SitesBLAST
Comparing WP_013519377.1 NCBI__GCF_000204645.1:WP_013519377.1 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)
47% identity, 95% coverage: 11:488/505 of query aligns to 3:481/489 of 4zz7A
- active site: N149 (= N158), K172 (= K181), L246 (≠ M255), C280 (= C289), E382 (= E389), A462 (≠ P469)
- binding nicotinamide-adenine-dinucleotide: T146 (= T155), P147 (= P156), F148 (= F157), N149 (= N158), K172 (= K181), E175 (= E184), K205 (≠ E214), V208 (= V217), F222 (= F231), V223 (= V232), G224 (= G233), S225 (= S234), I228 (≠ V237), L246 (≠ M255), G247 (≠ M256), C280 (= C289), E382 (= E389), F384 (= F391)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
48% identity, 94% coverage: 15:488/505 of query aligns to 10:485/491 of 4iymC
- active site: N153 (= N158), K176 (= K181), F250 (≠ M255), C284 (= C289), E386 (= E389), Q466 (≠ P469)
- binding nicotinamide-adenine-dinucleotide: I149 (= I154), T150 (= T155), P151 (= P156), F152 (= F157), N153 (= N158), F154 (= F159), K176 (= K181), K209 (≠ E214), V212 (= V217), F226 (= F231), V227 (= V232), G228 (= G233), S229 (= S234), I232 (≠ V237), G251 (≠ M256), C284 (= C289), E386 (= E389), F388 (= F391)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
48% identity, 94% coverage: 12:488/505 of query aligns to 5:479/484 of 1t90A
- active site: N151 (= N158), K174 (= K181), L248 (≠ M255), C282 (= C289), E380 (= E389), A460 (≠ P469)
- binding nicotinamide-adenine-dinucleotide: I147 (= I154), A148 (≠ T155), P149 (= P156), F150 (= F157), N151 (= N158), W159 (= W166), K174 (= K181), E177 (= E184), R178 (≠ Q185), H207 (≠ E214), V225 (= V232), G226 (= G233), S227 (= S234), V230 (= V237), L248 (≠ M255), T249 (≠ M256), C282 (= C289), E380 (= E389), F382 (= F391)
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: 12:488/505 of query aligns to 7:481/487 of P42412
- C36 (≠ A41) 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 (= R112) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T155) binding NAD(+)
- F152 (= F157) binding NAD(+)
- C160 (≠ L165) 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 (= K181) binding NAD(+)
- E179 (= E184) binding NAD(+)
- R180 (≠ Q185) binding NAD(+)
- S229 (= S234) binding NAD(+)
- T251 (≠ M256) binding NAD(+)
- R283 (= R288) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I292) 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 (≠ L355) 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 (= E389) binding NAD(+)
- C413 (≠ A420) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
46% identity, 94% coverage: 12:488/505 of query aligns to 3:455/468 of 5tjrD
- active site: N144 (= N158), K167 (= K181), L241 (≠ M255), C270 (= C289), E356 (= E389), A436 (≠ P469)
- binding adenosine-5'-diphosphate: I140 (= I154), T141 (= T155), F143 (= F157), K167 (= K181), E170 (= E184), K200 (≠ E214), F217 (= F231), S220 (= S234), I223 (≠ V237)
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)
33% identity, 91% coverage: 13:472/505 of query aligns to 8:475/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 155:158) binding NADPH
- K162 (≠ M167) active site, Charge relay system
- KPSE 176:179 (= KPSE 181:184) binding NADPH
- G209 (= G213) binding NADPH
- GTST 230:233 (≠ STRV 234:237) binding NADPH
- E252 (≠ M255) active site, Proton acceptor
- C286 (= C289) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E389) binding NADPH
- E464 (≠ A461) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
