SitesBLAST
Comparing WP_023432018.1 NCBI__GCF_000496075.1:WP_023432018.1 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
43% identity, 97% coverage: 4:482/492 of query aligns to 3:481/489 of 4o6rA
- active site: N150 (= N152), K173 (= K175), E248 (= E249), C282 (= C283), E383 (= E384), E460 (= E461)
- binding adenosine monophosphate: I146 (= I148), V147 (≠ T149), K173 (= K175), G206 (= G208), G210 (= G211), Q211 (≠ P212), F224 (= F225), G226 (= G227), S227 (≠ G228), T230 (= T231), R233 (= R234)
Q28399 Aldehyde dehydrogenase, cytosolic 1; ALDH class 1; ETA-crystallin; EC 1.2.1.3 from Elephantulus edwardii (Cape long-eared elephant shrew) (see paper)
42% identity, 97% coverage: 6:484/492 of query aligns to 22:500/501 of Q28399
1o9jA The x-ray crystal structure of eta-crystallin (see paper)
42% identity, 97% coverage: 6:484/492 of query aligns to 15:493/494 of 1o9jA
- active site: N163 (= N152), K186 (= K175), E262 (= E249), C296 (= C283), E393 (= E384), E470 (= E461)
- binding nicotinamide-adenine-dinucleotide: I159 (= I148), F160 (≠ T149), P161 (≠ A150), W162 (= W151), N163 (= N152), K186 (= K175), E189 (= E178), G219 (= G208), G223 (= G211), F237 (= F225), T238 (= T226), G239 (= G227), S240 (≠ G228), V243 (≠ T231), E262 (= E249), L263 (= L250), C296 (= C283), E393 (= E384), F395 (= F386), L421 (= L412)
P47895 Retinaldehyde dehydrogenase 3; RALDH-3; RalDH3; Aldehyde dehydrogenase 6; Aldehyde dehydrogenase family 1 member A3; ALDH1A3; EC 1.2.1.36 from Homo sapiens (Human) (see 2 papers)
42% identity, 98% coverage: 6:487/492 of query aligns to 33:512/512 of P47895
- R89 (= R60) to C: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514652
- K204 (= K175) binding NAD(+)
- E207 (= E178) binding NAD(+)
- GSTEVG 257:262 (≠ GGLPTA 227:232) binding NAD(+)
- Q361 (= Q330) binding NAD(+)
- E411 (= E384) binding NAD(+)
- A493 (≠ T466) to P: in MCOP8; does not affect ALDH1A3 expression; results in strongly reduced protein levels; dbSNP:rs397514653
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
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)
44% identity, 97% coverage: 6:480/492 of query aligns to 39:513/518 of O94788
- E50 (≠ S17) to G: in dbSNP:rs34266719
- A110 (= A75) to V: in dbSNP:rs35365164
- Q182 (≠ L147) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ TAW 149:151) binding NAD(+)
- KPAE 210:213 (≠ KPSE 175:178) binding NAD(+)
- STE 264:266 (≠ GLP 228:230) binding NAD(+)
- C320 (= C283) active site, Nucleophile
- R347 (≠ I310) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R311) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ AQFDR 329:333) binding NAD(+)
- A383 (= A346) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E384) binding NAD(+)
- E436 (≠ R403) to K: in dbSNP:rs34744827
- S461 (≠ A428) to Y: in DIH4; decreased retinoic acid biosynthetic process
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 97% coverage: 4:480/492 of query aligns to 16:490/491 of 5gtlA
- active site: N165 (= N152), K188 (= K175), E263 (= E249), C297 (= C283), E394 (= E384), E471 (= E461)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I148), P163 (≠ A150), K188 (= K175), A190 (≠ S177), E191 (= E178), Q192 (≠ H179), G221 (= G208), G225 (= G211), G241 (= G227), S242 (≠ G228), T245 (= T231), L264 (= L250), C297 (= C283), E394 (= E384), F396 (= F386)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
41% identity, 97% coverage: 4:480/492 of query aligns to 16:490/491 of 5gtkA
- active site: N165 (= N152), K188 (= K175), E263 (= E249), C297 (= C283), E394 (= E384), E471 (= E461)
- binding nicotinamide-adenine-dinucleotide: I161 (= I148), I162 (≠ T149), P163 (≠ A150), W164 (= W151), K188 (= K175), E191 (= E178), G221 (= G208), G225 (= G211), A226 (≠ P212), F239 (= F225), G241 (= G227), S242 (≠ G228), T245 (= T231), Y248 (≠ R234), L264 (= L250), C297 (= C283), Q344 (= Q330), R347 (= R333), E394 (= E384), F396 (= F386)
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, 97% coverage: 6:480/492 of query aligns to 13:487/492 of 6b5hA
- active site: N161 (= N152), E260 (= E249), C294 (= C283), E468 (= E461)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ S102), G116 (≠ F106), F162 (≠ S153), W169 (≠ N160), Q284 (≠ A273), F288 (≠ G277), T295 (≠ I284), N449 (≠ R442), L451 (≠ S444), N452 (≠ Y445), F457 (= F450)
- binding nicotinamide-adenine-dinucleotide: I157 (= I148), I158 (≠ T149), W160 (= W151), N161 (= N152), K184 (= K175), G217 (= G208), G221 (= G211), F235 (= F225), T236 (= T226), G237 (= G227), S238 (≠ G228), V241 (≠ T231), E260 (= E249), L261 (= L250), C294 (= C283), F393 (= F386)
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, 97% coverage: 6:480/492 of query aligns to 13:487/492 of 6b5gA
- active site: N161 (= N152), E260 (= E249), C294 (= C283), E468 (= E461)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ S153), L165 (≠ P156), W169 (≠ N160), F288 (≠ G277), C293 (≠ T282), C294 (= C283), T295 (≠ I284), N449 (≠ R442), L451 (≠ S444)
- binding nicotinamide-adenine-dinucleotide: I157 (= I148), I158 (≠ T149), P159 (≠ A150), W160 (= W151), N161 (= N152), M166 (≠ L157), K184 (= K175), E187 (= E178), G217 (= G208), G221 (= G211), F235 (= F225), T236 (= T226), G237 (= G227), S238 (≠ G228), V241 (≠ T231), E260 (= E249), L261 (= L250), C294 (= C283), E391 (= E384), F393 (= F386)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
44% identity, 97% coverage: 6:480/492 of query aligns to 13:487/492 of 6aljA