247 (≠ M260), C280 (= C293), E382 (= E393), F384 (= F395)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
48% identity, 94% coverage: 12:492/509 of query aligns to 1:479/484 of 1t90A
- active site: N151 (= N162), K174 (= K185), L248 (≠ M259), C282 (= C293), E380 (= E393), A460 (≠ P473)
- binding nicotinamide-adenine-dinucleotide: I147 (= I158), A148 (≠ T159), P149 (= P160), F150 (= F161), N151 (= N162), W159 (= W170), K174 (= K185), E177 (= E188), R178 (≠ Q189), H207 (≠ K218), V225 (= V236), G226 (= G237), S227 (= S238), V230 (= V241), L248 (≠ M259), T249 (≠ M260), C282 (= C293), E380 (= E393), F382 (= F395)
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)
48% identity, 94% coverage: 12:492/509 of query aligns to 3:481/487 of P42412
- C36 (≠ A45) 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 (= R116) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T159) binding NAD(+)
- F152 (= F161) binding NAD(+)
- C160 (≠ L169) 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 (= K185) binding NAD(+)
- E179 (= E188) binding NAD(+)
- R180 (≠ Q189) binding NAD(+)
- S229 (= S238) binding NAD(+)
- T251 (≠ M260) binding NAD(+)
- R283 (= R292) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ T296) 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 (≠ L359) 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 (= E393) binding NAD(+)
- C413 (≠ G424) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
47% identity, 93% coverage: 19:492/509 of query aligns to 10:485/491 of 4iymC
- active site: N153 (= N162), K176 (= K185), F250 (≠ M259), C284 (= C293), E386 (= E393), Q466 (≠ P473)
- binding nicotinamide-adenine-dinucleotide: I149 (= I158), T150 (= T159), P151 (= P160), F152 (= F161), N153 (= N162), F154 (= F163), K176 (= K185), K209 (= K218), V212 (= V221), F226 (= F235), V227 (= V236), G228 (= G237), S229 (= S238), I232 (≠ V241), G251 (≠ M260), C284 (= C293), E386 (= E393), F388 (= F395)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
47% identity, 94% coverage: 16:492/509 of query aligns to 3:455/468 of 5tjrD
- active site: N144 (= N162), K167 (= K185), L241 (≠ M259), C270 (= C293), E356 (= E393), A436 (≠ P473)
- binding adenosine-5'-diphosphate: I140 (= I158), T141 (= T159), F143 (= F161), K167 (= K185), E170 (= E188), K200 (= K218), F217 (= F235), S220 (= S238), I223 (≠ V241)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 93% coverage: 14:488/509 of query aligns to 15:486/491 of 5gtlA
- active site: N165 (= N162), K188 (= K185), E263 (≠ M259), C297 (= C293), E394 (= E393), E471 (≠ D470)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I158), P163 (= P160), K188 (= K185), A190 (≠ S187), E191 (= E188), Q192 (= Q189), G221 (= G217), G225 (≠ V221), G241 (= G237), S242 (= S238), T245 (≠ V241), L264 (≠ M260), C297 (= C293), E394 (= E393), F396 (= F395)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 93% coverage: 14:488/509 of query aligns to 15:486/491 of 5gtkA
- active site: N165 (= N162), K188 (= K185), E263 (≠ M259), C297 (= C293), E394 (= E393), E471 (≠ D470)
- binding nicotinamide-adenine-dinucleotide: I161 (= I158), I162 (≠ T159), P163 (= P160), W164 (≠ F161), K188 (= K185), E191 (= E188), G221 (= G217), G225 (≠ V221), A226 (≠ D222), F239 (= F235), G241 (= G237), S242 (= S238), T245 (≠ V241), Y248 (≠ H244), L264 (≠ M260), C297 (= C293), Q344 (≠ A339), R347 (= R342), E394 (= E393), F396 (= F395)
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)
32% identity, 96% coverage: 12:498/509 of query aligns to 3:489/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 159:162) binding NADPH
