SitesBLAST
Comparing CCNA_01360 FitnessBrowser__Caulo:CCNA_01360 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
64% identity, 97% coverage: 1:486/500 of query aligns to 3:488/491 of 4iymC
- active site: N153 (= N151), K176 (= K174), F250 (≠ M248), C284 (= C282), E386 (= E384), Q466 (= Q464)
- binding nicotinamide-adenine-dinucleotide: I149 (= I147), T150 (= T148), P151 (= P149), F152 (= F150), N153 (= N151), F154 (= F152), K176 (= K174), K209 (= K207), V212 (= V210), F226 (= F224), V227 (= V225), G228 (= G226), S229 (= S227), I232 (= I230), G251 (= G249), C284 (= C282), E386 (= E384), F388 (= F386)
4zz7A Crystal structure of methylmalonate-semialdehyde dehydrogenase (dddc) from oceanimonas doudoroffii (see paper)
56% identity, 97% coverage: 2:487/500 of query aligns to 1:485/489 of 4zz7A
- active site: N149 (= N151), K172 (= K174), L246 (≠ M248), C280 (= C282), E382 (= E384), A462 (≠ Q464)
- binding nicotinamide-adenine-dinucleotide: T146 (= T148), P147 (= P149), F148 (= F150), N149 (= N151), K172 (= K174), E175 (= E177), K205 (= K207), V208 (= V210), F222 (= F224), V223 (= V225), G224 (= G226), S225 (= S227), I228 (= I230), L246 (≠ M248), G247 (= G249), C280 (= C282), E382 (= E384), F384 (= F386)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
55% identity, 96% coverage: 5:485/500 of query aligns to 3:457/468 of 5tjrD
- active site: N144 (= N151), K167 (= K174), L241 (≠ M248), C270 (= C282), E356 (= E384), A436 (≠ Q464)
- binding adenosine-5'-diphosphate: I140 (= I147), T141 (= T148), F143 (= F150), K167 (= K174), E170 (= E177), K200 (= K207), F217 (= F224), S220 (= S227), I223 (= I230)
1t90A Crystal structure of methylmalonate semialdehyde dehydrogenase from bacillus subtilis
43% identity, 97% coverage: 2:484/500 of query aligns to 2:480/484 of 1t90A
- active site: N151 (= N151), K174 (= K174), L248 (≠ M248), C282 (= C282), E380 (= E384), A460 (≠ Q464)
- binding nicotinamide-adenine-dinucleotide: I147 (= I147), A148 (≠ T148), P149 (= P149), F150 (= F150), N151 (= N151), W159 (= W159), K174 (= K174), E177 (= E177), R178 (= R178), H207 (≠ K207), V225 (= V225), G226 (= G226), S227 (= S227), V230 (≠ I230), L248 (≠ M248), T249 (≠ G249), C282 (= C282), E380 (= E384), F382 (= F386)
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)
43% identity, 97% coverage: 2:484/500 of query aligns to 4:482/487 of P42412
- C36 (≠ A34) 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 (= R105) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T148) binding
- F152 (= F150) binding
- C160 (≠ M158) 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 (= K174) binding
- E179 (= E177) binding
- R180 (= R178) binding
- S229 (= S227) binding
- T251 (≠ G249) binding
- R283 (= R281) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ L285) 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 (≠ V350) 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 (= E384) binding
- C413 (≠ A415) mutation to A: No effect at either the structural or enzymatic levels; when associated with A-36; A-160; A-287 and A-351.
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
37% identity, 94% coverage: 8:479/500 of query aligns to 9:477/489 of 6wsbA
- active site: N152 (= N151), E250 (≠ M248), C284 (= C282), E462 (≠ L462)
- binding nicotinamide-adenine-dinucleotide: I148 (= I147), G149 (≠ T148), A150 (≠ P149), W151 (≠ F150), N152 (= N151), K175 (= K174), E178 (= E177), G208 (≠ K207), G211 (≠ V210), A212 (≠ E211), F225 (= F224), T226 (≠ V225), G227 (= G226), G228 (≠ S227), T231 (≠ I230), V235 (= V234), E250 (≠ M248), L251 (≠ G249), G252 (= G250), C284 (= C282), E385 (= E384), F387 (= F386)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
33% identity, 94% coverage: 8:479/500 of query aligns to 9:478/489 of 4cazA
- active site: N152 (= N151), K175 (= K174), E251 (≠ M248), C285 (= C282), E386 (= E384), E463 (≠ L462)
- 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 (= I147), G149 (≠ T148), W151 (≠ F150), N152 (= N151), K175 (= K174), E178 (= E177), G208 (vs. gap), G212 (≠ V210), F226 (= F224), T227 (≠ V225), G228 (= G226), G229 (≠ S227), T232 (≠ I230), V236 (= V234), E251 (≠ M248), L252 (≠ G249), C285 (= C282), E386 (= E384), F388 (= F386)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
