SitesBLAST
Comparing AZOBR_RS32620 FitnessBrowser__azobra:AZOBR_RS32620 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)
6dbbA Crystal structure of a putative aldehyde dehydrogenase family protein burkholderia cenocepacia j2315 in complex with partially reduced nadh
67% identity, 100% coverage: 1:498/500 of query aligns to 2:504/504 of 6dbbA
- active site: N152 (= N150), E259 (= E252), C293 (= C286), E471 (= E465)
- 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 (= E385), F393 (= F387)
- 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 (= E385), F393 (= F387)
6rtsA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with NAD+ (see paper)
64% identity, 98% coverage: 7:496/500 of query aligns to 18:508/509 of 6rtsA
- active site: N162 (= N150), E263 (= E252), C297 (= C286), E477 (= E465)
- 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 (= E385), F399 (= F387)
6rttA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with picolinic acid (see paper)
64% identity, 98% coverage: 7:496/500 of query aligns to 17:507/508 of 6rttA
- active site: N161 (= N150), E262 (= E252), C296 (= C286), E476 (= E465)
- binding pyridine-2-carboxylic acid: A159 (= A148), F162 (= F151), V166 (= V155), W169 (= W158), G240 (= G230), S241 (= S231), R295 (= R285), C296 (= C286), T297 (= T287), E396 (= E385), F398 (= F387), P421 (= P410), K469 (= K458), E470 (= E459)
6rtuA Piperideine-6-carboxylate dehydrogenase from streptomyces clavuligerus complexed with alpha-aminoadipic acid (see paper)
63% identity, 98% coverage: 7:496/500 of query aligns to 17:504/505 of 6rtuA
- active site: N161 (= N150), E259 (= E252), C293 (= C286), E473 (= E465)
- binding 2-aminohexanedioic acid: E115 (= E104), F162 (= F151), R292 (= R285), C293 (= C286), T294 (= T287), S454 (= S446), G455 (= G447), A456 (= A448), F462 (= F454)
2jg7A Crystal structure of seabream antiquitin and elucidation of its substrate specificity (see paper)
52% identity, 93% coverage: 34:496/500 of query aligns to 48:509/509 of 2jg7A
- active site: N166 (= N150), K189 (= K173), E267 (= E252), C301 (= C286), E398 (= E385), E478 (= E465)
- 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 (= E385), F400 (= F387)
4zulA Structure aldh7a1 complexed with alpha-aminoadipate (see paper)
52% identity, 91% coverage: 41:497/500 of query aligns to 56:509/509 of 4zulA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E477 (= E465)
- binding 2-aminohexanedioic acid: E119 (= E104), F166 (= F151), R299 (= R285), C300 (= C286), T301 (= T287), G459 (= G447), A460 (= A448), F466 (= F454)
4x0tA Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde and complexed with NAD+ (see paper)
52% identity, 91% coverage: 41:497/500 of query aligns to 56:509/509 of 4x0tA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E477 (= E465)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), V170 (= V155), W173 (= W158), C300 (= C286), F466 (= F454)
- 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 (= E385), F399 (= F387)
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)
52% identity, 91% coverage: 41:497/500 of query aligns to 86:539/539 of P49419
- 110:539 (vs. 65:497, 53% identical) natural variant: Missing (in PDE; loss of alpha-AASA dehydrogenase activity)
- 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 (= E385) binding ; to Q: in PDE; loss of alpha-AASA dehydrogenase activity; dbSNP:rs121912707
- K439 (≠ E397) to Q: in dbSNP:rs12514417
6o4dB Structure of aldh7a1 mutant w175a complexed with l-pipecolic acid (see paper)
51% identity, 91% coverage: 41:497/500 of query aligns to 57:510/510 of 6o4dB
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
51% identity, 88% coverage: 53:491/500 of query aligns to 64:498/498 of 4pxnA
- active site: N161 (= N150), K184 (= K173), E262 (= E252), C296 (= C286), E392 (= E385), E472 (= E465)
- 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 (= E385), F394 (= F387), F461 (= F454)
2j6lA Structure of aminoadipate-semialdehyde dehydrogenase (see paper)
51% identity, 89% coverage: 41:485/500 of query aligns to 56:497/497 of 2j6lA
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E477 (= E465)
- 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 (= E385), F399 (= F387)
4x0uD Structure aldh7a1 inactivated by 4-diethylaminobenzaldehyde (see paper)
49% identity, 89% coverage: 41:485/500 of query aligns to 56:487/487 of 4x0uD
