SitesBLAST
Comparing RR42_RS18500 FitnessBrowser__Cup4G11:RR42_RS18500 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)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
62% identity, 97% coverage: 14:492/492 of query aligns to 22:504/504 of 6dbbA
- active site: N152 (= N144), E259 (= E246), C293 (= C280), E471 (= E459)
- binding nicotinamide-adenine-dinucleotide: I148 (= I140), S149 (= S141), A150 (= A142), F151 (= F143), N152 (= N144), K175 (= K167), S177 (= S169), R218 (≠ P205), T236 (= T223), G237 (= G224), S238 (= S225), M241 (= M228), E259 (= E246), L260 (= L247), G261 (= G248), C293 (= C280), E391 (= E379), F393 (= F381)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I140), S149 (= S141), A150 (= A142), F151 (= F143), N152 (= N144), K175 (= K167), S177 (= S169), R218 (≠ P205), T236 (= T223), G237 (= G224), S238 (= S225), M241 (= M228), E259 (= E246), L260 (= L247), G261 (= G248), C293 (= C280), E391 (= E379), F393 (= F381)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
59% identity, 97% coverage: 14:490/492 of query aligns to 32:508/509 of 6rtsA
- active site: N162 (= N144), E263 (= E246), C297 (= C280), E477 (= E459)
- binding nicotinamide-adenine-dinucleotide: I158 (= I140), S159 (= S141), A160 (= A142), F161 (= F143), N162 (= N144), K185 (= K167), S187 (= S169), E188 (= E170), A222 (≠ P205), G225 (= G208), T240 (= T223), G241 (= G224), S242 (= S225), M245 (= M228), E263 (= E246), L264 (= L247), C297 (= C280), E397 (= E379), F399 (= F381)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
59% identity, 97% coverage: 14:490/492 of query aligns to 31:507/508 of 6rttA
- active site: N161 (= N144), E262 (= E246), C296 (= C280), E476 (= E459)
- binding pyridine-2-carboxylic acid: A159 (= A142), F162 (= F145), V166 (= V149), W169 (= W152), G240 (= G224), S241 (= S225), R295 (= R279), C296 (= C280), T297 (= T281), E396 (= E379), F398 (= F381), P421 (≠ E404), K469 (= K452), E470 (≠ A453)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
59% identity, 97% coverage: 14:490/492 of query aligns to 31:504/505 of 6rtuA
- active site: N161 (= N144), E259 (= E246), C293 (= C280), E473 (= E459)
- binding 2-aminohexanedioic acid: E115 (= E98), F162 (= F145), R292 (= R279), C293 (= C280), T294 (= T281), S454 (= S440), G455 (= G441), A456 (= A442), F462 (= F448)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
48% identity, 96% coverage: 20:490/492 of query aligns to 42:509/509 of 2jg7A
- active site: N166 (= N144), K189 (= K167), E267 (= E246), C301 (= C280), E398 (= E379), E478 (= E459)
- binding nicotinamide-adenine-dinucleotide: I162 (= I140), T163 (≠ S141), A164 (= A142), F165 (= F143), N166 (= N144), K189 (= K167), P192 (≠ E170), A226 (≠ P205), G229 (= G208), T230 (≠ Q209), F243 (≠ A222), T244 (= T223), G245 (= G224), S246 (= S225), V249 (≠ M228), E267 (= E246), L268 (= L247), C301 (= C280), E398 (= E379), F400 (= F381)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
48% identity, 96% coverage: 20:491/492 of query aligns to 41:509/509 of 4zulA
- active site: N165 (= N144), K188 (= K167), E266 (= E246), C300 (= C280), E397 (= E379), E477 (= E459)
- binding 2-aminohexanedioic acid: E119 (= E98), F166 (= F145), R299 (= R279), C300 (= C280), T301 (= T281), G459 (= G441), A460 (= A442), F466 (= F448)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
48% identity, 96% coverage: 20:491/492 of query aligns to 41:509/509 of 4x0tA
- active site: N165 (= N144), K188 (= K167), E266 (= E246), C300 (= C280), E397 (= E379), E477 (= E459)
- binding 4-(diethylamino)benzaldehyde: F166 (= F145), V170 (= V149), W173 (= W152), C300 (= C280), F466 (= F448)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S141), A163 (= A142), F164 (= F143), N165 (= N144), K188 (= K167), G189 (≠ P168), A190 (≠ S169), A225 (≠ P205), G228 (= G208), T229 (≠ Q209), F242 (≠ A222), T243 (= T223), G244 (= G224), S245 (= S225), V248 (≠ M228), E266 (= E246), L267 (= L247), C300 (= C280), E397 (= E379), F399 (= F381)
