SitesBLAST
Comparing PP_5258 FitnessBrowser__Putida:PP_5258 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
68% identity, 95% coverage: 25:496/496 of query aligns to 27:503/504 of 6dbbA
- active site: N152 (= N150), E259 (= E252), C293 (= C286), E471 (= E464)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), S149 (= S147), A150 (= A148), F151 (= F149), N152 (= N150), K175 (= K173), S177 (= S175), R218 (= R211), T236 (= T229), G237 (= G230), S238 (= S231), M241 (= M234), E259 (= E252), L260 (= L253), G261 (= G254), C293 (= C286), E391 (= E384), F393 (= F386)
- binding beta-6-hydroxy-1,4,5,6-tetrhydronicotinamide adenine dinucleotide: I148 (= I146), S149 (= S147), A150 (= A148), F151 (= F149), N152 (= N150), K175 (= K173), S177 (= S175), R218 (= R211), T236 (= T229), G237 (= G230), S238 (= S231), M241 (= M234), E259 (= E252), L260 (= L253), G261 (= G254), C293 (= C286), E391 (= E384), F393 (= F386)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
65% identity, 99% coverage: 6:495/496 of query aligns to 17:507/508 of 6rttA
- active site: N161 (= N150), E262 (= E252), C296 (= C286), E476 (= E464)
- binding pyridine-2-carboxylic acid: A159 (= A148), F162 (= F151), V166 (= V155), W169 (= W158), G240 (= G230), S241 (= S231), R295 (= R285), C296 (= C286), T297 (= T287), E396 (= E384), F398 (= F386), P421 (= P409), K469 (= K457), E470 (= E458)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
65% identity, 99% coverage: 6:495/496 of query aligns to 18:508/509 of 6rtsA
- active site: N162 (= N150), E263 (= E252), C297 (= C286), E477 (= E464)
- binding nicotinamide-adenine-dinucleotide: I158 (= I146), S159 (= S147), A160 (= A148), F161 (= F149), N162 (= N150), K185 (= K173), S187 (= S175), E188 (= E176), A222 (≠ R211), G225 (= G214), T240 (= T229), G241 (= G230), S242 (= S231), M245 (= M234), E263 (= E252), L264 (= L253), C297 (= C286), E397 (= E384), F399 (= F386)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
65% identity, 99% coverage: 6:495/496 of query aligns to 17:504/505 of 6rtuA
- active site: N161 (= N150), E259 (= E252), C293 (= C286), E473 (= E464)
- binding 2-aminohexanedioic acid: E115 (= E104), F162 (= F151), R292 (= R285), C293 (= C286), T294 (= T287), S454 (= S445), G455 (= G446), A456 (= A447), F462 (= F453)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
53% identity, 95% coverage: 24:495/496 of query aligns to 39:508/509 of 4zulA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E384), E477 (= E464)
- binding 2-aminohexanedioic acid: E119 (= E104), F166 (= F151), R299 (= R285), C300 (= C286), T301 (= T287), G459 (= G446), A460 (= A447), F466 (= F453)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
53% identity, 95% coverage: 24:495/496 of query aligns to 39:508/509 of 4x0tA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E384), E477 (= E464)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), V170 (= V155), W173 (= W158), C300 (= C286), F466 (= F453)
- binding nicotinamide-adenine-dinucleotide: T162 (≠ S147), A163 (= A148), F164 (= F149), N165 (= N150), K188 (= K173), G189 (≠ P174), A190 (≠ S175), A225 (≠ R211), G228 (= G214), T229 (≠ E215), F242 (≠ A228), T243 (= T229), G244 (= G230), S245 (= S231), V248 (≠ M234), E266 (= E252), L267 (= L253), C300 (= C286), E397 (= E384), F399 (= F386)
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)
53% identity, 95% coverage: 24:495/496 of query aligns to 69:538/539 of P49419
- TAF 192:194 (≠ SAF 147:149) binding
- A199 (= A154) to V: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912709
