SitesBLAST
Comparing CCNA_02357 FitnessBrowser__Caulo:CCNA_02357 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)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
62% identity, 97% coverage: 1:485/498 of query aligns to 4:488/491 of 4iymC
- active site: N153 (= N150), K176 (= K173), F250 (≠ M247), C284 (= C281), E386 (= E383), Q466 (= Q463)
- binding nicotinamide-adenine-dinucleotide: I149 (= I146), T150 (= T147), P151 (= P148), F152 (= F149), N153 (= N150), F154 (= F151), K176 (= K173), K209 (= K206), V212 (= V209), F226 (= F223), V227 (= V224), G228 (= G225), S229 (= S226), I232 (= I229), G251 (= G248), C284 (= C281), E386 (= E383), F388 (= F385)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
53% identity, 98% coverage: 1:487/498 of query aligns to 1:486/489 of 4zz7A
- active site: N149 (= N150), K172 (= K173), L246 (≠ M247), C280 (= C281), E382 (= E383), A462 (≠ Q463)
- binding nicotinamide-adenine-dinucleotide: T146 (= T147), P147 (= P148), F148 (= F149), N149 (= N150), K172 (= K173), E175 (= E176), K205 (= K206), V208 (= V209), F222 (= F223), V223 (= V224), G224 (= G225), S225 (= S226), I228 (= I229), L246 (≠ M247), G247 (= G248), C280 (= C281), E382 (= E383), F384 (= F385)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
52% identity, 97% coverage: 4:484/498 of query aligns to 3:457/468 of 5tjrD
- active site: N144 (= N150), K167 (= K173), L241 (≠ M247), C270 (= C281), E356 (= E383), A436 (≠ Q463)
- binding adenosine-5'-diphosphate: I140 (= I146), T141 (= T147), F143 (= F149), K167 (= K173), E170 (= E176), K200 (= K206), F217 (= F223), S220 (= S226), I223 (= I229)
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)
42% identity, 97% coverage: 1:483/498 of query aligns to 4:482/487 of P42412
- C36 (≠ A33) 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 (= R104) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T147) binding
- F152 (= F149) binding
- C160 (≠ M157) 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 (= K173) binding
- E179 (= E176) binding
- R180 (≠ K177) binding
- S229 (= S226) binding
- T251 (≠ G248) binding
- R283 (= R280) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ L284) 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 (≠ V349) 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 (= E383) binding
- C413 (≠ A414) 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
42% identity, 97% coverage: 1:483/498 of query aligns to 2:480/484 of 1t90A
- active site: N151 (= N150), K174 (= K173), L248 (≠ M247), C282 (= C281), E380 (= E383), A460 (≠ Q463)
- binding nicotinamide-adenine-dinucleotide: I147 (= I146), A148 (≠ T147), P149 (= P148), F150 (= F149), N151 (= N150), W159 (= W158), K174 (= K173), E177 (= E176), R178 (≠ K177), H207 (≠ K206), V225 (= V224), G226 (= G225), S227 (= S226), V230 (≠ I229), L248 (≠ M247), T249 (≠ G248), C282 (= C281), E380 (= E383), F382 (= F385)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
36% identity, 95% coverage: 7:478/498 of query aligns to 9:477/489 of 6wsbA
- active site: N152 (= N150), E250 (≠ M247), C284 (= C281), E462 (≠ T461)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), G149 (≠ T147), A150 (≠ P148), W151 (≠ F149), N152 (= N150), K175 (= K173), E178 (= E176), G208 (≠ K206), G211 (≠ V209), A212 (≠ D210), F225 (= F223), T226 (≠ V224), G227 (= G225), G228 (≠ S226), T231 (≠ I229), V235 (= V233), E250 (≠ M247), L251 (≠ G248), G252 (= G249), C284 (= C281), E385 (= E383), F387 (= F385)
7radA Crystal structure analysis of aldh1b1
