SitesBLAST
Comparing 7025959 FitnessBrowser__ANA3:7025959 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)
61% identity, 97% coverage: 1:481/496 of query aligns to 1:482/489 of 4zz7A
- active site: N149 (= N149), K172 (= K172), L246 (= L246), C280 (= C280), E382 (= E381), A462 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: T146 (≠ A146), P147 (= P147), F148 (= F148), N149 (= N149), K172 (= K172), E175 (= E175), K205 (= K205), V208 (= V208), F222 (= F222), V223 (= V223), G224 (= G224), S225 (= S225), I228 (= I228), L246 (= L246), G247 (= G247), C280 (= C280), E382 (= E381), F384 (= F383)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
59% identity, 98% coverage: 4:488/496 of query aligns to 3:463/468 of 5tjrD
- active site: N144 (= N149), K167 (= K172), L241 (= L246), C270 (= C280), E356 (= E381), A436 (≠ M461)
- binding adenosine-5'-diphosphate: I140 (= I145), T141 (≠ A146), F143 (= F148), K167 (= K172), E170 (= E175), K200 (= K205), F217 (= F222), S220 (= S225), I223 (= I228)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
55% identity, 97% coverage: 1:483/496 of query aligns to 4:488/491 of 4iymC
- active site: N153 (= N149), K176 (= K172), F250 (≠ L246), C284 (= C280), E386 (= E381), Q466 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I149 (= I145), T150 (≠ A146), P151 (= P147), F152 (= F148), N153 (= N149), F154 (= F150), K176 (= K172), K209 (= K205), V212 (= V208), F226 (= F222), V227 (= V223), G228 (= G224), S229 (= S225), I232 (= I228), G251 (= G247), C284 (= C280), E386 (= E381), F388 (= F383)
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)
47% identity, 96% coverage: 4:481/496 of query aligns to 7:482/487 of P42412
- C36 (≠ G32) 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 (= R103) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (= A146) binding
- F152 (= F148) binding
- C160 (≠ M156) 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 (= K172) binding
- E179 (= E175) binding
- R180 (≠ K176) binding
- S229 (= S225) binding
- T251 (≠ G247) binding
- R283 (= R279) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I283) 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 (≠ V347) 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 (= E381) binding
- C413 (≠ A412) 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
47% identity, 96% coverage: 4:481/496 of query aligns to 5:480/484 of 1t90A
- active site: N151 (= N149), K174 (= K172), L248 (= L246), C282 (= C280), E380 (= E381), A460 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I147 (= I145), A148 (= A146), P149 (= P147), F150 (= F148), N151 (= N149), W159 (= W157), K174 (= K172), E177 (= E175), R178 (≠ K176), H207 (≠ K205), V225 (= V223), G226 (= G224), S227 (= S225), V230 (≠ I228), L248 (= L246), T249 (≠ G247), C282 (= C280), E380 (= E381), F382 (= F383)
P49189 4-trimethylaminobutyraldehyde dehydrogenase; TMABA-DH; TMABALDH; Aldehyde dehydrogenase E3 isozyme; Aldehyde dehydrogenase family 9 member A1; Formaldehyde dehydrogenase; Gamma-aminobutyraldehyde dehydrogenase; R-aminobutyraldehyde dehydrogenase; EC 1.2.1.47; EC 1.2.1.3; EC 1.2.1.46; EC 1.2.1.19 from Homo sapiens (Human) (see 2 papers)
31% identity, 94% coverage: 14:477/496 of query aligns to 23:484/494 of P49189
- C116 (≠ V107) to S: in allele ALDH9A1*2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed; alternate
- 2 modified: N-acetylserine; in 4-trimethylaminobutyraldehyde dehydrogenase, N-terminally processed
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