- K218 (= K173) binding
- GT 258:259 (≠ GE 214:215) binding
- GS 274:275 (= GS 230:231) binding
- EL 296:297 (= EL 252:253) binding
- C330 (= C286) active site, Nucleophile
- E427 (= E384) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ D396) to Q: in dbSNP:rs12514417
Sites not aligning to the query:
- 110:539 natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
53% identity, 95% coverage: 24:495/496 of query aligns to 40:509/510 of 6o4dB
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
51% identity, 95% coverage: 24:495/496 of query aligns to 40:509/509 of 2jg7A
- active site: N166 (= N150), K189 (= K173), E267 (= E252), C301 (= C286), E398 (= E384), E478 (= E464)
- binding nicotinamide-adenine-dinucleotide: I162 (= I146), T163 (≠ S147), A164 (= A148), F165 (= F149), N166 (= N150), K189 (= K173), P192 (≠ E176), A226 (≠ R211), G229 (= G214), T230 (≠ E215), F243 (≠ A228), T244 (= T229), G245 (= G230), S246 (= S231), V249 (≠ M234), E267 (= E252), L268 (= L253), C301 (= C286), E398 (= E384), F400 (= F386)
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
52% identity, 93% coverage: 24:484/496 of query aligns to 39:497/497 of 2j6lA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E384), E477 (= E464)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I161 (= I146), T162 (≠ S147), A163 (= A148), F164 (= F149), N165 (= N150), K188 (= K173), A225 (≠ R211), G228 (= G214), T229 (≠ E215), F242 (≠ A228), T243 (= T229), G244 (= G230), S245 (= S231), V248 (≠ M234), E266 (= E252), L267 (= L253), C300 (= C286), E397 (= E384), F399 (= F386)
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
52% identity, 88% coverage: 53:490/496 of query aligns to 64:498/498 of 4pxnA
- active site: N161 (= N150), K184 (= K173), E262 (= E252), C296 (= C286), E392 (= E384), E472 (= E464)
- binding nicotinamide-adenine-dinucleotide: I157 (= I146), T158 (≠ S147), A159 (= A148), F160 (= F149), N161 (= N150), K184 (= K173), T221 (≠ R211), G224 (= G214), Q225 (≠ E215), F238 (≠ A228), T239 (= T229), G240 (= G230), S241 (= S231), A244 (≠ M234), V248 (= V238), E262 (= E252), L263 (= L253), S264 (≠ G254), C296 (= C286), E392 (= E384), F394 (= F386), F461 (= F453)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
50% identity, 93% coverage: 24:484/496 of query aligns to 39:487/487 of 4x0uD
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E384), E467 (= E464)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), A169 (= A154), V170 (= V155), C300 (= C286), F456 (= F453), H461 (≠ E458)
- binding magnesium ion: E119 (= E104), D122 (= D107)
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)
34% identity, 89% coverage: 49:491/496 of query aligns to 58:510/511 of 6fkuA
- active site: N159 (= N150), E261 (= E252), C295 (= C286), E483 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I146), T156 (≠ S147), N159 (= N150), K182 (= K173), S184 (= S175), E185 (= E176), G214 (= G210), G215 (≠ R211), K216 (≠ E212), G220 (= G214), Q221 (≠ E215), F237 (≠ A228), T238 (= T229), G239 (= G230), S240 (= S231), V243 (≠ M234), E261 (= E252), L262 (= L253), C295 (= C286), R342 (≠ Q331), F343 (≠ S332), E404 (= E384), F406 (= F386)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
31% identity, 96% coverage: 17:493/496 of query aligns to 20:489/490 of 5ekcE
- active site: N154 (= N150), K177 (= K173), E252 (= E252), C286 (= C286), E381 (= E384), E459 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I146), T151 (≠ S147), P152 (≠ A148), W153 (≠ F149), K177 (= K173), S180 (≠ E176), G210 (= G210), G214 (= G214), F228 (≠ A228), G230 (= G230), E231 (≠ S231), T234 (≠ M234), N331 (≠ D329), R333 (≠ Q331), Q334 (≠ S332)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
