SitesBLAST
Comparing RR42_RS34225 FitnessBrowser__Cup4G11:RR42_RS34225 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)
56% identity, 95% coverage: 13:493/506 of query aligns to 4:484/489 of 4zz7A
- active site: N149 (= N159), K172 (= K182), L246 (= L256), C280 (= C290), E382 (= E391), A462 (= A471)
- binding nicotinamide-adenine-dinucleotide: T146 (= T156), P147 (= P157), F148 (= F158), N149 (= N159), K172 (= K182), E175 (= E185), K205 (= K215), V208 (= V218), F222 (= F232), V223 (= V233), G224 (= G234), S225 (= S235), I228 (= I238), L246 (= L256), G247 (= G257), C280 (= C290), E382 (= E391), F384 (= F393)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
54% identity, 95% coverage: 12:494/506 of query aligns to 6:489/491 of 4iymC
- active site: N153 (= N159), K176 (= K182), F250 (≠ L256), C284 (= C290), E386 (= E391), Q466 (≠ A471)
- binding nicotinamide-adenine-dinucleotide: I149 (= I155), T150 (= T156), P151 (= P157), F152 (= F158), N153 (= N159), F154 (= F160), K176 (= K182), K209 (= K215), V212 (= V218), F226 (= F232), V227 (= V233), G228 (= G234), S229 (= S235), I232 (= I238), G251 (= G257), C284 (= C290), E386 (= E391), F388 (= F393)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
55% identity, 97% coverage: 13:502/506 of query aligns to 3:468/468 of 5tjrD
- active site: N144 (= N159), K167 (= K182), L241 (= L256), C270 (= C290), E356 (= E391), A436 (= A471)
- binding adenosine-5'-diphosphate: I140 (= I155), T141 (= T156), F143 (= F158), K167 (= K182), E170 (= E185), K200 (= K215), F217 (= F232), S220 (= S235), I223 (= I238)
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)
45% identity, 95% coverage: 12:491/506 of query aligns to 6:482/487 of P42412
- C36 (≠ R42) 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 (= R113) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ T156) binding
- F152 (= F158) binding
- C160 (= C166) 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 (= K182) binding
- E179 (= E185) binding
- R180 (= R186) binding
- S229 (= S235) binding
- T251 (≠ G257) binding
- R283 (= R289) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ I293) 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 (≠ V357) 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 (= E391) binding
- C413 (≠ A422) 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
45% identity, 95% coverage: 12:491/506 of query aligns to 4:480/484 of 1t90A
- active site: N151 (= N159), K174 (= K182), L248 (= L256), C282 (= C290), E380 (= E391), A460 (= A471)
- binding nicotinamide-adenine-dinucleotide: I147 (= I155), A148 (≠ T156), P149 (= P157), F150 (= F158), N151 (= N159), W159 (= W167), K174 (= K182), E177 (= E185), R178 (= R186), H207 (≠ K215), V225 (= V233), G226 (= G234), S227 (= S235), V230 (≠ I238), L248 (= L256), T249 (≠ G257), C282 (= C290), E380 (= E391), F382 (= F393)
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)
31% identity, 93% coverage: 15:487/506 of query aligns to 20:492/505 of 4neaA
- active site: N166 (= N159), K189 (= K182), E264 (≠ L256), C298 (= C290), E399 (= E391), E476 (≠ A471)
- binding nicotinamide-adenine-dinucleotide: P164 (= P157), K189 (= K182), E192 (= E185), G222 (≠ D214), G226 (≠ V218), G242 (= G234), G243 (≠ S235), T246 (≠ I238), H249 (≠ Y241), I250 (= I242), C298 (= C290), E399 (= E391), F401 (= F393)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
31% identity, 93% coverage: 15:487/506 of query aligns to 22:493/503 of 1bpwA
