SitesBLAST
Comparing RR42_RS01580 FitnessBrowser__Cup4G11:RR42_RS01580 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)
60% identity, 96% coverage: 9:492/505 of query aligns to 1:484/489 of 4zz7A
- active site: N149 (= N158), K172 (= K181), L246 (= L255), C280 (= C289), E382 (= E390), A462 (= A470)
- binding nicotinamide-adenine-dinucleotide: T146 (= T155), P147 (= P156), F148 (= F157), N149 (= N158), K172 (= K181), E175 (= E184), K205 (= K214), V208 (= V217), F222 (= F231), V223 (= V232), G224 (= G233), S225 (= S234), I228 (= I237), L246 (= L255), G247 (= G256), C280 (= C289), E382 (= E390), F384 (= F392)
5tjrD X-ray crystal structure of a methylmalonate semialdehyde dehydrogenase from pseudomonas sp. Aac (see paper)
61% identity, 95% coverage: 12:491/505 of query aligns to 3:457/468 of 5tjrD
- active site: N144 (= N158), K167 (= K181), L241 (= L255), C270 (= C289), E356 (= E390), A436 (= A470)
- binding adenosine-5'-diphosphate: I140 (= I154), T141 (= T155), F143 (= F157), K167 (= K181), E170 (= E184), K200 (= K214), F217 (= F231), S220 (= S234), I223 (= I237)
4iymC Crystal structure of putative methylmalonate-semialdehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD, target 011934
56% identity, 96% coverage: 11:493/505 of query aligns to 6:489/491 of 4iymC
- active site: N153 (= N158), K176 (= K181), F250 (≠ L255), C284 (= C289), E386 (= E390), Q466 (≠ A470)
- binding nicotinamide-adenine-dinucleotide: I149 (= I154), T150 (= T155), P151 (= P156), F152 (= F157), N153 (= N158), F154 (= F159), K176 (= K181), K209 (= K214), V212 (= V217), F226 (= F231), V227 (= V232), G228 (= G233), S229 (= S234), I232 (= I237), G251 (= G256), C284 (= C289), E386 (= E390), F388 (= F392)
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, 96% coverage: 8:490/505 of query aligns to 3:482/487 of P42412
- C36 (≠ G41) 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
- F152 (= F157) binding
- C160 (≠ M165) 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
- E179 (= E184) binding
- R180 (= R185) binding
- S229 (= S234) binding
- T251 (≠ G256) binding
- 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 (≠ T356) 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 (= E390) binding
- C413 (≠ S421) 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
48% identity, 96% coverage: 8:490/505 of query aligns to 1:480/484 of 1t90A
- active site: N151 (= N158), K174 (= K181), L248 (= L255), C282 (= C289), E380 (= E390), A460 (= A470)
- binding nicotinamide-adenine-dinucleotide: I147 (= I154), A148 (≠ T155), P149 (= P156), F150 (= F157), N151 (= N158), W159 (= W166), K174 (= K181), E177 (= E184), R178 (= R185), H207 (≠ K214), V225 (= V232), G226 (= G233), S227 (= S234), V230 (≠ I237), L248 (= L255), T249 (≠ G256), C282 (= C289), E380 (= E390), F382 (= F392)
2d4eC Crystal structure of the hpcc from thermus thermophilus hb8
34% identity, 93% coverage: 14:485/505 of query aligns to 29:501/515 of 2d4eC
- active site: N173 (= N158), K196 (= K181), E271 (≠ L255), C305 (= C289), E409 (= E390), E486 (≠ A470)
- binding nicotinamide-adenine-dinucleotide: I169 (= I154), T170 (= T155), P171 (= P156), W172 (≠ F157), K196 (= K181), A198 (≠ S183), G229 (= G213), G233 (≠ V217), A234 (≠ D218), T248 (≠ V232), G249 (= G233), E250 (≠ S234), T253 (≠ I237), E271 (≠ L255), L272 (≠ G256), C305 (= C289), E409 (= E390), F411 (= F392), F475 (= F457)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8vqwC
- binding coenzyme a: I147 (= I154), W150 (≠ F157), K174 (= K181), S176 (= S183), E177 (= E184), G207 (= G213), G211 (≠ V217), F225 (= F231), G227 (= G233), G228 (≠ S234), S231 (≠ I237), H331 (= H336), F387 (= F392)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8vj3A
8uzoA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (adp bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8uzoA
8uznA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (amp bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8uznA
- binding adenosine monophosphate: I147 (= I154), G148 (≠ T155), K174 (= K181), S176 (= S183), E177 (= E184), G207 (= G213), G211 (≠ V217), F225 (= F231), G228 (≠ S234), S231 (≠ I237), K234 (≠ Y240)
