SitesBLAST
Comparing WP_079650369.1 NCBI__GCF_900167915.1:WP_079650369.1 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
44% identity, 92% coverage: 35:489/494 of query aligns to 35:486/491 of 5gtlA
- active site: N165 (= N168), K188 (= K191), E263 (= E266), C297 (= C300), E394 (= E397), E471 (= E474)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I164), P163 (= P166), K188 (= K191), A190 (≠ S193), E191 (= E194), Q192 (≠ L195), G221 (= G224), G225 (= G228), G241 (= G244), S242 (= S245), T245 (≠ V248), L264 (= L267), C297 (= C300), E394 (= E397), F396 (= F399)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
44% identity, 92% coverage: 35:489/494 of query aligns to 35:486/491 of 5gtkA
- active site: N165 (= N168), K188 (= K191), E263 (= E266), C297 (= C300), E394 (= E397), E471 (= E474)
- binding nicotinamide-adenine-dinucleotide: I161 (= I164), I162 (≠ T165), P163 (= P166), W164 (= W167), K188 (= K191), E191 (= E194), G221 (= G224), G225 (= G228), A226 (= A229), F239 (= F242), G241 (= G244), S242 (= S245), T245 (≠ V248), Y248 (≠ R251), L264 (= L267), C297 (= C300), Q344 (≠ H347), R347 (≠ G350), E394 (= E397), F396 (= F399)
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)
43% identity, 99% coverage: 4:492/494 of query aligns to 14:512/518 of O94788
- E50 (= E27) to G: in dbSNP:rs34266719
- A110 (= A88) to V: in dbSNP:rs35365164
- Q182 (≠ L163) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TPW 165:167) binding NAD(+)
- KPAE 210:213 (≠ KPSE 191:194) binding NAD(+)
- STE 264:266 (≠ STA 245:247) binding NAD(+)
- C320 (= C300) active site, Nucleophile
- R347 (≠ M327) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R328) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ RHRAG 346:350) binding NAD(+)
- A383 (= A363) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E397) binding NAD(+)
- E436 (≠ R416) to K: in dbSNP:rs34744827
- S461 (≠ A441) to Y: in DIH4; decreased retinoic acid biosynthetic process
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
44% identity, 96% coverage: 21:492/494 of query aligns to 15:486/492 of 6b5hA
- active site: N161 (= N168), E260 (= E266), C294 (= C300), E468 (= E474)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ G116), G116 (≠ A120), F162 (≠ G169), W169 (= W176), Q284 (≠ D290), F288 (≠ G294), T295 (≠ V301), N449 (≠ G455), L451 (≠ P457), N452 (≠ E458), F457 (≠ I463)
- binding nicotinamide-adenine-dinucleotide: I157 (= I164), I158 (≠ T165), W160 (= W167), N161 (= N168), K184 (= K191), G217 (= G224), G221 (= G228), F235 (= F242), T236 (= T243), G237 (= G244), S238 (= S245), V241 (= V248), E260 (= E266), L261 (= L267), C294 (= C300), F393 (= F399)
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)
44% identity, 96% coverage: 21:492/494 of query aligns to 15:486/492 of 6b5gA
- active site: N161 (= N168), E260 (= E266), C294 (= C300), E468 (= E474)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ G169), L165 (≠ V172), W169 (= W176), F288 (≠ G294), C293 (≠ V299), C294 (= C300), T295 (≠ V301), N449 (≠ G455), L451 (≠ P457)
- binding nicotinamide-adenine-dinucleotide: I157 (= I164), I158 (≠ T165), P159 (= P166), W160 (= W167), N161 (= N168), M166 (≠ I173), K184 (= K191), E187 (= E194), G217 (= G224), G221 (= G228), F235 (= F242), T236 (= T243), G237 (= G244), S238 (= S245), V241 (= V248), E260 (= E266), L261 (= L267), C294 (= C300), E391 (= E397), F393 (= F399)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
44% identity, 96% coverage: 21:492/494 of query aligns to 15:486/492 of 6aljA
