SitesBLAST
Comparing WP_086509055.1 NCBI__GCF_002151265.1:WP_086509055.1 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)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
45% identity, 89% coverage: 42:500/516 of query aligns to 20:478/489 of 4o6rA
- active site: N150 (= N171), K173 (= K194), E248 (= E269), C282 (= C303), E383 (= E405), E460 (≠ S482)
- binding adenosine monophosphate: I146 (= I167), V147 (≠ T168), K173 (= K194), G206 (= G227), G210 (= G231), Q211 (≠ A232), F224 (= F245), G226 (= G247), S227 (= S248), T230 (≠ S251), R233 (≠ L254)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
43% identity, 92% coverage: 30:504/516 of query aligns to 6:480/487 of 4go4A
- active site: N149 (= N171), K172 (= K194), E247 (= E269), C281 (= C303), E381 (= E405), E458 (≠ S482)
- binding nicotinamide-adenine-dinucleotide: I145 (= I167), V146 (≠ T168), W148 (= W170), N149 (= N171), F154 (≠ T176), K172 (= K194), G205 (= G227), G209 (= G231), Q210 (≠ A232), F223 (= F245), T224 (≠ V246), G225 (= G247), S226 (= S248), T229 (≠ S251), E247 (= E269), G249 (= G271), C281 (= C303), E381 (= E405), F383 (= F407)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
41% identity, 91% coverage: 39:506/516 of query aligns to 51:518/518 of O94788
- A110 (≠ V95) to V: in dbSNP:rs35365164
- Q182 (= Q166) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 168:170) binding
- KPAE 210:213 (≠ KPSE 194:197) binding
- STE 264:266 (≠ SPQ 248:250) binding
- C320 (= C303) active site, Nucleophile
- R347 (≠ I330) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ E331) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RQYAH 349:353) binding
- A383 (= A366) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E405) binding
- E436 (≠ R424) to K: in dbSNP:rs34744827
- S461 (≠ A449) to Y: in DIH4; decreased retinoic acid biosynthetic process
Sites not aligning to the query:
- 50 E → G: in dbSNP:rs34266719
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
41% identity, 91% coverage: 39:506/516 of query aligns to 25:492/492 of 6b5hA
- active site: N161 (= N171), E260 (= E269), C294 (= C303), E468 (≠ S482)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G122), G116 (≠ K126), F162 (≠ A172), W169 (= W179), Q284 (≠ A293), F288 (≠ A297), T295 (≠ V304), N449 (≠ K463), L451 (≠ I465), N452 (≠ S466), F457 (= F471)
- binding nicotinamide-adenine-dinucleotide: I157 (= I167), I158 (≠ T168), W160 (= W170), N161 (= N171), K184 (= K194), G217 (= G227), G221 (= G231), F235 (= F245), T236 (≠ V246), G237 (= G247), S238 (= S248), V241 (≠ S251), E260 (= E269), L261 (= L270), C294 (= C303), F393 (= F407)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
41% identity, 91% coverage: 39:506/516 of query aligns to 25:492/492 of 6b5gA
- active site: N161 (= N171), E260 (= E269), C294 (= C303), E468 (≠ S482)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ A172), L165 (≠ F175), W169 (= W179), F288 (≠ A297), C293 (≠ S302), C294 (= C303), T295 (≠ V304), N449 (≠ K463), L451 (≠ I465)
- binding nicotinamide-adenine-dinucleotide: I157 (= I167), I158 (≠ T168), P159 (= P169), W160 (= W170), N161 (= N171), M166 (≠ T176), K184 (= K194), E187 (= E197), G217 (= G227), G221 (= G231), F235 (= F245), T236 (≠ V246), G237 (= G247), S238 (= S248), V241 (≠ S251), E260 (= E269), L261 (= L270), C294 (= C303), E391 (= E405), F393 (= F407)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
