SitesBLAST
Comparing SM_b21635 FitnessBrowser__Smeli:SM_b21635 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)
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
55% identity, 98% coverage: 9:682/688 of query aligns to 1:673/678 of 6jqoA
- active site: N157 (= N165), E255 (= E263), C294 (= C302), L483 (= L496)
- binding crotonyl coenzyme a: V97 (≠ I105), F107 (= F115), S111 (= S119), F158 (= F166), W161 (= W169), R638 (≠ S652)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N162), F156 (= F164), N157 (= N165), T183 (≠ S191), T230 (= T238), G231 (= G239), S232 (= S240), T235 (= T243), A256 (= A264), D257 (= D265), C294 (= C302)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
55% identity, 98% coverage: 9:682/688 of query aligns to 1:673/678 of 6jqnA
- active site: N157 (= N165), E255 (= E263), C294 (= C302), L483 (= L496)
- binding octanoyl-coenzyme a: F562 (= F575), H565 (= H578), F576 (= F590), G583 (= G597), V595 (= V609), A604 (= A618), N605 (= N619), Y606 (= Y620), F613 (= F627), I614 (≠ L628)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (≠ V27), I153 (= I161), N154 (= N162), A155 (= A163), F156 (= F164), K180 (= K188), A182 (= A190), T183 (≠ S191), T230 (= T238), G231 (= G239), S232 (= S240), T235 (= T243), L239 (= L247), E255 (= E263), A256 (= A264), D257 (= D265), C294 (= C302), F396 (= F409), H471 (= H484)
6jqmA Structure of paaz with NADPH (see paper)
55% identity, 98% coverage: 9:682/688 of query aligns to 1:673/678 of 6jqmA
- active site: N157 (= N165), E255 (= E263), C294 (= C302), L483 (= L496)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (≠ V27), I153 (= I161), N154 (= N162), A155 (= A163), F156 (= F164), N157 (= N165), K180 (= K188), A182 (= A190), T183 (≠ S191), G231 (= G239), S232 (= S240), T235 (= T243), A256 (= A264), D257 (= D265), C294 (= C302), E394 (= E407), F396 (= F409)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
55% identity, 98% coverage: 9:682/688 of query aligns to 2:674/681 of P77455
- E256 (= E263) mutation to Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA.
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
47% identity, 69% coverage: 11:484/688 of query aligns to 6:484/521 of 2vroA
- active site: N160 (= N165), K183 (= K188), E258 (= E263), C297 (= C302), E401 (= E407)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I161), K183 (= K188), S217 (≠ P222), S235 (= S240), T238 (= T243), L242 (= L247), F403 (= F409)
Sites not aligning to the query:
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
46% identity, 69% coverage: 11:484/688 of query aligns to 6:483/529 of 2y53A
- active site: N160 (= N165), K183 (= K188), Q258 (≠ E263), C297 (= C302), E401 (= E407)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I161), N157 (= N162), F159 (= F164), N160 (= N165), K183 (= K188), A185 (= A190), T186 (≠ S191), S217 (≠ P222), F232 (= F237), G234 (= G239), S235 (= S240), A236 (= A241), T238 (= T243), A259 (= A264), D260 (= D265), C297 (= C302), F403 (= F409)
Sites not aligning to the query:
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
28% identity, 64% coverage: 69:511/688 of query aligns to 67:475/483 of 3b4wA
- active site: N154 (= N165), K177 (= K188), E251 (= E263), C285 (= C302), E384 (= E407), E460 (≠ A490)
- binding nicotinamide-adenine-dinucleotide: I150 (= I161), V151 (≠ N162), W153 (≠ F164), N154 (= N165), K177 (= K188), I210 (vs. gap), G213 (= G223), T228 (= T238), G229 (= G239), S230 (= S240), V233 (≠ T243), E236 (≠ K246), E251 (= E263), L252 (≠ A264), C285 (= C302), E384 (= E407), F386 (= F409)
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)
26% identity, 64% coverage: 71:512/688 of query aligns to 81:498/505 of 4neaA
- active site: N166 (= N165), K189 (= K188), E264 (= E263), C298 (= C302), E399 (= E407), E476 (≠ A490)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A163), K189 (= K188), E192 (≠ Q192), G222 (vs. gap), G226 (= G223), G242 (= G239), G243 (≠ S240), T246 (= T243), H249 (≠ K246), I250 (≠ L247), C298 (= C302), E399 (= E407), F401 (= F409)