- active site: N161 (= N168), E260 (= E266), C294 (= C300), E468 (= E474)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A120), F162 (≠ G169), L165 (≠ V172), M166 (≠ I173), W169 (= W176), E260 (= E266), C293 (≠ V299), C294 (= C300), L451 (≠ P457), N452 (≠ E458), A453 (≠ L459)
- binding nicotinamide-adenine-dinucleotide: I157 (= I164), I158 (≠ T165), P159 (= P166), W160 (= W167), N161 (= N168), K184 (= K191), E187 (= E194), G217 (= G224), G221 (= G228), F235 (= F242), G237 (= G244), S238 (= S245), V241 (= V248), Q341 (≠ H347), K344 (≠ G350), E391 (= E397), F393 (= F399)
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)
43% identity, 99% coverage: 4:492/494 of query aligns to 14:512/518 of Q63639
7radA Crystal structure analysis of aldh1b1
43% identity, 96% coverage: 19:492/494 of query aligns to 11:487/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ T165), P160 (= P166), W161 (= W167), N162 (= N168), M167 (≠ I173), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), A223 (= A229), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), E261 (= E266), L262 (= L267), C295 (= C300), E392 (= E397), F394 (= F399)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ G116), E117 (≠ A120), F163 (≠ G169), E285 (≠ D290), F289 (≠ G294), N450 (≠ G455), V452 (≠ P457)
7mjdA Crystal structure analysis of aldh1b1
43% identity, 96% coverage: 19:492/494 of query aligns to 11:487/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ T165), P160 (= P166), W161 (= W167), N162 (= N168), M167 (≠ I173), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), F236 (= F242), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), E261 (= E266), L262 (= L267), C295 (= C300), E392 (= E397), F394 (= F399)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ A120), E285 (≠ D290), F289 (≠ G294), N450 (≠ G455), V452 (≠ P457)
7mjcA Crystal structure analysis of aldh1b1
43% identity, 96% coverage: 19:492/494 of query aligns to 11:487/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I164), I159 (≠ T165), P160 (= P166), W161 (= W167), N162 (= N168), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), E261 (= E266), L262 (= L267), C295 (= C300), E392 (= E397), F394 (= F399)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
44% identity, 96% coverage: 21:492/494 of query aligns to 43:514/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
P00352 Aldehyde dehydrogenase 1A1; 3-deoxyglucosone dehydrogenase; ALDH-E1; ALHDII; Aldehyde dehydrogenase family 1 member A1; Aldehyde dehydrogenase, cytosolic; Retinal dehydrogenase 1; RALDH 1; RalDH1; EC 1.2.1.19; EC 1.2.1.28; EC 1.2.1.3; EC 1.2.1.36 from Homo sapiens (Human) (see 7 papers)
40% identity, 100% coverage: 1:492/494 of query aligns to 1:495/501 of P00352
- M1 (= M1) modified: Initiator methionine, Removed
- S2 (= S2) modified: N-acetylserine
- N121 (≠ G116) to S: in dbSNP:rs1049981
- IPWN 167:170 (≠ TPWN 165:168) binding NAD(+)
- I177 (≠ A175) to F: in dbSNP:rs8187929
- KPAE 193:196 (≠ KPSE 191:194) binding NAD(+)
- GP 226:227 (≠ GA 224:225) binding NAD(+)
- GS 246:247 (= GS 244:245) binding NAD(+)
- E269 (= E266) active site, Proton acceptor
- ELG 269:271 (= ELG 266:268) binding NAD(+)
- C302 (≠ V299) mutation C->A,S: Does not prevent inhibition by duocarmycin analogs.
- C303 (= C300) active site, Nucleophile
- EQYDK 349:353 (≠ RHRAG 346:350) binding NAD(+)
- EIF 400:402 (≠ EVF 397:399) binding NAD(+)
- G458 (= G455) mutation to N: No significant effect on aldehyde dehydrogenase activity. Prevents the inhibition by ALDH1A1-specific inhibitors.