41% identity, 91% coverage: 39:506/516 of query aligns to 25:492/492 of 6aljA
- active site: N161 (= N171), E260 (= E269), C294 (= C303), E468 (≠ S482)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ K126), F162 (≠ A172), L165 (≠ F175), M166 (≠ T176), W169 (= W179), E260 (= E269), C293 (≠ S302), C294 (= C303), L451 (≠ I465), N452 (≠ S466), A453 (≠ V467)
- binding nicotinamide-adenine-dinucleotide: I157 (= I167), I158 (≠ T168), P159 (= P169), W160 (= W170), N161 (= N171), K184 (= K194), E187 (= E197), G217 (= G227), G221 (= G231), F235 (= F245), G237 (= G247), S238 (= S248), V241 (≠ S251), Q341 (= Q350), K344 (≠ H353), E391 (= E405), F393 (= F407)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 89% coverage: 40:499/516 of query aligns to 31:488/491 of 5gtlA
- active site: N165 (= N171), K188 (= K194), E263 (= E269), C297 (= C303), E394 (= E405), E471 (≠ S482)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I167), P163 (= P169), K188 (= K194), A190 (≠ S196), E191 (= E197), Q192 (≠ L198), G221 (= G227), G225 (= G231), G241 (= G247), S242 (= S248), T245 (≠ S251), L264 (= L270), C297 (= C303), E394 (= E405), F396 (= F407)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
40% identity, 89% coverage: 40:499/516 of query aligns to 31:488/491 of 5gtkA
- active site: N165 (= N171), K188 (= K194), E263 (= E269), C297 (= C303), E394 (= E405), E471 (≠ S482)
- binding nicotinamide-adenine-dinucleotide: I161 (= I167), I162 (≠ T168), P163 (= P169), W164 (= W170), K188 (= K194), E191 (= E197), G221 (= G227), G225 (= G231), A226 (= A232), F239 (= F245), G241 (= G247), S242 (= S248), T245 (≠ S251), Y248 (≠ L254), L264 (= L270), C297 (= C303), Q344 (= Q350), R347 (≠ H353), E394 (= E405), F396 (= F407)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
41% identity, 91% coverage: 39:506/516 of query aligns to 51:518/518 of Q63639
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
41% identity, 93% coverage: 28:506/516 of query aligns to 46:520/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
7radA Crystal structure analysis of aldh1b1
39% identity, 93% coverage: 28:506/516 of query aligns to 19:493/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I167), I159 (≠ T168), P160 (= P169), W161 (= W170), N162 (= N171), M167 (≠ T176), K185 (= K194), E188 (= E197), G218 (= G227), G222 (= G231), A223 (= A232), T237 (≠ V246), G238 (= G247), S239 (= S248), V242 (≠ S251), E261 (= E269), L262 (= L270), C295 (= C303), E392 (= E405), F394 (= F407)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ K126), F163 (≠ A172), E285 (≠ A293), F289 (≠ A297), N450 (≠ K463), V452 (≠ I465)
7mjdA Crystal structure analysis of aldh1b1
39% identity, 93% coverage: 28:506/516 of query aligns to 19:493/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I167), I159 (≠ T168), P160 (= P169), W161 (= W170), N162 (= N171), M167 (≠ T176), K185 (= K194), E188 (= E197), G218 (= G227), G222 (= G231), F236 (= F245), T237 (≠ V246), G238 (= G247), S239 (= S248), V242 (≠ S251), E261 (= E269), L262 (= L270), C295 (= C303), E392 (= E405), F394 (= F407)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ K126), E285 (≠ A293), F289 (≠ A297), N450 (≠ K463), V452 (≠ I465)
7mjcA Crystal structure analysis of aldh1b1