31% identity, 94% coverage: 14:477/496 of query aligns to 22:483/493 of 6vr6D
- active site: N156 (= N149), E253 (≠ L246), C287 (= C280), E467 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I152 (= I145), G153 (≠ A146), W155 (≠ F148), K179 (= K172), A212 (≠ K205), G215 (≠ V208), Q216 (≠ D209), F229 (= F222), G231 (= G224), S232 (= S225), T235 (≠ I228), I239 (= I232)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
31% identity, 92% coverage: 19:476/496 of query aligns to 37:492/503 of 1bpwA
- active site: N166 (= N149), K189 (= K172), E263 (≠ L246), C297 (= C280), E400 (= E381), E477 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I162 (= I145), L163 (≠ A146), W165 (≠ F148), N166 (= N149), K189 (= K172), G221 (≠ D204), G225 (≠ V208), T240 (≠ V223), G241 (= G224), S242 (= S225), T245 (≠ I228), E263 (≠ L246), L264 (≠ G247), C297 (= C280), E400 (= E381), F402 (= F383), F466 (= F448)
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, 92% coverage: 19:476/496 of query aligns to 37:492/503 of P56533
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
31% identity, 95% coverage: 7:476/496 of query aligns to 9:478/489 of 4cazA
- active site: N152 (= N149), K175 (= K172), E251 (≠ L246), C285 (= C280), E386 (= E381), E463 (≠ M461)
- 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 (= I145), G149 (≠ A146), W151 (≠ F148), N152 (= N149), K175 (= K172), E178 (= E175), G208 (vs. gap), G212 (≠ V208), F226 (= F222), T227 (≠ V223), G228 (= G224), G229 (≠ S225), T232 (≠ I228), V236 (≠ I232), E251 (≠ L246), L252 (≠ G247), C285 (= C280), E386 (= E381), F388 (= F383)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
31% identity, 95% coverage: 7:476/496 of query aligns to 9:478/489 of 2woxA
- active site: N152 (= N149), K175 (= K172), E251 (≠ L246), C285 (= C280), E386 (= E381), E463 (≠ M461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I145), G149 (≠ A146), W151 (≠ F148), N152 (= N149), K175 (= K172), S177 (= S174), E178 (= E175), G208 (vs. gap), G212 (≠ V208), F226 (= F222), T227 (≠ V223), G228 (= G224), G229 (≠ S225), T232 (≠ I228), V236 (≠ I232), E251 (≠ L246), L252 (≠ G247), C285 (= C280), E386 (= E381), F388 (= F383)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
31% identity, 95% coverage: 7:476/496 of query aligns to 9:478/489 of 2wmeA
- active site: N152 (= N149), K175 (= K172), E251 (≠ L246), C285 (= C280), E386 (= E381), E463 (≠ M461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ A146), W151 (≠ F148), K175 (= K172), S177 (= S174), E178 (= E175), G208 (vs. gap), G212 (≠ V208), F226 (= F222), G228 (= G224), G229 (≠ S225), T232 (≠ I228), V236 (≠ I232)
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: 7:476/496 of query aligns to 10:479/490 of Q9HTJ1
- GAWN 150:153 (≠ APFN 146:149) binding
- K162 (≠ M158) active site, Charge relay system
- KPSE 176:179 (= KPSE 172:175) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ STPI 225:228) binding
- E252 (≠ L246) active site, Proton acceptor
- C286 (= C280) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E381) binding
- E464 (≠ M461) active site, Charge relay system
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
33% identity, 95% coverage: 6:476/496 of query aligns to 29:501/515 of 2d4eC
- active site: N173 (= N149), K196 (= K172), E271 (≠ L246), C305 (= C280), E409 (= E381), E486 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I169 (= I145), T170 (≠ A146), P171 (= P147), W172 (≠ F148), K196 (= K172), A198 (≠ S174), G229 (≠ D204), G233 (≠ V208), A234 (≠ D209), T248 (≠ V223), G249 (= G224), E250 (≠ S225), T253 (≠ I228), E271 (≠ L246), L272 (≠ G247), C305 (= C280), E409 (= E381), F411 (= F383), F475 (= F448)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