32% identity, 96% coverage: 7:484/498 of query aligns to 16:490/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (≠ F149), N162 (= N150), M167 (≠ I155), K185 (= K173), E188 (= E176), G218 (≠ D205), G222 (≠ V209), A223 (≠ D210), T237 (≠ V224), G238 (= G225), S239 (= S226), V242 (≠ I229), E261 (≠ M247), L262 (≠ G248), C295 (= C281), E392 (= E383), F394 (= F385)
- 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 (≠ R104), F163 (= F151), E285 (≠ G271), F289 (≠ G275), N450 (≠ P442), V452 (≠ P444)
7mjdA Crystal structure analysis of aldh1b1
32% identity, 96% coverage: 7:484/498 of query aligns to 16:490/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (≠ F149), N162 (= N150), M167 (≠ I155), K185 (= K173), E188 (= E176), G218 (≠ D205), G222 (≠ V209), F236 (= F223), T237 (≠ V224), G238 (= G225), S239 (= S226), V242 (≠ I229), E261 (≠ M247), L262 (≠ G248), C295 (= C281), E392 (= E383), F394 (= F385)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ R104), E285 (≠ G271), F289 (≠ G275), N450 (≠ P442), V452 (≠ P444)
7mjcA Crystal structure analysis of aldh1b1
32% identity, 96% coverage: 7:484/498 of query aligns to 16:490/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), P160 (= P148), W161 (≠ F149), N162 (= N150), K185 (= K173), E188 (= E176), G218 (≠ D205), G222 (≠ V209), T237 (≠ V224), G238 (= G225), S239 (= S226), V242 (≠ I229), E261 (≠ M247), L262 (≠ G248), C295 (= C281), E392 (= E383), F394 (= F385)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
31% identity, 92% coverage: 22:478/498 of query aligns to 22:475/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (≠ M247), C282 (= C281), E383 (= E383), E460 (≠ Q463)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ T147), K173 (= K173), G206 (≠ D205), G210 (≠ V209), Q211 (≠ D210), F224 (= F223), G226 (= G225), S227 (= S226), T230 (≠ I229), R233 (≠ Y232)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
34% identity, 92% coverage: 25:484/498 of query aligns to 61:517/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
34% identity, 92% coverage: 25:484/498 of query aligns to 37:493/496 of 4fr8C
- active site: N165 (= N150), K188 (= K173), Q264 (≠ M247), C298 (= C281), E395 (= E383), E472 (≠ Q463)
- binding nicotinamide-adenine-dinucleotide: I161 (= I146), I162 (≠ T147), W164 (≠ F149), K188 (= K173), G221 (≠ D205), G225 (≠ V209), A226 (≠ D210), F239 (= F223), G241 (= G225), S242 (= S226), I245 (= I229), Q345 (≠ H329), E395 (= E383), F397 (= F385)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
34% identity, 92% coverage: 25:484/498 of query aligns to 34:490/493 of 4fr8A
- active site: N162 (= N150), K185 (= K173), Q261 (≠ M247), C295 (= C281), E392 (= E383), E469 (≠ Q463)
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), I159 (≠ T147), W161 (≠ F149), K185 (= K173), G218 (≠ D205), G222 (≠ V209), A223 (≠ D210), F236 (= F223), G238 (= G225), S239 (= S226), I242 (= I229), Q342 (≠ H329), K345 (= K332), E392 (= E383), F394 (= F385)
- binding propane-1,2,3-triyl trinitrate: F163 (= F151), L166 (≠ M154), W170 (= W158), F289 (≠ G275), S294 (≠ R280), C295 (= C281), D450 (≠ P442), F452 (≠ P444)
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)
31% identity, 95% coverage: 7:478/498 of query aligns to 10:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 147:150) binding
- K162 (≠ M159) active site, Charge relay system
- KPSE 176:179 (= KPSE 173:176) binding
- G209 (≠ K206) binding
- GTST 230:233 (≠ SSDI 226:229) binding
- E252 (≠ M247) active site, Proton acceptor
- C286 (= C281) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E383) binding