39% identity, 93% coverage: 28:506/516 of query aligns to 19:493/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I167), I159 (≠ T168), P160 (= P169), W161 (= W170), N162 (= N171), K185 (= K194), E188 (= E197), G218 (= G227), G222 (= G231), T237 (≠ V246), G238 (= G247), S239 (= S248), V242 (≠ S251), E261 (= E269), L262 (= L270), C295 (= C303), E392 (= E405), F394 (= F407)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 31:496/496 of 4fr8C
- active site: N165 (= N171), K188 (= K194), Q264 (≠ E269), C298 (= C303), E395 (= E405), E472 (≠ S482)
- binding nicotinamide-adenine-dinucleotide: I161 (= I167), I162 (≠ T168), W164 (= W170), K188 (= K194), G221 (= G227), G225 (= G231), A226 (= A232), F239 (= F245), G241 (= G247), S242 (= S248), I245 (≠ S251), Q345 (= Q350), E395 (= E405), F397 (= F407)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 29:494/494 of 5l13A
- active site: N163 (= N171), K186 (= K194), E262 (= E269), C296 (= C303), E393 (= E405), E470 (≠ S482)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ A172), M168 (≠ T176), W171 (= W179), F290 (≠ A297), C295 (≠ S302), C296 (= C303), C297 (≠ V304), D451 (≠ K463), F453 (≠ I465)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 29:494/494 of 4kwgA
- active site: N163 (= N171), K186 (= K194), E262 (= E269), C296 (= C303), E393 (= E405), E470 (≠ S482)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (≠ A172), M168 (≠ T176), C295 (≠ S302), C296 (= C303), C297 (≠ V304), D451 (≠ K463), F453 (≠ I465)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 29:494/494 of 4kwfA
- active site: N163 (= N171), K186 (= K194), E262 (= E269), C296 (= C303), E393 (= E405), E470 (≠ S482)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (≠ A172), M168 (≠ T176), W171 (= W179), E262 (= E269), C295 (≠ S302), C296 (= C303), C297 (≠ V304), D451 (≠ K463), F453 (≠ I465), F459 (= F471)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 29:494/494 of 3sz9A
- active site: N163 (= N171), K186 (= K194), E262 (= E269), C296 (= C303), E393 (= E405), E470 (≠ S482)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (≠ A172), C295 (≠ S302), C296 (= C303), D451 (≠ K463), F453 (≠ I465), F459 (= F471)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 29:494/494 of 3injA
- active site: N163 (= N171), K186 (= K194), E262 (= E269), C296 (= C303), E393 (= E405), E470 (≠ S482)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ K126), F164 (≠ A172), L167 (≠ F175), F286 (≠ A293), F290 (≠ A297), D451 (≠ K463), F453 (≠ I465)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
41% identity, 90% coverage: 41:506/516 of query aligns to 29:494/494 of 2vleA
- active site: N163 (= N171), K186 (= K194), E262 (= E269), C296 (= C303), E393 (= E405), E470 (≠ S482)
- binding daidzin: M118 (≠ K126), F164 (≠ A172), M168 (≠ T176), W171 (= W179), F286 (≠ A293), F290 (≠ A297), C295 (≠ S302), C296 (= C303), D451 (≠ K463), V452 (≠ A464), F453 (≠ I465)
Query Sequence
>WP_086509055.1 NCBI__GCF_002151265.1:WP_086509055.1
MNRLNRQARERLSTLLDGFELQGATPLSNWIDGTACPGAGETITLIDPATGEALLDYRDA
GPALVERAVSSASRAQQAWMALTASERGRRMNAAVRGLEGHEEALAQLESVVAGKPIRDC
RGEVGKVREMFDYYAGWCDKQHGEVIPVPTSHLNYVRHVPYGVVGQITPWNAPMFTCAWQ
LAPAIAAGNGAVLKPSELTPFTSVVIARLLERGGLPKGLVNIVNGLGPSTGAALTGSEGI
SKLVFVGSPQSGRLIAEAGARRLVPSVLELGGKSANIVFADASLDAAVAGAQAAIFAAAG
QSCVAGSRLLVQREVFAEVTERLARAAAGIEVGLPGDEATRMGPLQNARQYAHVTRMIED
AVAAGARVIVGGSRPAGLPEEARGYFLAPTVLVDVTPEMEIAREEVFGPVLVAMPFDDEA
DAVRLANATRFGLAGAVWTQDPARAHRVAAQLRAGTVWINGYKAISVMSPFGGFGDSGFG
RSSGLDGLREYTLPQSVWVETASEASVAMGYGSGVG
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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