- active site: N166 (= N159), K189 (= K182), E263 (≠ L256), C297 (= C290), E400 (= E391), E477 (≠ T469)
- binding nicotinamide-adenine-dinucleotide: I162 (= I155), L163 (≠ T156), W165 (≠ F158), N166 (= N159), K189 (= K182), G221 (≠ D214), G225 (≠ V218), T240 (≠ V233), G241 (= G234), S242 (= S235), T245 (≠ I238), E263 (≠ L256), L264 (≠ G257), C297 (= C290), E400 (= E391), F402 (= F393), F466 (= F458)
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, 93% coverage: 15:487/506 of query aligns to 22:493/503 of P56533
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
34% identity, 93% coverage: 15:486/506 of query aligns to 29:501/515 of 2d4eC
- active site: N173 (= N159), K196 (= K182), E271 (≠ L256), C305 (= C290), E409 (= E391), E486 (≠ A471)
- binding nicotinamide-adenine-dinucleotide: I169 (= I155), T170 (= T156), P171 (= P157), W172 (≠ F158), K196 (= K182), A198 (≠ S184), G229 (≠ D214), G233 (≠ V218), A234 (≠ D219), T248 (≠ V233), G249 (= G234), E250 (≠ S235), T253 (≠ I238), E271 (≠ L256), L272 (≠ G257), C305 (= C290), E409 (= E391), F411 (= F393), F475 (= F458)
6vr6D Structure of aldh9a1 complexed with NAD+ in space group p1 (see paper)
31% identity, 93% coverage: 15:486/506 of query aligns to 12:482/493 of 6vr6D
- active site: N156 (= N159), E253 (≠ L256), C287 (= C290), E467 (≠ T469)
- binding nicotinamide-adenine-dinucleotide: I152 (= I155), G153 (≠ T156), W155 (≠ F158), K179 (= K182), A212 (≠ K215), G215 (≠ V218), Q216 (≠ D219), F229 (= F232), G231 (= G234), S232 (= S235), T235 (≠ I238), I239 (= I242)
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, 93% coverage: 15:486/506 of query aligns to 13:483/494 of P49189
- C116 (≠ I117) 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
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
35% identity, 93% coverage: 16:487/506 of query aligns to 14:485/494 of 4pz2B
- active site: N159 (= N159), K182 (= K182), E258 (≠ L256), C292 (= C290), E392 (= E391), D469 (≠ T469)
- binding nicotinamide-adenine-dinucleotide: I155 (= I155), I156 (≠ T156), P157 (= P157), W158 (≠ F158), N159 (= N159), M164 (≠ V164), K182 (= K182), A184 (≠ S184), E185 (= E185), G215 (≠ D214), G219 (≠ V218), F233 (= F232), T234 (≠ V233), G235 (= G234), S236 (= S235), V239 (≠ I238), E258 (≠ L256), L259 (≠ G257), C292 (= C290), E392 (= E391), F394 (= F393)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
34% identity, 91% coverage: 17:475/506 of query aligns to 15:470/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
34% identity, 91% coverage: 17:475/506 of query aligns to 14:469/481 of 3jz4A
- active site: N156 (= N159), K179 (= K182), E254 (≠ L256), C288 (= C290), E385 (= E391), E462 (≠ D468)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P157), W155 (≠ F158), K179 (= K182), A181 (≠ S184), S182 (≠ E185), A212 (≠ K215), G216 (vs. gap), G232 (= G234), S233 (= S235), I236 (= I238), C288 (= C290), K338 (≠ R340), E385 (= E391), F387 (= F393)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
31% identity, 86% coverage: 16:450/506 of query aligns to 6:440/494 of 5izdA
- active site: N149 (= N159), K172 (= K182), E247 (≠ A255), C281 (= C290), E381 (= E391)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I155), T146 (= T156), W148 (≠ F158), K172 (= K182), P173 (= P183), S174 (= S184), S175 (≠ E185), R204 (≠ D214), G205 (≠ K215), G209 (vs. gap), D210 (= D219), G225 (= G234), S226 (= S235), T229 (≠ I238)
