SitesBLAST
Comparing PfGW456L13_4766 4-aminobutyraldehyde dehydrogenase (EC 1.2.1.19) 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)
P77674 Gamma-aminobutyraldehyde dehydrogenase; ABALDH; 1-pyrroline dehydrogenase; 4-aminobutanal dehydrogenase; 5-aminopentanal dehydrogenase; EC 1.2.1.19; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
75% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of P77674
1wndA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase as determined by kinetics and crystal structure (see paper)
75% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of 1wndA
- active site: N149 (= N149), K172 (= K172), E246 (= E246), C280 (= C280), E378 (= E378), D455 (= D455)
- binding calcium ion: G249 (= G249), K250 (= K250), A251 (= A251), G405 (= G405), L406 (= L406), A407 (= A407), Y427 (= Y427)
1wnbB Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
75% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of 1wnbB
- active site: N149 (= N149), K172 (= K172), E246 (= E246), C280 (= C280), E378 (= E378), D455 (= D455)
- binding betaine aldehyde: D279 (= D279), F436 (= F436), L438 (= L438)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I145), A146 (= A146), W148 (= W148), K172 (= K172), G204 (= G204), G208 (= G208), D209 (≠ S209), T223 (= T223), G224 (= G224), S225 (= S225), T228 (= T228), H231 (≠ N231), G248 (= G248), E378 (= E378)
1wnbA Escherichia coli ydcw gene product is a medium-chain aldehyde dehydrogenase (complexed with nadh and betaine aldehyde) (see paper)
75% identity, 100% coverage: 1:474/474 of query aligns to 1:474/474 of 1wnbA
- active site: N149 (= N149), K172 (= K172), E246 (= E246), C280 (= C280), E378 (= E378), D455 (= D455)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I145 (= I145), A146 (= A146), W148 (= W148), K172 (= K172), G204 (= G204), G208 (= G208), D209 (≠ S209), G224 (= G224), S225 (= S225), T228 (= T228), H231 (≠ N231), G248 (= G248), F380 (= F380)
4f3xA Crystal structure of putative aldehyde dehydrogenase from sinorhizobium meliloti 1021 complexed with NAD
63% identity, 100% coverage: 1:474/474 of query aligns to 2:475/476 of 4f3xA
- active site: N150 (= N149), K173 (= K172), E247 (= E246), C281 (= C280), E379 (= E378), D456 (= D455)
- binding nicotinamide-adenine-dinucleotide: I146 (= I145), A147 (= A146), P148 (= P147), W149 (= W148), K173 (= K172), E176 (= E175), G205 (= G204), G209 (= G208), I213 (≠ V212), I223 (≠ L222), G225 (= G224), D226 (≠ S225), T229 (= T228), G249 (= G248), C281 (= C280), Q328 (≠ H327), R331 (= R330), E379 (= E378), F381 (= F380)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
44% identity, 99% coverage: 1:470/474 of query aligns to 2:475/489 of 4o6rA
- active site: N150 (= N149), K173 (= K172), E248 (= E246), C282 (= C280), E383 (= E378), E460 (≠ D455)
- binding adenosine monophosphate: I146 (= I145), V147 (≠ A146), K173 (= K172), G206 (= G204), G210 (= G208), Q211 (≠ S209), F224 (≠ L222), G226 (= G224), S227 (= S225), T230 (= T228), R233 (≠ N231)
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 2:470/474 of query aligns to 16:486/491 of 5gtlA
- active site: N165 (= N149), K188 (= K172), E263 (= E246), C297 (= C280), E394 (= E378), E471 (≠ D455)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I145), P163 (= P147), K188 (= K172), A190 (≠ S174), E191 (= E175), Q192 (= Q176), G221 (= G204), G225 (= G208), G241 (= G224), S242 (= S225), T245 (= T228), L264 (= L247), C297 (= C280), E394 (= E378), F396 (= F380)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
39% identity, 99% coverage: 2:470/474 of query aligns to 16:486/491 of 5gtkA