31% identity, 96% coverage: 17:493/496 of query aligns to 13:482/482 of 5ek6A
- active site: N147 (= N150), K170 (= K173), E245 (= E252), C279 (= C286), E374 (= E384), E452 (= E464)
- binding 2-methylpropanal: I152 (≠ V155), K155 (≠ W158), T222 (= T229), E245 (= E252), F441 (= F453)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I146), T144 (≠ S147), W146 (≠ F149), N147 (= N150), I152 (≠ V155), K170 (= K173), A172 (≠ S175), S173 (≠ E176), P202 (vs. gap), G203 (= G210), G207 (= G214), F221 (≠ A228), T222 (= T229), G223 (= G230), E224 (≠ S231), T227 (≠ M234), I231 (≠ V238), E245 (= E252), L246 (= L253), C279 (= C286), E374 (= E384)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
31% identity, 96% coverage: 17:493/496 of query aligns to 13:482/482 of 4h73A
- active site: N147 (= N150), K170 (= K173), E245 (= E252), C279 (= C286), E374 (= E384), E452 (= E464)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I146), T144 (≠ S147), P145 (≠ A148), W146 (≠ F149), K170 (= K173), A172 (≠ S175), S173 (≠ E176), G203 (= G210), G207 (= G214), F221 (≠ A228), G223 (= G230), E224 (≠ S231), T227 (≠ M234)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
31% identity, 91% coverage: 23:474/496 of query aligns to 29:472/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E252), C288 (= C286), E385 (= E384), E462 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A148), W155 (≠ F149), K179 (= K173), A181 (≠ S175), S182 (≠ E176), A212 (≠ R211), G216 (= G214), G232 (= G230), S233 (= S231), I236 (≠ M234), C288 (= C286), K338 (≠ A335), E385 (= E384), F387 (= F386)
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)
31% identity, 91% coverage: 23:474/496 of query aligns to 30:473/482 of P25526
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
33% identity, 96% coverage: 14:488/496 of query aligns to 14:484/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E252), C282 (= C286), E383 (= E384), E460 (= E464)
- binding adenosine monophosphate: I146 (= I146), V147 (≠ S147), K173 (= K173), G206 (= G210), G210 (= G214), Q211 (≠ E215), F224 (≠ A228), G226 (= G230), S227 (= S231), T230 (≠ M234), R233 (≠ E237)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 93% coverage: 22:483/496 of query aligns to 20:477/477 of 6j76A
- active site: N148 (= N150), E246 (= E252), C280 (= C286), E458 (= E464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I146), T145 (≠ S147), A146 (= A148), W147 (≠ F149), N148 (= N150), K171 (= K173), T173 (≠ S175), S174 (≠ E176), G204 (= G210), G208 (= G214), T223 (= T229), G224 (= G230), S225 (= S231), A228 (≠ M234), S231 (≠ E237), I232 (≠ V238), E246 (= E252), L247 (= L253), C280 (= C286), E381 (= E384), F383 (= F386), H447 (≠ F453)
Query Sequence
>PP_5258 FitnessBrowser__Putida:PP_5258
MVAGLLERLGVAAEAYTQGDYPVHTPIDGSQIASVKLLGKAETIARIDQAQSAFEAWRSV
PAPRRGELVRLFGEVLREHKADLGELVSIEAGKITQEGLGEVQEMIDICDFAVGLSRQLY
GLTIASERPGHHMRETWHPLGVVGVISAFNFPVAVWAWNTALALVAGNSVVWKPSEKTPL
TALACQALFEKALKAFGDAPAGLAQLVIGGREAGEAMVDDPRVPLVSATGSTRMGREVGP
RVAARFGRSILELGGNNAMILAPSADLDLAVRGILFSAVGTAGQRCTTLRRLIVHRSIKD
EVVARVKAAYGKVRIGDPRKDNLVGPLIDKQSFDAMQGALAKARDEGGQVFGGERQLADQ
YPNAYYVSPAIAEMPAQSDVVRHETFAPILYVLAYDDFEEALRLNNEVPQGLSSCIFTTD
IREAERFQSASGSDCGIANVNIGTSGAEIGGAFGGEKETGGGRESGSDAWKGYMRRQTNT
VNYSRELPLAQGIVFD
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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