31% identity, 95% coverage: 7:476/496 of query aligns to 20:486/491 of 5gtlA
- active site: N165 (= N149), K188 (= K172), E263 (≠ L246), C297 (= C280), E394 (= E381), E471 (≠ M461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I145), P163 (= P147), K188 (= K172), A190 (≠ S174), E191 (= E175), Q192 (≠ K176), G221 (≠ D204), G225 (≠ V208), G241 (= G224), S242 (= S225), T245 (≠ I228), L264 (≠ G247), C297 (= C280), E394 (= E381), F396 (= F383)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
31% identity, 95% coverage: 7:476/496 of query aligns to 20:486/491 of 5gtkA
- active site: N165 (= N149), K188 (= K172), E263 (≠ L246), C297 (= C280), E394 (= E381), E471 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ A146), P163 (= P147), W164 (≠ F148), K188 (= K172), E191 (= E175), G221 (≠ D204), G225 (≠ V208), A226 (≠ D209), F239 (= F222), G241 (= G224), S242 (= S225), T245 (≠ I228), Y248 (= Y231), L264 (≠ G247), C297 (= C280), Q344 (≠ H327), R347 (≠ K330), E394 (= E381), F396 (= F383)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
32% identity, 95% coverage: 7:476/496 of query aligns to 9:477/489 of 6wsbA
- active site: N152 (= N149), E250 (≠ L246), C284 (= C280), E462 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: I148 (= I145), G149 (≠ A146), A150 (≠ P147), W151 (≠ F148), N152 (= N149), K175 (= K172), E178 (= E175), G208 (≠ K205), G211 (≠ V208), A212 (≠ D209), F225 (= F222), T226 (≠ V223), G227 (= G224), G228 (≠ S225), T231 (≠ I228), V235 (≠ I232), E250 (≠ L246), L251 (≠ G247), G252 (= G248), C284 (= C280), E385 (= E381), F387 (= F383)
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, 96% coverage: 2:476/496 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N149), K189 (= K172), E264 (≠ L246), C298 (= C280), E399 (= E381), E476 (≠ M461)
- binding nicotinamide-adenine-dinucleotide: P164 (= P147), K189 (= K172), E192 (= E175), G222 (≠ D204), G226 (≠ V208), G242 (= G224), G243 (≠ S225), T246 (≠ I228), H249 (≠ Y231), I250 (= I232), C298 (= C280), E399 (= E381), F401 (= F383)
7um9A Human aldh1a1 with bound compound cm38 (see paper)
31% identity, 95% coverage: 7:479/496 of query aligns to 17:488/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I145), I160 (≠ A146), P161 (= P147), W162 (≠ F148), N163 (= N149), K186 (= K172), E189 (= E175), G219 (≠ D204), G223 (≠ V208), F237 (= F222), T238 (≠ V223), G239 (= G224), S240 (= S225), V243 (≠ I228), E262 (≠ L246), G264 (= G248), Q343 (≠ H327), K346 (= K330), E393 (= E381), F395 (= F383)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (= W157), H286 (≠ G270), Y290 (≠ G274), I297 (≠ M281), G451 (≠ P440)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
31% identity, 95% coverage: 7:479/496 of query aligns to 17:488/494 of 5l2oA
Query Sequence
>7025959 FitnessBrowser__ANA3:7025959
MLTMTHYVNGEHTAASTRSQEIFEPATGECRGQVSLASRDEVSAAIAIAKSAFDTWSQVT
PLNRARVLFKFKALVEQHMDELAQLITLEHGKVLDDARGELIRGLEVVEFACGIPHLLKG
EHTEQVGGGVDAWSVNQALGVVAGIAPFNFPVMVPMWMFPIAIACGNTFIMKPSEKDPSA
VMRIAELLTQAGLPAGVFNVVNGDKEAVDTLLSHEDIQAVSFVGSTPIAEYIYSTASKHG
KRVQALGGAKNHMLLMPDADLDQAVSALMGAAYGSAGERCMAISVVLAVGDVGDKLVDKL
LPQIQQLKVGNGLTPEMEMGPLISRQHLAKVTEFVDAGVKEGATLVVDGRQLTVADHQQG
YFLGACLFDNVTPEMRIYREEIFGPVLSIVRVKDYASALALINQHEFGNGTAIFTQSGEA
ARHFCHHVQVGMVGVNVPIPVPMAFHSFGGWKRSLFGPLHMHGPDGVRFYTKRKAITARW
PVGKQTQAEFVMPTMK
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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