33% identity, 91% coverage: 13:472/505 of query aligns to 7:474/489 of 4cazA
- active site: N152 (= N158), K175 (= K181), E251 (≠ M255), C285 (= C289), E386 (= E389), E463 (≠ A461)
- 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 (= I154), G149 (≠ T155), W151 (≠ F157), N152 (= N158), K175 (= K181), E178 (= E184), G208 (= G213), G212 (≠ V217), F226 (= F231), T227 (≠ V232), G228 (= G233), G229 (≠ S234), T232 (≠ V237), V236 (= V241), E251 (≠ M255), L252 (≠ M256), C285 (= C289), E386 (= E389), F388 (= F391)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
33% identity, 91% coverage: 13:472/505 of query aligns to 7:474/489 of 2woxA
- active site: N152 (= N158), K175 (= K181), E251 (≠ M255), C285 (= C289), E386 (= E389), E463 (≠ A461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I154), G149 (≠ T155), W151 (≠ F157), N152 (= N158), K175 (= K181), S177 (= S183), E178 (= E184), G208 (= G213), G212 (≠ V217), F226 (= F231), T227 (≠ V232), G228 (= G233), G229 (≠ S234), T232 (≠ V237), V236 (= V241), E251 (≠ M255), L252 (≠ M256), C285 (= C289), E386 (= E389), F388 (= F391)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
33% identity, 91% coverage: 13:472/505 of query aligns to 7:474/489 of 2wmeA
- active site: N152 (= N158), K175 (= K181), E251 (≠ M255), C285 (= C289), E386 (= E389), E463 (≠ A461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T155), W151 (≠ F157), K175 (= K181), S177 (= S183), E178 (= E184), G208 (= G213), G212 (≠ V217), F226 (= F231), G228 (= G233), G229 (≠ S234), T232 (≠ V237), V236 (= V241)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 94% coverage: 12:484/505 of query aligns to 17:486/491 of 5gtlA
- active site: N165 (= N158), K188 (= K181), E263 (≠ M255), C297 (= C289), E394 (= E389), E471 (≠ D466)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I154), P163 (= P156), K188 (= K181), A190 (≠ S183), E191 (= E184), Q192 (= Q185), G221 (= G213), G225 (≠ V217), G241 (= G233), S242 (= S234), T245 (≠ V237), L264 (≠ M256), C297 (= C289), E394 (= E389), F396 (= F391)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 94% coverage: 12:484/505 of query aligns to 17:486/491 of 5gtkA
- active site: N165 (= N158), K188 (= K181), E263 (≠ M255), C297 (= C289), E394 (= E389), E471 (≠ D466)
- binding nicotinamide-adenine-dinucleotide: I161 (= I154), I162 (≠ T155), P163 (= P156), W164 (≠ F157), K188 (= K181), E191 (= E184), G221 (= G213), G225 (≠ V217), A226 (≠ N218), F239 (= F231), G241 (= G233), S242 (= S234), T245 (≠ V237), Y248 (≠ H240), L264 (≠ M256), C297 (= C289), Q344 (≠ A335), R347 (= R338), E394 (= E389), F396 (= F391)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
32% identity, 93% coverage: 15:484/505 of query aligns to 30:501/515 of 2d4eC
- active site: N173 (= N158), K196 (= K181), E271 (≠ M255), C305 (= C289), E409 (= E389), E486 (≠ P469)
- binding nicotinamide-adenine-dinucleotide: I169 (= I154), T170 (= T155), P171 (= P156), W172 (≠ F157), K196 (= K181), A198 (≠ S183), G229 (= G213), G233 (≠ V217), A234 (≠ N218), T248 (≠ V232), G249 (= G233), E250 (≠ S234), T253 (≠ V237), E271 (≠ M255), L272 (≠ M256), C305 (= C289), E409 (= E389), F411 (= F391), F475 (= F456)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
31% identity, 93% coverage: 15:485/505 of query aligns to 13:484/487 of Q9H2A2
- R109 (= R112) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N158) mutation to A: Complete loss of activity.
- R451 (≠ V449) mutation to A: Complete loss of activity.