- active site: N165 (= N149), K188 (= K172), E263 (= E246), C297 (= C280), E394 (= E378), E471 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ A146), P163 (= P147), W164 (= W148), K188 (= K172), E191 (= E175), G221 (= G204), G225 (= G208), A226 (≠ S209), F239 (≠ L222), G241 (= G224), S242 (= S225), T245 (= T228), Y248 (≠ N231), L264 (= L247), C297 (= C280), Q344 (≠ H327), R347 (= R330), E394 (= E378), F396 (= F380)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
42% identity, 99% coverage: 1:470/474 of query aligns to 1:473/487 of 4go4A
- active site: N149 (= N149), K172 (= K172), E247 (= E246), C281 (= C280), E381 (= E378), E458 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I145 (= I145), V146 (≠ A146), W148 (= W148), N149 (= N149), F154 (≠ M154), K172 (= K172), G205 (= G204), G209 (= G208), Q210 (≠ S209), F223 (≠ L222), T224 (= T223), G225 (= G224), S226 (= S225), T229 (= T228), E247 (= E246), G249 (= G248), C281 (= C280), E381 (= E378), F383 (= F380)
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)
40% identity, 99% coverage: 3:473/474 of query aligns to 38:512/518 of O94788
- E50 (= E15) to G: in dbSNP:rs34266719
- A110 (= A71) to V: in dbSNP:rs35365164
- Q182 (≠ S144) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ APW 146:148) binding
- KPAE 210:213 (≠ KPSE 172:175) binding
- STE 264:266 (≠ SIA 225:227) binding
- C320 (= C280) active site, Nucleophile
- R347 (≠ I307) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K308) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ QHRDR 326:330) binding
- A383 (≠ I344) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E378) binding
- E436 (≠ G397) to K: in dbSNP:rs34744827
- S461 (= S422) 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)
40% identity, 99% coverage: 3:473/474 of query aligns to 12:486/492 of 6b5hA
- active site: N161 (= N149), E260 (= E246), C294 (= C280), E468 (≠ D455)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ D99), G116 (≠ A103), F162 (≠ Y150), W169 (= W157), Q284 (≠ T270), F288 (≠ Y274), T295 (= T281), N449 (≠ F436), L451 (= L438), N452 (≠ V439), F457 (≠ H444)
- binding nicotinamide-adenine-dinucleotide: I157 (= I145), I158 (≠ A146), W160 (= W148), N161 (= N149), K184 (= K172), G217 (= G204), G221 (= G208), F235 (≠ L222), T236 (= T223), G237 (= G224), S238 (= S225), V241 (≠ T228), E260 (= E246), L261 (= L247), C294 (= C280), F393 (= F380)
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)
40% identity, 99% coverage: 3:473/474 of query aligns to 12:486/492 of 6b5gA
- active site: N161 (= N149), E260 (= E246), C294 (= C280), E468 (≠ D455)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (≠ Y150), L165 (≠ M153), W169 (= W157), F288 (≠ Y274), C293 (≠ D279), C294 (= C280), T295 (= T281), N449 (≠ F436), L451 (= L438)
- binding nicotinamide-adenine-dinucleotide: I157 (= I145), I158 (≠ A146), P159 (= P147), W160 (= W148), N161 (= N149), M166 (= M154), K184 (= K172), E187 (= E175), G217 (= G204), G221 (= G208), F235 (≠ L222), T236 (= T223), G237 (= G224), S238 (= S225), V241 (≠ T228), E260 (= E246), L261 (= L247), C294 (= C280), E391 (= E378), F393 (= F380)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
40% identity, 99% coverage: 3:473/474 of query aligns to 12:486/492 of 6aljA
- active site: N161 (= N149), E260 (= E246), C294 (= C280), E468 (≠ D455)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ A103), F162 (≠ Y150), L165 (≠ M153), M166 (= M154), W169 (= W157), E260 (= E246), C293 (≠ D279), C294 (= C280), L451 (= L438), N452 (≠ V439), A453 (≠ S440)
- binding nicotinamide-adenine-dinucleotide: I157 (= I145), I158 (≠ A146), P159 (= P147), W160 (= W148), N161 (= N149), K184 (= K172), E187 (= E175), G217 (= G204), G221 (= G208), F235 (≠ L222), G237 (= G224), S238 (= S225), V241 (≠ T228), Q341 (≠ H327), K344 (≠ R330), E391 (= E378), F393 (= F380)