P49419 Alpha-aminoadipic semialdehyde dehydrogenase; Alpha-AASA dehydrogenase; Aldehyde dehydrogenase family 7 member A1; Antiquitin-1; Betaine aldehyde dehydrogenase; Delta1-piperideine-6-carboxylate dehydrogenase; P6c dehydrogenase; EC 1.2.1.31; EC 1.2.1.3; EC 1.2.1.8 from Homo sapiens (Human) (see 5 papers)
48% identity, 96% coverage: 20:491/492 of query aligns to 71:539/539 of P49419
- 110:539 (vs. 59:491, 50% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- TAF 192:194 (≠ SAF 141:143) binding
- A199 (= A148) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K167) binding
- GT 258:259 (≠ GQ 208:209) binding
- GS 274:275 (= GS 224:225) binding
- EL 296:297 (= EL 246:247) binding
- C330 (= C280) active site, Nucleophile
- E427 (= E379) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ T391) to Q: in dbSNP:rs12514417
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
47% identity, 97% coverage: 8:485/492 of query aligns to 27:498/498 of 4pxnA
- active site: N161 (= N144), K184 (= K167), E262 (= E246), C296 (= C280), E392 (= E379), E472 (= E459)
- binding nicotinamide-adenine-dinucleotide: I157 (= I140), T158 (≠ S141), A159 (= A142), F160 (= F143), N161 (= N144), K184 (= K167), T221 (≠ P205), G224 (= G208), Q225 (= Q209), F238 (≠ A222), T239 (= T223), G240 (= G224), S241 (= S225), A244 (≠ M228), V248 (= V232), E262 (= E246), L263 (= L247), S264 (≠ G248), C296 (= C280), E392 (= E379), F394 (= F381), F461 (= F448)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
48% identity, 96% coverage: 20:491/492 of query aligns to 42:510/510 of 6o4dB
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
48% identity, 93% coverage: 20:478/492 of query aligns to 41:496/497 of 2j6lA
- active site: N165 (= N144), K188 (= K167), E266 (= E246), C300 (= C280), E397 (= E379), E477 (= E459)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I140), T162 (≠ S141), A163 (= A142), F164 (= F143), N165 (= N144), K188 (= K167), A225 (≠ P205), G228 (= G208), T229 (≠ Q209), F242 (≠ A222), T243 (= T223), G244 (= G224), S245 (= S225), V248 (≠ M228), E266 (= E246), L267 (= L247), C300 (= C280), E397 (= E379), F399 (= F381)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
46% identity, 93% coverage: 20:478/492 of query aligns to 41:486/487 of 4x0uD
- active site: N165 (= N144), K188 (= K167), E266 (= E246), C300 (= C280), E397 (= E379), E467 (= E459)
- binding 4-(diethylamino)benzaldehyde: F166 (= F145), A169 (= A148), V170 (= V149), C300 (= C280), F456 (= F448), H461 (≠ A453)
- binding magnesium ion: E119 (= E98), D122 (= D101)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 94% coverage: 16:478/492 of query aligns to 20:477/477 of 6j76A
- active site: N148 (= N144), E246 (= E246), C280 (= C280), E458 (= E459)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I140), T145 (≠ S141), A146 (= A142), W147 (≠ F143), N148 (= N144), K171 (= K167), T173 (≠ S169), S174 (≠ E170), G204 (= G204), G208 (= G208), T223 (= T223), G224 (= G224), S225 (= S225), A228 (≠ M228), S231 (≠ A231), I232 (≠ V232), E246 (= E246), L247 (= L247), C280 (= C280), E381 (= E379), F383 (= F381), H447 (≠ F448)
6fkuA Structure and function of aldehyde dehydrogenase from thermus thermophilus: an enzyme with an evolutionarily-distinct c-terminal arm (recombinant protein with shortened c-terminal, in complex with NADP) (see paper)
33% identity, 97% coverage: 9:486/492 of query aligns to 25:510/511 of 6fkuA
- active site: N159 (= N144), E261 (= E246), C295 (= C280), E483 (= E459)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I140), T156 (≠ S141), N159 (= N144), K182 (= K167), S184 (= S169), E185 (= E170), G214 (= G203), G215 (= G204), K216 (≠ P205), G220 (= G208), Q221 (= Q209), F237 (≠ A222), T238 (= T223), G239 (= G224), S240 (= S225), V243 (≠ M228), E261 (= E246), L262 (= L247), C295 (= C280), R342 (vs. gap), F343 (vs. gap), E404 (= E379), F406 (= F381)