O14293 Putative aldehyde dehydrogenase-like protein C9E9.09c; EC 1.2.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 94% coverage: 12:484/505 of query aligns to 23:493/503 of O14293
- S248 (= S234) modified: Phosphoserine
Sites not aligning to the query:
- 501 modified: Phosphoserine
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
29% identity, 94% coverage: 13:489/505 of query aligns to 19:503/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (≠ M255), C298 (= C289), E399 (= E389), E476 (≠ D466)
- binding nicotinamide-adenine-dinucleotide: P164 (= P156), K189 (= K181), E192 (= E184), G222 (= G213), G226 (≠ V217), G242 (= G233), G243 (≠ S234), T246 (≠ V237), H249 (= H240), I250 (≠ V241), C298 (= C289), E399 (= E389), F401 (= F391)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
31% identity, 94% coverage: 18:494/505 of query aligns to 26:502/503 of 1bpwA
- active site: N166 (= N158), K189 (= K181), E263 (≠ M255), C297 (= C289), E400 (= E389), E477 (≠ L467)
- binding nicotinamide-adenine-dinucleotide: I162 (= I154), L163 (≠ T155), W165 (≠ F157), N166 (= N158), K189 (= K181), G221 (= G213), G225 (≠ V217), T240 (≠ V232), G241 (= G233), S242 (= S234), T245 (≠ V237), E263 (≠ M255), L264 (≠ M256), C297 (= C289), E400 (= E389), F402 (= F391), F466 (= F456)
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)
31% identity, 94% coverage: 18:494/505 of query aligns to 26:502/503 of P56533
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
33% identity, 93% coverage: 13:484/505 of query aligns to 4:473/487 of 4go4A
- active site: N149 (= N158), K172 (= K181), E247 (≠ M255), C281 (= C289), E381 (= E389), E458 (≠ P469)
- binding nicotinamide-adenine-dinucleotide: I145 (= I154), V146 (≠ T155), W148 (≠ F157), N149 (= N158), F154 (≠ I163), K172 (= K181), G205 (= G213), G209 (≠ V217), Q210 (≠ N218), F223 (= F231), T224 (≠ V232), G225 (= G233), S226 (= S234), T229 (≠ V237), E247 (≠ M255), G249 (= G257), C281 (= C289), E381 (= E389), F383 (= F391)
8t0nA Structure of compound 4 bound to human aldh1a1 (see paper)
33% identity, 95% coverage: 5:485/505 of query aligns to 7:486/494 of 8t0nA
- binding nicotinamide-adenine-dinucleotide: I159 (= I154), I160 (≠ T155), P161 (= P156), W162 (≠ F157), N163 (= N158), K186 (= K181), E189 (= E184), G219 (= G213), G223 (≠ V217), A224 (≠ N218), F237 (= F231), T238 (≠ V232), G239 (= G233), S240 (= S234), V243 (= V237), E262 (≠ M255), G264 (= G257), C296 (= C289), Q343 (≠ A335), K346 (≠ R338), E393 (= E389), F395 (= F391)
- binding 2-methoxy-6-{[(1-propyl-1H-benzimidazol-2-yl)amino]methyl}phenol: S114 (≠ G108), G118 (≠ R112), T122 (≠ V116), V167 (≠ M162), W171 (= W166), V453 (= V447), S454 (≠ P448), A455 (≠ V449)
7jwwA Crystal structure of human aldh1a1 bound to compound (r)-28 (see paper)
33% identity, 95% coverage: 5:485/505 of query aligns to 7:486/494 of 7jwwA
- active site: N163 (= N158), K186 (= K181), E262 (≠ M255), C296 (= C289), E393 (= E389), E470 (≠ D466)
- binding 5-{4-[(Z)-2-hydroxyethenyl]phenyl}-1-methyl-6-{[(1R)-1-phenylethyl]sulfanyl}-1,5-dihydro-4H-pyrazolo[3,4-d]pyrimidin-4-one: G118 (≠ R112), T122 (≠ V116), F164 (= F159), M168 (≠ I163), Y290 (≠ G283), C295 (≠ R288), C296 (= C289), I297 (≠ M290), V453 (= V447), F459 (≠ L453)
Query Sequence
>WP_013519377.1 NCBI__GCF_000204645.1:WP_013519377.1
MDASTAVQAPTVKLLINGQMVESKTTQWRNVVNPATQEVLARVPFATPDEVNAAVANAKE
AFKTWRKTPIGTRARIFLKLQQLIRENMKELAALLTAEQGKTLPDAEGDVFRGLEVVEHA
AAIGNLQLGELANNVASGVDTYTVLQPLGVCAGITPFNFPAMIPLWMFPMAIATGNTFVL
KPSEQDPMVTMRLCELALEAGIPPGVLNVVHGGEDVVNAICDHPDIKAISFVGSTRVGTH
VYNRASLAGKRVQCMMGAKNHAIVMPDANKEQSINAILGASFGAAGQRCMAISVVLLVGE
AQKWLPDFVEKAKGLKVSAGTTPGADLGPLISCAARERVEGLIARGVQEGAKLELDGRNP
GIAGFEKGNFVGPTIFSGVKPGMSIYDQEVFGPVLCVVAADDLEQAIEFINANPNGNGTA
IFTQSGAAARMFQEDIDVGQVGINLPVPVPVPLFSFTGSRASKLGDLGPYGKQVVLFYTQ
TKTVTERWFDDSTLHHGVNTTISLK
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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