- K162 (≠ M171) active site, Charge relay system
- KPSE 176:179 (= KPSE 185:188) binding NADPH
- G209 (= G217) binding NADPH
- GTST 230:233 (≠ STAV 238:241) binding NADPH
- E252 (≠ M259) active site, Proton acceptor
- C286 (= C293) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E393) binding NADPH
- E464 (≠ P473) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
32% identity, 96% coverage: 12:498/509 of query aligns to 2:488/489 of 4cazA
- active site: N152 (= N162), K175 (= K185), E251 (≠ M259), C285 (= C293), E386 (= E393), E463 (≠ P473)
- 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 (= I158), G149 (≠ T159), W151 (≠ F161), N152 (= N162), K175 (= K185), E178 (= E188), G208 (= G217), G212 (≠ V221), F226 (= F235), T227 (≠ V236), G228 (= G237), G229 (≠ S238), T232 (≠ V241), V236 (= V245), E251 (≠ M259), L252 (≠ M260), C285 (= C293), E386 (= E393), F388 (= F395)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
32% identity, 96% coverage: 12:498/509 of query aligns to 2:488/489 of 2woxA
- active site: N152 (= N162), K175 (= K185), E251 (≠ M259), C285 (= C293), E386 (= E393), E463 (≠ P473)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I158), G149 (≠ T159), W151 (≠ F161), N152 (= N162), K175 (= K185), S177 (= S187), E178 (= E188), G208 (= G217), G212 (≠ V221), F226 (= F235), T227 (≠ V236), G228 (= G237), G229 (≠ S238), T232 (≠ V241), V236 (= V245), E251 (≠ M259), L252 (≠ M260), C285 (= C293), E386 (= E393), F388 (= F395)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
32% identity, 96% coverage: 12:498/509 of query aligns to 2:488/489 of 2wmeA
- active site: N152 (= N162), K175 (= K185), E251 (≠ M259), C285 (= C293), E386 (= E393), E463 (≠ P473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T159), W151 (≠ F161), K175 (= K185), S177 (= S187), E178 (= E188), G208 (= G217), G212 (≠ V221), F226 (= F235), G228 (= G237), G229 (≠ S238), T232 (≠ V241), V236 (= V245)
4wb9A Human aldh1a1 complexed with nadh (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 9:487/493 of 4wb9A
- active site: N162 (= N162), K185 (= K185), E261 (≠ M259), C295 (= C293), E392 (= E393), E469 (≠ D470)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I158), I159 (≠ T159), P160 (= P160), W161 (≠ F161), N162 (= N162), K185 (= K185), E188 (= E188), G218 (= G217), G222 (≠ V221), F236 (= F235), T237 (≠ V236), G238 (= G237), S239 (= S238), V242 (= V241), G263 (= G261), C295 (= C293), Q342 (≠ A339), K345 (≠ R342), E392 (= E393), F394 (= F395)
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, 94% coverage: 12:491/509 of query aligns to 17:495/501 of P00352
- N121 (≠ G112) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ TPFN 159:162) binding NAD(+)
- I177 (≠ L169) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPSE 185:188) binding NAD(+)
- GP 226:227 (≠ GK 217:218) binding NAD(+)
- GS 246:247 (= GS 237:238) binding NAD(+)
- E269 (≠ M259) active site, Proton acceptor
- ELG 269:271 (≠ MMG 259:261) binding NAD(+)
- C302 (≠ R292) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C293) active site, Nucleophile
- EQYDK 349:353 (≠ AAKAR 338:342) binding NAD(+)
- EIF 400:402 (= EIF 393:395) binding NAD(+)
- G458 (vs. gap) 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
5teiA Structure of human aldh1a1 with inhibitor cm039
33% identity, 94% coverage: 12:491/509 of query aligns to 9:487/493 of 5teiA
- active site: N162 (= N162), K185 (= K185), E261 (≠ M259), C295 (= C293), E392 (= E393), E469 (≠ D470)