- active site: N165 (= N150), K188 (= K173), E266 (= E252), C300 (= C286), E397 (= E385), E467 (= E465)
- binding 4-(diethylamino)benzaldehyde: F166 (= F151), A169 (= A154), V170 (= V155), C300 (= C286), F456 (= F454), H461 (≠ E459)
- 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)
33% identity, 95% coverage: 17:492/500 of query aligns to 25:510/511 of 6fkuA
- active site: N159 (= N150), E261 (= E252), C295 (= C286), E483 (= E465)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I155 (= I146), T156 (≠ S147), N159 (= N150), K182 (= K173), S184 (= S175), E185 (= E176), G214 (= G209), G215 (= G210), K216 (≠ R211), G220 (= G214), Q221 (≠ E215), F237 (≠ A228), T238 (= T229), G239 (= G230), S240 (= S231), V243 (≠ M234), E261 (= E252), L262 (= L253), C295 (= C286), R342 (≠ G332), F343 (≠ A333), E404 (= E385), F406 (= F387)
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, 92% coverage: 17:475/500 of query aligns to 24:473/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
31% identity, 92% coverage: 17:475/500 of query aligns to 23:472/481 of 3jz4A
- active site: N156 (= N150), K179 (= K173), E254 (= E252), C288 (= C286), E385 (= E385), E462 (= E465)
- 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 (≠ G336), E385 (= E385), F387 (= F387)
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
31% identity, 94% coverage: 16:484/500 of query aligns to 14:477/477 of 6j76A
- active site: N148 (= N150), E246 (= E252), C280 (= C286), E458 (= E465)
- 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 (= E385), F383 (= F387), H447 (≠ F454)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
32% identity, 95% coverage: 17:489/500 of query aligns to 17:484/489 of 4o6rA
- active site: N150 (= N150), K173 (= K173), E248 (= E252), C282 (= C286), E383 (= E385), E460 (= E465)
- 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)
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)
30% identity, 92% coverage: 23:484/500 of query aligns to 26:481/487 of P42412
- C36 (≠ G33) 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 (≠ E104) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- A150 (≠ S147) binding
- F152 (= F149) binding
- C160 (≠ A157) 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 (= K173) binding
- E179 (= E176) binding
- R180 (≠ K177) binding
- S229 (= S231) binding
- T251 (≠ L253) binding
- R283 (= R285) mutation to L: At least 50-fold decrease of the second-order rate constant for the acylation step.
- C287 (≠ L289) 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 (≠ G353) 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 (= E385) binding
- C413 (= C416) 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
30% identity, 92% coverage: 23:484/500 of query aligns to 24:479/484 of 1t90A
- active site: N151 (= N150), K174 (= K173), L248 (≠ E252), C282 (= C286), E380 (= E385), A460 (≠ E465)
- binding nicotinamide-adenine-dinucleotide: I147 (= I146), A148 (≠ S147), P149 (≠ A148), F150 (= F149), N151 (= N150), W159 (= W158), K174 (= K173), E177 (= E176), R178 (≠ K177), H207 (≠ R211), V225 (≠ T229), G226 (= G230), S227 (= S231), V230 (≠ M234), L248 (≠ E252), T249 (≠ L253), C282 (= C286), E380 (= E385), F382 (= F387)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
31% identity, 95% coverage: 18:490/500 of query aligns to 20:487/489 of 6wsbA
- active site: N152 (= N150), E250 (= E252), C284 (= C286), E462 (= E465)
- binding nicotinamide-adenine-dinucleotide: I148 (= I146), G149 (≠ S147), A150 (= A148), W151 (≠ F149), N152 (= N150), K175 (= K173), E178 (= E176), G208 (≠ R211), G211 (= G214), A212 (≠ E215), F225 (≠ A228), T226 (= T229), G227 (= G230), G228 (≠ S231), T231 (≠ M234), V235 (= V238), E250 (= E252), L251 (= L253), G252 (= G254), C284 (= C286), E385 (= E385), F387 (= F387)
Query Sequence
>AZOBR_RS32620 FitnessBrowser__azobra:AZOBR_RS32620
MQHRDLLSRLGLELPADGAGLSVRSPIDGAALGVAPVTPASEIPEVAARAQRAFEAWRSV
PAPRRGELVRLLGEELRDAKEDLGRLVTLEMGKIFQEGLGEVQEMIDICDFAVGLSRQLY
GLTIASERPGHAMRETWHPMGPCAVISAFNFPVAVWAWNAALALVCGDPVIWKPSEKTPL
TALACQRIFERAVARFGDAPADLLQVVNGGRDVGEALVASPLVPIVSATGSTRMGREVAL
KVAERFARPILELGGNNAMIVAPSADLDMAVRAIVFSAVGTCGQRCTTLRRLIVHKDVRD
TLLPRLKAAYASVPIGNPLESGVLVGPLNDKGAFDGMQRALEQAKADGGTVTGGGRALAD
QYPDAWYVQPAIVEMPGQTDIVRHETFAPILYVLTYETLEEAIALQNAVPQGLSSCIFTT
DIREAESFLSAAGSDCGIANVNIGPSGAEIGGAFGGEKETGGGRESGSDAWKGYMRRQTA
TVNYSRALPLAQGIKFEIAG
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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