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)
39% identity, 99% coverage: 3:473/474 of query aligns to 38:512/518 of Q63639
4neaA 1.90 angstrom resolution crystal structure of betaine aldehyde dehydrogenase (betb) from staphylococcus aureus in complex with NAD+ and bme-free cys289 (see paper)
39% identity, 99% coverage: 1:471/474 of query aligns to 16:492/505 of 4neaA
- active site: N166 (= N149), K189 (= K172), E264 (= E246), C298 (= C280), E399 (= E378), E476 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: P164 (= P147), K189 (= K172), E192 (= E175), G222 (= G204), G226 (= G208), G242 (= G224), G243 (≠ S225), T246 (= T228), H249 (≠ N231), I250 (= I232), C298 (= C280), E399 (= E378), F401 (= F380)
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
41% identity, 99% coverage: 3:471/474 of query aligns to 11:485/494 of 4pz2B
- active site: N159 (= N149), K182 (= K172), E258 (= E246), C292 (= C280), E392 (= E378), D469 (= D455)
- binding nicotinamide-adenine-dinucleotide: I155 (= I145), I156 (≠ A146), P157 (= P147), W158 (= W148), N159 (= N149), M164 (= M154), K182 (= K172), A184 (≠ S174), E185 (= E175), G215 (= G204), G219 (= G208), F233 (≠ L222), T234 (= T223), G235 (= G224), S236 (= S225), V239 (≠ T228), E258 (= E246), L259 (= L247), C292 (= C280), E392 (= E378), F394 (= F380)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
40% identity, 96% coverage: 20:473/474 of query aligns to 31:487/493 of 4fr8A
- active site: N162 (= N149), K185 (= K172), Q261 (≠ E246), C295 (= C280), E392 (= E378), E469 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I158 (= I145), I159 (≠ A146), W161 (= W148), K185 (= K172), G218 (= G204), G222 (= G208), A223 (≠ S209), F236 (≠ L222), G238 (= G224), S239 (= S225), I242 (≠ T228), Q342 (≠ H327), K345 (≠ R330), E392 (= E378), F394 (= F380)
- binding propane-1,2,3-triyl trinitrate: F163 (≠ Y150), L166 (≠ M153), W170 (= W157), F289 (≠ Y274), S294 (≠ D279), C295 (= C280), D450 (≠ F436), F452 (≠ L438)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
40% identity, 96% coverage: 20:473/474 of query aligns to 34:490/496 of 4fr8C
- active site: N165 (= N149), K188 (= K172), Q264 (≠ E246), C298 (= C280), E395 (= E378), E472 (≠ D455)
- binding nicotinamide-adenine-dinucleotide: I161 (= I145), I162 (≠ A146), W164 (= W148), K188 (= K172), G221 (= G204), G225 (= G208), A226 (≠ S209), F239 (≠ L222), G241 (= G224), S242 (= S225), I245 (≠ T228), Q345 (≠ H327), E395 (= E378), F397 (= F380)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
41% identity, 96% coverage: 20:473/474 of query aligns to 58:514/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
5l13A Structure of aldh2 in complex with 2p3 (see paper)
41% identity, 96% coverage: 20:473/474 of query aligns to 32:488/494 of 5l13A
- active site: N163 (= N149), K186 (= K172), E262 (= E246), C296 (= C280), E393 (= E378), E470 (≠ D455)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (≠ Y150), M168 (= M154), W171 (= W157), F290 (≠ Y274), C295 (≠ D279), C296 (= C280), C297 (≠ T281), D451 (≠ F436), F453 (≠ L438)
Query Sequence
>PfGW456L13_4766 4-aminobutyraldehyde dehydrogenase (EC 1.2.1.19)
MQTKLLINGQLQSGEGPAQPVFNPALGSVLVEINEASEAQVDAAVRAADAAFDSWSHTPP
KDRSLLLLKLADAIEARGEELAKLESDNCGKPYSAALNDEIPAIADVFRFFAGASRCMSG
STGGEYLPGHTSMIRRDPVGVIASIAPWNYPLMMVAWKIAPALAAGNTVVLKPSEQTPLT
ALRLAELASDIFPAGVLNLVFGRGPTVGSPLVTHPKVRMVSLTGSIATGSNIISSTADTV
KRMHMELGGKAPVIIFDDADIDAAVEGIRTFGFYNAGQDCTAACRIYAQEGIYDKFVEKL
GAAVSSIKYGLQDDPSTELGPLITAQHRDRVAGFVERAIAQPHIRLITGGKAVEGDGFFF
EPTVLADAQQDDEIVRREVFGPVVSVTKFTDEAQVLGWANDSDYGLASSVWTADVGRAHR
LSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSMYGLEDYTVVRHVMFKH
Or try a new SitesBLAST search
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