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
29% identity, 67% coverage: 36:496/688 of query aligns to 31:471/485 of 4u3wA
Sites not aligning to the query:
4npiA 1.94 angstroms x-ray crystal structure of NAD- and intermediate- bound alpha-aminomuconate-epsilon-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
26% identity, 62% coverage: 65:492/688 of query aligns to 57:466/483 of 4npiA
- active site: N152 (= N165), K175 (= K188), E251 (= E263), C285 (= C302), E387 (= E407), E464 (≠ A490)
- binding (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (≠ G109), L157 (≠ G170), W160 (≠ E173), E251 (= E263), C285 (= C302), Y445 (≠ V461), R447 (≠ I463), F453 (≠ L479)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), S149 (≠ N162), P150 (≠ A163), W151 (≠ F164), K175 (= K188), E178 (≠ S191), G208 (vs. gap), G213 (= G223), E214 (≠ D224), F227 (= F237), G229 (= G239), E230 (≠ S240), T233 (= T243), G253 (≠ D265), C285 (= C302), K335 (≠ E352), E387 (= E407), F389 (= F409)
4i2rA 2.15 angstroms x-ray crystal structure of NAD- and alternative substrate-bound 2-aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
26% identity, 62% coverage: 65:492/688 of query aligns to 57:466/483 of 4i2rA
- active site: N152 (= N165), K175 (= K188), E251 (= E263), C285 (= C302), E387 (= E407), E464 (≠ A490)
- binding (2E,4E)-2-hydroxy-6-oxohexa-2,4-dienoic acid: R103 (≠ G109), L157 (≠ G170), C285 (= C302), Y445 (≠ V461), R447 (≠ I463), F453 (≠ L479)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), S149 (≠ N162), W151 (≠ F164), N152 (= N165), K175 (= K188), E178 (≠ S191), G208 (vs. gap), F227 (= F237), T228 (= T238), G229 (= G239), E230 (≠ S240), T233 (= T243), E251 (= E263), L252 (≠ A264), G253 (≠ D265), C285 (= C302), E387 (= E407), F389 (= F409)
4i25A 2.00 angstroms x-ray crystal structure of NAD- and substrate-bound 2- aminomuconate 6-semialdehyde dehydrogenase from pseudomonas fluorescens (see paper)
26% identity, 62% coverage: 65:492/688 of query aligns to 57:466/483 of 4i25A
- active site: N152 (= N165), K175 (= K188), E251 (= E263), C285 (= C302), E387 (= E407), E464 (≠ A490)
- binding (2E,4E)-2-amino-6-oxohexa-2,4-dienoic acid: R103 (≠ G109), L157 (≠ G170), C285 (= C302), Y445 (≠ V461), R447 (≠ I463), F453 (≠ L479)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), S149 (≠ N162), P150 (≠ A163), W151 (≠ F164), N152 (= N165), K175 (= K188), E178 (≠ S191), G208 (vs. gap), G213 (= G223), F227 (= F237), T228 (= T238), G229 (= G239), E230 (≠ S240), T233 (= T243), E251 (= E263), L252 (≠ A264), C285 (= C302), E387 (= E407), F389 (= F409)
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)
26% identity, 72% coverage: 14:511/688 of query aligns to 41:509/518 of Q63639
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
25% identity, 72% coverage: 14:511/688 of query aligns to 8:473/477 of 2opxA
- active site: N151 (= N165), K174 (= K188), E249 (= E263), C283 (= C302), E381 (= E407), A458 (≠ E494)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ I111), F152 (= F166), N284 (≠ T303), F312 (≠ L331), G313 (= G332), R318 (≠ E337), D320 (vs. gap), I321 (≠ V339), A322 (≠ R340), Y362 (≠ L387), F440 (≠ A469), F440 (≠ A469), E441 (≠ K470)
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
24% identity, 67% coverage: 12:475/688 of query aligns to 7:452/454 of 3ty7B
4ou2A A 2.15 angstroms x-ray crystal structure of e268a 2-aminomuconate 6- semialdehyde dehydrogenase catalytic intermediate from pseudomonas fluorescens (see paper)
26% identity, 62% coverage: 65:492/688 of query aligns to 57:466/483 of 4ou2A
- active site: N152 (= N165), K175 (= K188), A251 (≠ T261), C285 (= C302), E387 (= E407), E464 (≠ A490)
- binding (2Z,4E)-2,6-dihydroxyhexa-2,4-dienoic acid: R103 (≠ G109), L157 (≠ G170), C285 (= C302), Y445 (≠ V461), R447 (≠ I463), F453 (≠ L479)