- E464 (≠ T461) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
31% identity, 95% coverage: 7:478/498 of query aligns to 9:478/489 of 4cazA
- active site: N152 (= N150), K175 (= K173), E251 (≠ M247), C285 (= C281), E386 (= E383), E463 (≠ T461)
- 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 (= I146), G149 (≠ T147), W151 (≠ F149), N152 (= N150), K175 (= K173), E178 (= E176), G208 (≠ K206), G212 (≠ D210), F226 (= F223), T227 (≠ V224), G228 (= G225), G229 (≠ S226), T232 (≠ I229), V236 (= V233), E251 (≠ M247), L252 (≠ G248), C285 (= C281), E386 (= E383), F388 (= F385)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
31% identity, 95% coverage: 7:478/498 of query aligns to 9:478/489 of 2woxA
- active site: N152 (= N150), K175 (= K173), E251 (≠ M247), C285 (= C281), E386 (= E383), E463 (≠ T461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I146), G149 (≠ T147), W151 (≠ F149), N152 (= N150), K175 (= K173), S177 (= S175), E178 (= E176), G208 (≠ K206), G212 (≠ D210), F226 (= F223), T227 (≠ V224), G228 (= G225), G229 (≠ S226), T232 (≠ I229), V236 (= V233), E251 (≠ M247), L252 (≠ G248), C285 (= C281), E386 (= E383), F388 (= F385)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
31% identity, 95% coverage: 7:478/498 of query aligns to 9:478/489 of 2wmeA
- active site: N152 (= N150), K175 (= K173), E251 (≠ M247), C285 (= C281), E386 (= E383), E463 (≠ T461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T147), W151 (≠ F149), K175 (= K173), S177 (= S175), E178 (= E176), G208 (≠ K206), G212 (≠ D210), F226 (= F223), G228 (= G225), G229 (≠ S226), T232 (≠ I229), V236 (= V233)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
34% identity, 92% coverage: 25:484/498 of query aligns to 35:491/494 of 5l13A
- active site: N163 (= N150), K186 (= K173), E262 (≠ M247), C296 (= C281), E393 (= E383), E470 (≠ Q463)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F151), M168 (≠ I155), W171 (= W158), F290 (≠ G275), C295 (≠ R280), C296 (= C281), C297 (≠ M282), D451 (≠ P442), F453 (≠ P444)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
34% identity, 92% coverage: 25:484/498 of query aligns to 35:491/494 of 4kwgA
- active site: N163 (= N150), K186 (= K173), E262 (≠ M247), C296 (= C281), E393 (= E383), E470 (≠ Q463)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F151), M168 (≠ I155), C295 (≠ R280), C296 (= C281), C297 (≠ M282), D451 (≠ P442), F453 (≠ P444)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
34% identity, 92% coverage: 25:484/498 of query aligns to 35:491/494 of 4kwfA
- active site: N163 (= N150), K186 (= K173), E262 (≠ M247), C296 (= C281), E393 (= E383), E470 (≠ Q463)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F151), M168 (≠ I155), W171 (= W158), E262 (≠ M247), C295 (≠ R280), C296 (= C281), C297 (≠ M282), D451 (≠ P442), F453 (≠ P444), F459 (= F450)
Query Sequence
>CCNA_02357 FitnessBrowser__Caulo:CCNA_02357
MRDIAHFVKGQTLVGASGRFGDVFNPNTGEVQARVQFATDAELDAAVQVAAKAQVGWAQT
NPQRRARVMFEFKRLIERDMNTLAEILSSEHGKVIADSKGDIQRGLEVIEFACGIPHILK
GEYTEGAGPGIDVYSMRQPLGVCAGITPFNFPAMIPMWMFGISIAVGNSFILKPSEKDPT
VPVKLAELMMEAGAPAGVLNVVHGDKSAVDAILTHPLIRAVSFVGSSDIAHYVYQTGTAH
GKRVQAMGGAKNHGIVLPDADMDQVVKDLSGAAFGSAGERCMALPVVVPVGQKTADELRE
RMVAEIASLKVGVSTDPDAHYGPVVSAQHRDKIADYIRIGQEEGAELVVDGRDFQLQGFE
KGFFIGPSLFDGVKKGMKTYHEEIFGPVLQIVRAETLEEAIALPSEHQYGNGVAIFTRNG
RAAREFAANVNVGMVGINVPIPVPVAYHTFGGWKRSAFGDTNQHGVEGVKFYTKVKTVTA
RWPEGEVADSSFVIPTMK
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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