- binding 6-{[(3-fluorophenyl)methyl]sulfanyl}-5-(2-methylphenyl)-2,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: S113 (≠ G112), F163 (= F163), H285 (≠ G283), G286 (≠ A284), Y289 (≠ G287), C295 (= C293), G450 (vs. gap), V452 (≠ I451), F458 (= F457)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I158), I159 (≠ T159), P160 (= P160), W161 (≠ F161), N162 (= N162), K185 (= K185), E188 (= E188), G218 (= G217), G222 (≠ V221), A223 (≠ D222), F236 (= F235), T237 (≠ V236), G238 (= G237), S239 (= S238), V242 (= V241), C295 (= C293), Q342 (≠ A339), K345 (≠ R342), E392 (= E393), F394 (= F395)
4x4lA Structure of human aldh1a1 with inhibitor cm037 (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 9:487/493 of 4x4lA
- active site: N162 (= N162), K185 (= K185), E261 (≠ M259), C295 (= C293), E392 (= E393), E469 (≠ D470)
- binding ethyl ({4-oxo-3-[3-(pyrrolidin-1-yl)propyl]-3,4-dihydro[1]benzothieno[3,2-d]pyrimidin-2-yl}sulfanyl)acetate: S113 (≠ G112), M167 (≠ I167), W170 (= W170), Y289 (≠ G287), G450 (vs. gap), F458 (= F457)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I158), I159 (≠ T159), P160 (= P160), W161 (≠ F161), K185 (= K185), E188 (= E188), G218 (= G217), G222 (≠ V221), F236 (= F235), T237 (≠ V236), G238 (= G237), S239 (= S238), V242 (= V241), C295 (= C293), Q342 (≠ A339), K345 (≠ R342), E392 (= E393), F394 (= F395)
8t0tA Structure of compound 4 bound to human aldh1a1 (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 10:488/494 of 8t0tA
7um9A Human aldh1a1 with bound compound cm38 (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 10:488/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I158), I160 (≠ T159), P161 (= P160), W162 (≠ F161), N163 (= N162), K186 (= K185), E189 (= E188), G219 (= G217), G223 (≠ V221), F237 (= F235), T238 (≠ V236), G239 (= G237), S240 (= S238), V243 (= V241), E262 (≠ M259), G264 (= G261), Q343 (≠ A339), K346 (≠ R342), E393 (= E393), F395 (= F395)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (= W170), H286 (≠ G283), Y290 (≠ G287), I297 (≠ M294), G451 (vs. gap)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 10:488/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 10:488/494 of 5l2nA
- active site: N163 (= N162), K186 (= K185), E262 (≠ M259), C296 (= C293), E393 (= E393), E470 (≠ D470)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (= F163), M168 (≠ I167), W171 (= W170), H286 (≠ G283), G287 (≠ A284), Y290 (≠ G287), C295 (≠ R292), C296 (= C293), I297 (≠ M294), Y450 (≠ P450), G451 (vs. gap), V453 (≠ I451), F459 (= F457)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
33% identity, 94% coverage: 12:491/509 of query aligns to 10:488/494 of 5l2mA
- active site: N163 (= N162), K186 (= K185), E262 (≠ M259), C296 (= C293), E393 (= E393), E470 (≠ D470)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F163), F283 (≠ A280), H286 (≠ G283), Y290 (≠ G287)
Query Sequence
>WP_012404379.1 NCBI__GCF_000020045.1:WP_012404379.1
MSAIATTVAGQKVETVKLLINGEFVESNATEWRDIVNPATQEVLARVPFATQQEVDAAIR
AAHAAFATWKNTPIGARMRIMLKYQALIREHMPRIAKTLTAEQGKTLPDAEGDIFRGLEV
VEHACSIGTLQQGEFAENVAGSVDTYTLRQPIGVCAGITPFNFPAMIPLWMFPMAIVCGN
TFVLKPSEQDPLSTMQLVELAIEAGVPKGVLNVVHGGKEVVDSLCTHELVKAISFVGSTA
VGTHVYNLGSQYGKRVQSMMGAKNHAVVLPDANREQTLNALVGAGFGAAGQRCMATSVVV
LVGASKDWLPELVEKAKTLKVNAGHEPKTDVGPVVSRAAKARILGLIEKGVEEGATLALD
GRDVDVAGYADGNFVGPTVFSDVTVGMEIYKTEIFGPVLCVMTVPTLDDAIALVNSNPMG
NGVGLFTQSGAAARKFQSEIDVGQVGINIPIPVPVPFFSFTGSRGSKLGDLGPYGKQVVQ
FYTQTKTVTARWFDDATVGDGVNTTIALR
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