- binding nicotinamide-adenine-dinucleotide: I148 (= I161), S149 (≠ N162), P150 (≠ A163), W151 (≠ F164), N152 (= N165), K175 (= K188), G208 (vs. gap), G213 (= G223), E214 (≠ D224), F227 (= F237), T228 (= T238), G229 (= G239), E230 (≠ S240), T233 (= T243), A251 (≠ T261), L252 (≠ M262), G253 (≠ E263), C285 (= C302), E387 (= E407), F389 (= F409)
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)]; Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase; Triosephosphate dehydrogenase; EC 1.2.1.9 from Streptococcus mutans serotype c (strain ATCC 700610 / UA159) (see 3 papers)
24% identity, 66% coverage: 9:464/688 of query aligns to 3:438/475 of Q59931
- R103 (≠ G110) binding
- S151 (≠ N162) binding
- K177 (= K188) binding
- T180 (≠ S191) binding
- D215 (= D227) binding
- 230:251 (vs. 239:264, 15% identical) binding
- E377 (= E407) binding
- R437 (≠ I463) binding
2esdA Crystal structure of thioacylenzyme intermediate of an NADP dependent aldehyde dehydrogenase (see paper)
24% identity, 66% coverage: 9:464/688 of query aligns to 2:437/474 of 2esdA
- active site: N153 (= N165), K176 (= K188), A249 (= A277), C283 (= C302), E376 (= E407)
- binding glyceraldehyde-3-phosphate: R102 (≠ G110), Y154 (≠ F166), R282 (≠ K301), C283 (= C302), T284 (= T303), Q435 (≠ M462), R436 (≠ I463)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: F152 (= F164), K176 (= K188), P178 (≠ A190), T179 (≠ S191), G209 (≠ P222), G213 (≠ L226), D214 (= D227), F227 (= F237), S230 (= S240), I233 (≠ T243), K328 (≠ D348), S329 (≠ Q349), Y332 (≠ E352)
Sites not aligning to the query:
P25553 Lactaldehyde dehydrogenase; Aldehyde dehydrogenase A; Glycolaldehyde dehydrogenase; EC 1.2.1.22; EC 1.2.1.21 from Escherichia coli (strain K12) (see 5 papers)
25% identity, 72% coverage: 14:511/688 of query aligns to 10:475/479 of P25553
- L150 (≠ N162) binding
- R161 (≠ E173) binding
- KPSE 176:179 (≠ KPAS 188:191) binding
- F180 (≠ Q192) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D224) binding
- S230 (= S240) binding
- E251 (= E263) binding
- N286 (≠ T303) binding ; mutation to E: 4-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to H: 15-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.; mutation to T: 6-fold increase in catalytic efficiency with L-lactaldehyde as substrate. Shows expanded substrate specificity.
- R336 (≠ E352) binding
- E443 (≠ K470) binding
- H449 (= H484) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2impA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the ternary complex with lactate (occupancy 0.5) and nadh. Crystals soaked with (l)-lactate. (see paper)
25% identity, 72% coverage: 14:511/688 of query aligns to 8:473/477 of 2impA
- active site: N151 (= N165), K174 (= K188), E249 (= E263), C283 (= C302), E381 (= E407), A458 (≠ E494)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I161), L148 (≠ N162), P149 (≠ A163), W150 (≠ F164), K174 (= K188), E177 (≠ S191), F178 (≠ Q192), G207 (vs. gap), G211 (= G223), Q212 (≠ D224), S228 (= S240), A231 (≠ T243), K234 (= K246), R334 (≠ E352)
Query Sequence
>SM_b21635 FitnessBrowser__Smeli:SM_b21635
MNVVADRPRRLESYIAGAWMRGSKDGVTLCDAATGAPVALVDSSGIDFAAALAYGREKGG
PALRRMSFHERAMMLKALAQALMERKEEFYALSTATGATRADSWIDIEGGIGTLFSYASK
GRRELPNSHVLLDGDVEALSRDGTFSAQHILTPLQGIAVHINAFNFPCWGMLEKLAPTLL
AGMPAIVKPASQTAYLAELVVRRIVDTGLLPEGALQLVCGSPGDLLDRVGDQDVVTFTGS
ATTGRKLKTHPAIVGNSVRFTMEADSLNAAVLGLDAAPGAEEFGLFVREVAREMTSKAGQ
KCTAIRRVIAPRAHCDALITALGERLAKVPLGDPADENVRMGPLASRDQREEVRARILDL
TTDAEIVAGDPARPQLVSGDAEAGAFLNPVLLYCDSPDAARSVHDVEAFGPVSTVMPYDT
AEEAVDLVRRGRGSLVTSVFTNDPDIARELVIGMAPFHGRVMIGNRLSAKSSTGHGSPLP
GLVHGGPGRAGGGEELGGMRGVRHYMQRTAVQGAPGLVAAVTGRWMEGAPARSGGEHPFR
KSLAELRVGDQIVTETRTVTLEDIEHFAEFTGDTFYAHMDEEAARANPFFDGRVAHGYLV
VSLAAGLFVDPAPGPVLANYGVDGMRFLTPVYPGDTLQVRLTCKEISPRINSDYGEVRWD
CRVTNQTGATVAQYDVLTMVAKTGSGEE
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