8uzmA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADPH bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8uzmA
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G148 (≠ T155), W150 (≠ F157), K174 (= K181), S176 (= S183), E177 (= E184), G207 (= G213), G211 (≠ V217), F225 (= F231), T226 (≠ V232), G227 (= G233), G228 (≠ S234), S231 (≠ I237), E250 (≠ L255), G252 (= G257), C284 (= C289), E385 (= E390), F387 (= F392)
8uzkA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (NADP+ bound)
34% identity, 95% coverage: 8:485/505 of query aligns to 1:477/488 of 8uzkA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I147 (= I154), G148 (≠ T155), W150 (≠ F157), N151 (= N158), K174 (= K181), S176 (= S183), E177 (= E184), G207 (= G213), G211 (≠ V217), F225 (= F231), G227 (= G233), G228 (≠ S234), S231 (≠ I237), E250 (≠ L255), F387 (= F392)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
34% identity, 95% coverage: 8:485/505 of query aligns to 10:486/497 of 8skfA
- binding calcium ion: T33 (≠ V31), I34 (≠ F32), D100 (≠ E98), V187 (≠ R185)
- binding nicotinamide-adenine-dinucleotide: I156 (= I154), G157 (≠ T155), A158 (≠ P156), W159 (≠ F157), K183 (= K181), E186 (= E184), G216 (= G213), G220 (≠ V217), T235 (≠ V232), G236 (= G233), G237 (≠ S234), S240 (≠ I237), K243 (≠ Y240), E259 (≠ L255), C293 (= C289), F396 (= F392)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 94% coverage: 11:485/505 of query aligns to 16:486/491 of 5gtlA
- active site: N165 (= N158), K188 (= K181), E263 (≠ L255), C297 (= C289), E394 (= E390), E471 (≠ A470)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I154), P163 (= P156), K188 (= K181), A190 (≠ S183), E191 (= E184), Q192 (≠ R185), G221 (= G213), G225 (≠ V217), G241 (= G233), S242 (= S234), T245 (≠ I237), L264 (≠ G256), C297 (= C289), E394 (= E390), F396 (= F392)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
33% identity, 94% coverage: 11:485/505 of query aligns to 16:486/491 of 5gtkA
- active site: N165 (= N158), K188 (= K181), E263 (≠ L255), C297 (= C289), E394 (= E390), E471 (≠ A470)
- binding nicotinamide-adenine-dinucleotide: I161 (= I154), I162 (≠ T155), P163 (= P156), W164 (≠ F157), K188 (= K181), E191 (= E184), G221 (= G213), G225 (≠ V217), A226 (≠ D218), F239 (= F231), G241 (= G233), S242 (= S234), T245 (≠ I237), Y248 (= Y240), L264 (≠ G256), C297 (= C289), Q344 (≠ H336), R347 (≠ K339), E394 (= E390), F396 (= F392)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
37% identity, 93% coverage: 15:485/505 of query aligns to 14:481/494 of 4pz2B
- active site: N159 (= N158), K182 (= K181), E258 (≠ L255), C292 (= C289), E392 (= E390), D469 (≠ E473)
- binding nicotinamide-adenine-dinucleotide: I155 (= I154), I156 (≠ T155), P157 (= P156), W158 (≠ F157), N159 (= N158), M164 (≠ V163), K182 (= K181), A184 (≠ S183), E185 (= E184), G215 (= G213), G219 (≠ V217), F233 (= F231), T234 (≠ V232), G235 (= G233), S236 (= S234), V239 (≠ I237), E258 (≠ L255), L259 (≠ G256), C292 (= C289), E392 (= E390), F394 (= F392)
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, 93% coverage: 15:485/505 of query aligns to 10:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPFN 155:158) binding
- K162 (≠ M167) active site, Charge relay system
- KPSE 176:179 (= KPSE 181:184) binding
- G209 (= G213) binding
- GTST 230:233 (≠ STPI 234:237) binding
- E252 (≠ L255) active site, Proton acceptor
- C286 (= C289) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E390) binding
- E464 (≠ H468) active site, Charge relay system
Query Sequence
>RR42_RS01580 FitnessBrowser__Cup4G11:RR42_RS01580
MNIAENRQIADIAHYIGGTVRAASSDRFADVFNPATGAVAGRVALGSAQDVDAAVAAAHA
AFPAWSETAPLKRARILFKFKELLDRHHDDLAALITREHGKVFSDAKGEVTRGVEIVEFA
CGIPNLLKTDFTDNIGGGIDNWNLRQPLGVVAGITPFNFPVMVPMWMFPVALACGNTFVL
KPSERDPSPSLLIADLLKQAGLPDGVFNVVQGGKEAVDALLAHKDVQALSFVGSTPIAEY
IYTEGTRRGKRVQALGGAKNHLVVMPDADLDQAVDALIGAAYGSAGERCMAISVAVAVGD
VADKLVPRLAERARSLKIRNGMQDDAEMGPLVTAAHKAKVEGYIAKGVEEGAKLVTDGRG
HKVDGHENGFYVGGTLFDNVTPDMTIYKEEIFGPVLSVVRVHDLAEAVDLINGHEYGNGV
SCYTSDGGVARAFSRQIQVGMVGINVPIPVPMAWHSFGGWKRSLFGDHHAYGEEGIRFYT
RYKSIMQRWPDSIGKGAEFTMPVAK
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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