SitesBLAST
Comparing WP_012592831.1 NCBI__GCF_000021745.1:WP_012592831.1 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)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
52% identity, 97% coverage: 17:506/507 of query aligns to 8:490/491 of 5gtlA
- active site: N165 (= N180), K188 (= K203), E263 (= E278), C297 (= C312), E394 (= E409), E471 (= E487)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I176), P163 (= P178), K188 (= K203), A190 (= A205), E191 (= E206), Q192 (≠ E207), G221 (= G236), G225 (= G240), G241 (= G256), S242 (= S257), T245 (≠ V260), L264 (= L279), C297 (= C312), E394 (= E409), F396 (= F411)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
52% identity, 97% coverage: 17:506/507 of query aligns to 8:490/491 of 5gtkA
- active site: N165 (= N180), K188 (= K203), E263 (= E278), C297 (= C312), E394 (= E409), E471 (= E487)
- binding nicotinamide-adenine-dinucleotide: I161 (= I176), I162 (= I177), P163 (= P178), W164 (= W179), K188 (= K203), E191 (= E206), G221 (= G236), G225 (= G240), A226 (= A241), F239 (= F254), G241 (= G256), S242 (= S257), T245 (≠ V260), Y248 (≠ L263), L264 (= L279), C297 (= C312), Q344 (= Q359), R347 (= R362), E394 (= E409), F396 (= F411)
P05091 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Homo sapiens (Human) (see 5 papers)
52% identity, 94% coverage: 28:506/507 of query aligns to 39:512/517 of P05091
- E337 (= E330) to V: in dbSNP:rs1062136
- E496 (≠ Q490) to K: in allele ALDH2*3; dbSNP:rs769724893
- E504 (= E498) to K: in AMEDS; allele ALDH2*2; drastic reduction of enzyme activity; dbSNP:rs671
Sites not aligning to the query:
5l13A Structure of aldh2 in complex with 2p3 (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 5l13A
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F181), M168 (= M185), W171 (= W188), F290 (= F306), C295 (= C311), C296 (= C312), C297 (≠ N313), D451 (≠ H468), F453 (= F470)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 4kwgA
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F181), M168 (= M185), C295 (= C311), C296 (= C312), C297 (≠ N313), D451 (≠ H468), F453 (= F470)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 4kwfA
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F181), M168 (= M185), W171 (= W188), E262 (= E278), C295 (= C311), C296 (= C312), C297 (≠ N313), D451 (≠ H468), F453 (= F470), F459 (= F476)
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)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 3sz9A
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F181), C295 (= C311), C296 (= C312), D451 (≠ H468), F453 (= F470), F459 (= F476)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 3injA
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L129), F164 (= F181), L167 (= L184), F286 (≠ A302), F290 (= F306), D451 (≠ H468), F453 (= F470)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 2vleA
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding daidzin: M118 (≠ L129), F164 (= F181), M168 (= M185), W171 (= W188), F286 (≠ A302), F290 (= F306), C295 (= C311), C296 (= C312), D451 (≠ H468), V452 (= V469), F453 (= F470)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 1o01B
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding (2e)-but-2-enal: C296 (= C312), C297 (≠ N313), F453 (= F470)
- binding nicotinamide-adenine-dinucleotide: I159 (= I176), I160 (= I177), P161 (= P178), W162 (= W179), K186 (= K203), E189 (= E206), G219 (= G236), G223 (= G240), A224 (= A241), F237 (= F254), G239 (= G256), S240 (= S257), I243 (≠ V260), L263 (= L279), G264 (= G280), C296 (= C312), Q343 (= Q359), E393 (= E409), F395 (= F411)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 1cw3A
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding magnesium ion: V34 (≠ F46), D103 (= D114), Q190 (≠ E207)
- binding nicotinamide-adenine-dinucleotide: I159 (= I176), I160 (= I177), P161 (= P178), W162 (= W179), K186 (= K203), G219 (= G236), G223 (= G240), A224 (= A241), F237 (= F254), G239 (= G256), S240 (= S257), I243 (≠ V260), L263 (= L279), G264 (= G280), C296 (= C312), Q343 (= Q359), K346 (≠ R362), E393 (= E409), F395 (= F411)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
50% identity, 99% coverage: 4:506/507 of query aligns to 18:515/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
51% identity, 94% coverage: 28:506/507 of query aligns to 18:491/496 of 4fr8C
- active site: N165 (= N180), K188 (= K203), Q264 (≠ E278), C298 (= C312), E395 (= E409), E472 (= E487)
- binding nicotinamide-adenine-dinucleotide: I161 (= I176), I162 (= I177), W164 (= W179), K188 (= K203), G221 (= G236), G225 (= G240), A226 (= A241), F239 (= F254), G241 (= G256), S242 (= S257), I245 (≠ V260), Q345 (= Q359), E395 (= E409), F397 (= F411)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
51% identity, 94% coverage: 28:506/507 of query aligns to 15:488/493 of 4fr8A
- active site: N162 (= N180), K185 (= K203), Q261 (≠ E278), C295 (= C312), E392 (= E409), E469 (= E487)