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: 19:480/492 of query aligns to 28:485/490 of Q9HTJ1
- GAWN 150:153 (≠ SAFN 141:144) binding
- K162 (≠ N153) active site, Charge relay system
- KPSE 176:179 (= KPSE 167:170) binding
- G209 (= G204) binding
- GTST 230:233 (≠ STRM 225:228) binding
- E252 (= E246) active site, Proton acceptor
- C286 (= C280) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E379) binding
- E464 (= E459) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
33% identity, 94% coverage: 19:480/492 of query aligns to 27:484/489 of 4cazA
- active site: N152 (= N144), K175 (= K167), E251 (= E246), C285 (= C280), E386 (= E379), E463 (= E459)
- 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 (= I140), G149 (≠ S141), W151 (≠ F143), N152 (= N144), K175 (= K167), E178 (= E170), G208 (= G204), G212 (= G208), F226 (≠ A222), T227 (= T223), G228 (= G224), G229 (≠ S225), T232 (≠ M228), V236 (= V232), E251 (= E246), L252 (= L247), C285 (= C280), E386 (= E379), F388 (= F381)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
33% identity, 94% coverage: 19:480/492 of query aligns to 27:484/489 of 2woxA
- active site: N152 (= N144), K175 (= K167), E251 (= E246), C285 (= C280), E386 (= E379), E463 (= E459)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I140), G149 (≠ S141), W151 (≠ F143), N152 (= N144), K175 (= K167), S177 (= S169), E178 (= E170), G208 (= G204), G212 (= G208), F226 (≠ A222), T227 (= T223), G228 (= G224), G229 (≠ S225), T232 (≠ M228), V236 (= V232), E251 (= E246), L252 (= L247), C285 (= C280), E386 (= E379), F388 (= F381)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
33% identity, 94% coverage: 19:480/492 of query aligns to 27:484/489 of 2wmeA
- active site: N152 (= N144), K175 (= K167), E251 (= E246), C285 (= C280), E386 (= E379), E463 (= E459)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ S141), W151 (≠ F143), K175 (= K167), S177 (= S169), E178 (= E170), G208 (= G204), G212 (= G208), F226 (≠ A222), G228 (= G224), G229 (≠ S225), T232 (≠ M228), V236 (= V232)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
31% identity, 95% coverage: 19:484/492 of query aligns to 27:487/489 of 6wsbA
- active site: N152 (= N144), E250 (= E246), C284 (= C280), E462 (= E459)
- binding nicotinamide-adenine-dinucleotide: I148 (= I140), G149 (≠ S141), A150 (= A142), W151 (≠ F143), N152 (= N144), K175 (= K167), E178 (= E170), G208 (≠ P205), G211 (= G208), A212 (≠ Q209), F225 (≠ A222), T226 (= T223), G227 (= G224), G228 (≠ S225), T231 (≠ M228), V235 (= V232), E250 (= E246), L251 (= L247), G252 (= G248), C284 (= C280), E385 (= E379), F387 (= F381)
1bpwA Betaine aldehyde dehydrogenase from cod liver (see paper)
29% identity, 95% coverage: 16:480/492 of query aligns to 39:498/503 of 1bpwA
- active site: N166 (= N144), K189 (= K167), E263 (= E246), C297 (= C280), E400 (= E379), E477 (= E459)
- binding nicotinamide-adenine-dinucleotide: I162 (= I140), L163 (≠ S141), W165 (≠ F143), N166 (= N144), K189 (= K167), G221 (= G204), G225 (= G208), T240 (= T223), G241 (= G224), S242 (= S225), T245 (≠ M228), E263 (= E246), L264 (= L247), C297 (= C280), E400 (= E379), F402 (= F381), F466 (= F448)
Query Sequence
>RR42_RS18500 FitnessBrowser__Cup4G11:RR42_RS18500
MTPPWRDGEGPTGALPVRSPIDGEAFGHLPACSLAEADARIERARVMQASWALVPAPVRG
EVVRRFGEVLREHKKHLGELVSLEAGKILQEGLGEVQEMIDICDFAVGLSRQLHGLTIAS
ERPQHAMRETWHPYGLCGVISAFNFPVAVWAWNAALALVCGNGVIWKPSEKTPLTALAMQ
SLLDGVLEIAAPQHVGIATVLSGGPALGQHLVEHAAVRLVSATGSTRMGRAVGIACAERF
KRAILELGGNNAAIIAPSADLELAVRAMTFSAAGTAGQRCTSLRRAFVHVDVLEAVTTRL
IQVFGRLPVGDPLAETTLVGPLIDGAAGAAMAAALLRCREHGNTVHGGERVLAEKYPNAE
YVRPALVLTDRQHETMLSETFAPILYVMPYTTLDEAIALNNASEHGLSSCIFTESLREAE
RFMSASGSDCGIANVNIGTSGAEIGGAFGGEKATGGGRESGSDAWKGYMRRATNTVNYGD
ALPLAQGVRFEV
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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