Sites not aligning to the query:
- 336:501 Mediates interaction with PRMT3
4wb9A Human aldh1a1 complexed with nadh (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 7:487/493 of 4wb9A
- active site: N162 (= N168), K185 (= K191), E261 (= E266), C295 (= C300), E392 (= E397), E469 (= E474)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I158 (= I164), I159 (≠ T165), P160 (= P166), W161 (= W167), N162 (= N168), K185 (= K191), E188 (= E194), G218 (= G224), G222 (= G228), F236 (= F242), T237 (= T243), G238 (= G244), S239 (= S245), V242 (= V248), G263 (= G268), C295 (= C300), Q342 (≠ H347), K345 (≠ G350), E392 (= E397), F394 (= F399)
8t0tA Structure of compound 4 bound to human aldh1a1 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 8t0tA
7um9A Human aldh1a1 with bound compound cm38 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 7um9A
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (≠ T165), P161 (= P166), W162 (= W167), N163 (= N168), K186 (= K191), E189 (= E194), G219 (= G224), G223 (= G228), F237 (= F242), T238 (= T243), G239 (= G244), S240 (= S245), V243 (= V248), E262 (= E266), G264 (= G268), Q343 (≠ H347), K346 (≠ G350), E393 (= E397), F395 (= F399)
- binding (4-methylfuro[3,2-c]quinolin-2-yl)(piperidin-1-yl)methanone: W171 (= W176), H286 (≠ D290), Y290 (≠ G294), I297 (≠ V301), G451 (= G455)
5l2oA Crystal structure of aldh1a1 in complex with buc22 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 5l2oA
5l2nA Structure of aldh1a1 in complex with buc25 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 5l2nA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E397), E470 (= E474)
- binding 3-benzyl-4-methyl-2-oxo-2H-1-benzopyran-7-yl methanesulfonate: F164 (≠ G169), M168 (≠ I173), W171 (= W176), H286 (≠ D290), G287 (≠ A291), Y290 (≠ G294), C295 (≠ V299), C296 (= C300), I297 (≠ V301), Y450 (≠ H454), G451 (= G455), V453 (≠ P457), F459 (≠ I463)
5l2mA Structure of aldh1a1 in complex with buc11 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 5l2mA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E397), E470 (= E474)
- binding 2,3,5-trimethyl-6-[3-oxo-3-(piperidin-1-yl)propyl]-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ G169), F283 (≠ G287), H286 (≠ D290), Y290 (≠ G294)
4wpnA Structure of human aldh1a1 with inhibitor cm053 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 4wpnA
- active site: N163 (= N168), K186 (= K191), E262 (= E266), C296 (= C300), E393 (= E397), E470 (= E474)
- binding 1-{[1,3-dimethyl-7-(3-methylbutyl)-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-8-yl]methyl}piperidine-4-carboxamide: F164 (≠ G169), H286 (≠ D290), G287 (≠ A291), Y290 (≠ G294), C295 (≠ V299), I297 (≠ V301), G451 (= G455), V453 (≠ P457)
8t0nA Structure of compound 4 bound to human aldh1a1 (see paper)
40% identity, 97% coverage: 12:492/494 of query aligns to 8:488/494 of 8t0nA
- binding nicotinamide-adenine-dinucleotide: I159 (= I164), I160 (≠ T165), P161 (= P166), W162 (= W167), N163 (= N168), K186 (= K191), E189 (= E194), G219 (= G224), G223 (= G228), A224 (= A229), F237 (= F242), T238 (= T243), G239 (= G244), S240 (= S245), V243 (= V248), E262 (= E266), G264 (= G268), C296 (= C300), Q343 (≠ H347), K346 (≠ G350), E393 (= E397), F395 (= F399)
- binding 2-methoxy-6-{[(1-propyl-1H-benzimidazol-2-yl)amino]methyl}phenol: S114 (≠ G116), G118 (≠ A120), T122 (= T124), V167 (= V172), W171 (= W176), V453 (≠ P457), S454 (≠ E458), A455 (≠ L459)
Query Sequence
>WP_079650369.1 NCBI__GCF_900167915.1:WP_079650369.1
MSTAGPSAATLDFLTRPRPYLVGDRWEEGRTVPADVLDPSTGRPCGMAHVADPAAVDRAA
AAARAAFDDRRWRGKTPAERQRILWRIADLIERDAQLLAELETLNGGKPLGAALHGEVAA
AAETFRYYAGWVTKIDGGTFDPSVPGQSFLGYGRHEPVGVAALITPWNGPLVIAAWKLAP
ALAAGCCAILKPSELTPFTTLHLAALALEAGVPEGVVQVLPGIGATVGAALARHPGIDKI
SFTGSTAVGRRLMADASGDLKRLSLELGGKSPVLIFADADLDRAAEGAADAIFGNAGQVC
VAGSRVYVERSIEAALVERLADIAGRMRIGPGFDPLTQMGPLISDRHRAGVDGFVRRARE
AGATIVTGGEPIDGPGFFYPPTIVTGCRQDSELVQGEVFGPVLAVQSFVDEAEAVRLAND
SSYGLAASIWTRDVGRAHRVAADVRAGIVWVNSHGIPELAMPIGGMKQSGIGREHGWAGL
EAFTEFKSVMLRAD
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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