33% identity, 94% coverage: 8:479/500 of query aligns to 9:478/489 of 2woxA
- active site: N152 (= N151), K175 (= K174), E251 (≠ M248), C285 (= C282), E386 (= E384), E463 (≠ L462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I147), G149 (≠ T148), W151 (≠ F150), N152 (= N151), K175 (= K174), S177 (= S176), E178 (= E177), G208 (vs. gap), G212 (≠ V210), F226 (= F224), T227 (≠ V225), G228 (= G226), G229 (≠ S227), T232 (≠ I230), V236 (= V234), E251 (≠ M248), L252 (≠ G249), C285 (= C282), E386 (= E384), F388 (= F386)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
33% identity, 94% coverage: 8:479/500 of query aligns to 9:478/489 of 2wmeA
- active site: N152 (= N151), K175 (= K174), E251 (≠ M248), C285 (= C282), E386 (= E384), E463 (≠ L462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T148), W151 (≠ F150), K175 (= K174), S177 (= S176), E178 (= E177), G208 (vs. gap), G212 (≠ V210), F226 (= F224), G228 (= G226), G229 (≠ S227), T232 (≠ I230), V236 (= V234)
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, 94% coverage: 8:479/500 of query aligns to 10:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 148:151) binding
- K162 (≠ M160) active site, Charge relay system
- KPSE 176:179 (= KPSE 174:177) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ SSDI 227:230) binding
- E252 (≠ M248) active site, Proton acceptor
- C286 (= C282) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E384) binding
- E464 (≠ L462) active site, Charge relay system
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
32% identity, 94% coverage: 8:479/500 of query aligns to 6:473/487 of 4go4A
- active site: N149 (= N151), K172 (= K174), E247 (≠ M248), C281 (= C282), E381 (= E384), E458 (≠ Q464)
- binding nicotinamide-adenine-dinucleotide: I145 (= I147), V146 (≠ T148), W148 (≠ F150), N149 (= N151), F154 (≠ I156), K172 (= K174), G205 (≠ K207), G209 (vs. gap), Q210 (≠ E211), F223 (= F224), T224 (≠ V225), G225 (= G226), S226 (= S227), T229 (≠ I230), E247 (≠ M248), G249 (= G250), C281 (= C282), E381 (= E384), F383 (= F386)
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, 96% coverage: 5:482/500 of query aligns to 10:486/487 of Q9H2A2
- R109 (= R105) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N151) mutation to A: Complete loss of activity.
- R451 (≠ P445) mutation to A: Complete loss of activity.
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8vqwC
- binding coenzyme a: I147 (= I147), W150 (≠ F150), K174 (= K174), S176 (= S176), E177 (= E177), G207 (≠ D206), G211 (≠ V210), F225 (= F224), G227 (= G226), G228 (≠ S227), S231 (≠ I230), H331 (= H330), F387 (= F386)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8vj3A
8uzoA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (adp bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8uzoA
8uznA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (amp bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8uznA
- binding adenosine monophosphate: I147 (= I147), G148 (≠ T148), K174 (= K174), S176 (= S176), E177 (= E177), G207 (≠ D206), G211 (≠ V210), F225 (= F224), G228 (≠ S227), S231 (≠ I230), K234 (≠ S233)
8uzmA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADPH bound)
33% identity, 94% coverage: 8:479/500 of query aligns to 8:477/488 of 8uzmA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G148 (≠ T148), W150 (≠ F150), K174 (= K174), S176 (= S176), E177 (= E177), G207 (≠ D206), G211 (≠ V210), F225 (= F224), T226 (≠ V225), G227 (= G226), G228 (≠ S227), S231 (≠ I230), E250 (≠ M248), G252 (= G250), C284 (= C282), E385 (= E384), F387 (= F386)
Query Sequence
>CCNA_01360 FitnessBrowser__Caulo:CCNA_01360
MMRDIPHFIGGQKVDGASGRFGEVFDPNTGKVQARVALASAGELNTAIANAKVAQAAWAA
TNPQRRARVMFEFKRLLEVHMDELAALLSSEHGKVIADSKGDIQRGLEVIEFACGVPHLL
KGEYTQGAGPGIDVYSMRQPLGVVAGITPFNFPAMIPMWMFGPAIATGNAFILKPSERDP
SVPVRLAELMIEAGLPPGVLNVVHGDKDCVEAILDHPDIKAVSFVGSSDIAQSVFQRAGA
AGKRVQAMGGAKNHGLVMPDADLDQAVADIIGAAYGSAGERCMALPVVVPVGEKTATALR
EKLVAAIGGLRVGVSTDPDAHYGPVVSAAHKARIESYIQMGVDEGAELVVDGRGFSLQGH
EEGFFVGPTLFDHVKPTSRSYHDEIFGPVLQMVRAESLEEGIALASRHQYGNGVAIFTRN
GDAAREFADQVEVGMVGINVPIPVPVAYHSFGGWKRSGFGDLNQYGMDGVRFYTRTKTVT
QRWPKGGAVLDQSFVIPTMR
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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