- binding nicotinamide-adenine-dinucleotide: I158 (= I176), I159 (= I177), W161 (= W179), K185 (= K203), G218 (= G236), G222 (= G240), A223 (= A241), F236 (= F254), G238 (= G256), S239 (= S257), I242 (≠ V260), Q342 (= Q359), K345 (≠ R362), E392 (= E409), F394 (= F411)
- binding propane-1,2,3-triyl trinitrate: F163 (= F181), L166 (= L184), W170 (= W188), F289 (= F306), S294 (≠ C311), C295 (= C312), D450 (≠ H468), F452 (= F470)
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
52% identity, 94% coverage: 28:506/507 of query aligns to 16:489/494 of 1nzwA
- active site: N163 (= N180), K186 (= K203), E262 (= E278), S296 (≠ C312), E393 (= E409), E470 (= E487)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I176), I160 (= I177), P161 (= P178), K186 (= K203), E189 (= E206), G219 (= G236), P220 (≠ E237), G223 (= G240), A224 (= A241), F237 (= F254), G239 (= G256), S240 (= S257), I243 (≠ V260), E262 (= E278), G264 (= G280), S296 (≠ C312), Q343 (= Q359), E393 (= E409), F395 (= F411)
2onmA Human mitochondrial aldehyde dehydrogenase asian variant, aldh2 2, Complexed with NAD+ (see paper)
52% identity, 93% coverage: 28:496/507 of query aligns to 16:479/494 of 2onmA
- active site: N163 (= N180), K186 (= K203), E262 (= E278), C296 (= C312), E393 (= E409), E470 (= E487)
- binding adenosine-5'-diphosphate: E189 (= E206), G219 (= G236), G223 (= G240), A224 (= A241), F237 (= F254), G239 (= G256), S240 (= S257), I243 (≠ V260)
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)
47% identity, 99% coverage: 5:506/507 of query aligns to 17:513/518 of O94788
- E50 (≠ V38) to G: in dbSNP:rs34266719
- A110 (≠ G97) to V: in dbSNP:rs35365164
- Q182 (= Q175) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (= IPW 177:179) binding NAD(+)
- KPAE 210:213 (≠ KIAE 203:206) binding NAD(+)
- STE 264:266 (= STE 257:259) binding NAD(+)
- C320 (= C312) active site, Nucleophile
- R347 (≠ I339) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K340) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ VQYDR 358:362) binding NAD(+)
- A383 (= A375) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E409) binding NAD(+)
- E436 (≠ A429) to K: in dbSNP:rs34744827
- S461 (≠ A454) 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)
49% identity, 94% coverage: 28:506/507 of query aligns to 14:487/492 of 6b5hA
- active site: N161 (= N180), E260 (= E278), C294 (= C312), E468 (= E487)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ A125), G116 (≠ L129), F162 (= F181), W169 (= W188), Q284 (≠ A302), F288 (= F306), T295 (≠ N313), N449 (≠ H468), L451 (≠ F470), N452 (≠ D471), F457 (= F476)
- binding nicotinamide-adenine-dinucleotide: I157 (= I176), I158 (= I177), W160 (= W179), N161 (= N180), K184 (= K203), G217 (= G236), G221 (= G240), F235 (= F254), T236 (= T255), G237 (= G256), S238 (= S257), V241 (= V260), E260 (= E278), L261 (= L279), C294 (= C312), F393 (= F411)
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)
49% identity, 94% coverage: 28:506/507 of query aligns to 14:487/492 of 6b5gA
- active site: N161 (= N180), E260 (= E278), C294 (= C312), E468 (= E487)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F181), L165 (= L184), W169 (= W188), F288 (= F306), C293 (= C311), C294 (= C312), T295 (≠ N313), N449 (≠ H468), L451 (≠ F470)
- binding nicotinamide-adenine-dinucleotide: I157 (= I176), I158 (= I177), P159 (= P178), W160 (= W179), N161 (= N180), M166 (= M185), K184 (= K203), E187 (= E206), G217 (= G236), G221 (= G240), F235 (= F254), T236 (= T255), G237 (= G256), S238 (= S257), V241 (= V260), E260 (= E278), L261 (= L279), C294 (= C312), E391 (= E409), F393 (= F411)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
49% identity, 94% coverage: 28:506/507 of query aligns to 14:487/492 of 6aljA
- active site: N161 (= N180), E260 (= E278), C294 (= C312), E468 (= E487)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ L129), F162 (= F181), L165 (= L184), M166 (= M185), W169 (= W188), E260 (= E278), C293 (= C311), C294 (= C312), L451 (≠ F470), N452 (≠ D471), A453 (= A472)
- binding nicotinamide-adenine-dinucleotide: I157 (= I176), I158 (= I177), P159 (= P178), W160 (= W179), N161 (= N180), K184 (= K203), E187 (= E206), G217 (= G236), G221 (= G240), F235 (= F254), G237 (= G256), S238 (= S257), V241 (= V260), Q341 (= Q359), K344 (≠ R362), E391 (= E409), F393 (= F411)
Query Sequence
>WP_012592831.1 NCBI__GCF_000021745.1:WP_012592831.1
MNVRANVSAAAAVIPDEIRNWLSGPRPMLIDGKWVKSVSGKTFDVFDPATGEKIASVAEG
DAADVDLAVAAARRAFESGPWSRMTPSERGRIIHRIGDLILDHADELAAIESLDNGKPKA
VAKAADVTLSADMFHYMSGWATKLEGKHIPISALTAPGMEFVSMTRLEPIGVVGQIIPWN
FPLLMAAWKLAPALTTGCAVVLKIAEETPLSALRLGELLIEAGVPDGVVNIVPGFGETAG
AALAGHPGVDKVAFTGSTEVGRLIVQAASRDLKKVSLELGGKSPNIVLGDADPEMAIAGA
TAAIFFNHGQCCNAGSRLFVQRNLFDKVVEGIAAQAEKIKLGHGLNAETEMGPLVSRVQY
DRVTGLLASGRQEGARAVCGGEGLGGAGYFVPPTVLVDTNPGMRVVREEIFGPVLVATPF
DEPDDALIAEANNTIYGLAAGVWSGNTGRAHQIANRLRAGTVWINCYHVFDAALPFGGYK
QSGWGREMGQAVLSNYLEAKAITTRIG
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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