Sites not aligning to the query:
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
31% identity, 94% coverage: 12:486/506 of query aligns to 16:486/491 of 5gtlA
- active site: N165 (= N159), K188 (= K182), E263 (≠ L256), C297 (= C290), E394 (= E391), E471 (≠ A471)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I155), P163 (= P157), K188 (= K182), A190 (≠ S184), E191 (= E185), Q192 (≠ R186), G221 (≠ D214), G225 (≠ V218), G241 (= G234), S242 (= S235), T245 (≠ I238), L264 (≠ G257), C297 (= C290), E394 (= E391), F396 (= F393)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
31% identity, 94% coverage: 12:486/506 of query aligns to 16:486/491 of 5gtkA
- active site: N165 (= N159), K188 (= K182), E263 (≠ L256), C297 (= C290), E394 (= E391), E471 (≠ A471)
- binding nicotinamide-adenine-dinucleotide: I161 (= I155), I162 (≠ T156), P163 (= P157), W164 (≠ F158), K188 (= K182), E191 (= E185), G221 (≠ D214), G225 (≠ V218), A226 (≠ D219), F239 (= F232), G241 (= G234), S242 (= S235), T245 (≠ I238), Y248 (= Y241), L264 (≠ G257), C297 (= C290), Q344 (≠ A337), R347 (= R340), E394 (= E391), F396 (= F393)
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, 93% coverage: 16:486/506 of query aligns to 10:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 156:159) binding
- K162 (≠ M168) active site, Charge relay system
- KPSE 176:179 (= KPSE 182:185) binding
- G209 (vs. gap) binding
- GTST 230:233 (≠ STPI 235:238) binding
- E252 (≠ A255) active site, Proton acceptor
- C286 (= C290) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E391) binding
- E464 (≠ T469) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
31% identity, 93% coverage: 16:486/506 of query aligns to 9:478/489 of 4cazA
- active site: N152 (= N159), K175 (= K182), E251 (≠ A255), C285 (= C290), E386 (= E391), E463 (≠ T469)
- 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 (= I155), G149 (≠ T156), W151 (≠ F158), N152 (= N159), K175 (= K182), E178 (= E185), G208 (vs. gap), G212 (≠ V218), F226 (= F232), T227 (≠ V233), G228 (= G234), G229 (≠ S235), T232 (≠ I238), V236 (≠ I242), E251 (≠ A255), L252 (= L256), C285 (= C290), E386 (= E391), F388 (= F393)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
31% identity, 93% coverage: 16:486/506 of query aligns to 9:478/489 of 2woxA
- active site: N152 (= N159), K175 (= K182), E251 (≠ A255), C285 (= C290), E386 (= E391), E463 (≠ T469)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I155), G149 (≠ T156), W151 (≠ F158), N152 (= N159), K175 (= K182), S177 (= S184), E178 (= E185), G208 (vs. gap), G212 (≠ V218), F226 (= F232), T227 (≠ V233), G228 (= G234), G229 (≠ S235), T232 (≠ I238), V236 (≠ I242), E251 (≠ A255), L252 (= L256), C285 (= C290), E386 (= E391), F388 (= F393)
Query Sequence
>RR42_RS34225 FitnessBrowser__Cup4G11:RR42_RS34225
MKTPIAYTEGGQLGHYINGSRVASASGRAQDVFNPATGAAARSVALGSADEAGTAVAAAA
AAFAAWADTPPIRRARVMQRFLQLMNQHRDTLAAMITAEHGKVFSDAQGEVSRGIDIIEF
ACGIPQLLKGDYTDQVSTGMDNWTLRQPLGVVVGITPFNFPCMVPCWMFPIALAAGNTFV
LKPSERDPSASLFMADLLTEAGLPAGVFNVVQGDKVVVDALIAHPEVKAVSFVGSTPIAQ
YISERSAHFGKRVQALGGAKNHLVVMPDADIEQAVDALIGAGYGSAGERCMAISIAVLVG
DVADKILPLLAERVKALVIGNGMNAEAEMGPIVTRQALERIEGYVGLGVAEGATLVVDGR
DCRVPGHEAGFFTGGTLFDNVTPAMRIYKEEIFGPVLGCVRVKDFAQAVQLVNDHEFGNG
VACYTSDGGVAREFARRIQVGMVGINVPIPVPMAWHGFGGWKRSLFGDTHAYGEEGVRFY
TKQKSVMQRWPDSIGKGAEFAMPTAK
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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