SitesBLAST
Comparing BWI76_RS13085 FitnessBrowser__Koxy:BWI76_RS13085 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)
P77455 Bifunctional protein PaaZ; EC 3.3.2.12; EC 1.2.1.91 from Escherichia coli (strain K12) (see paper)
87% identity, 100% coverage: 1:679/681 of query aligns to 1:679/681 of P77455
- E256 (= E256) mutation to Q: Catalyzes the formation of 3-oxo-5,6-dehydrosuberyl-CoA semialdehyde instead of 3-oxo-5,6-dehydrosuberyl-CoA.
6jqoA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ccoa (see paper)
87% identity, 100% coverage: 2:679/681 of query aligns to 1:678/678 of 6jqoA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L484)
- binding crotonyl coenzyme a: V97 (= V98), F107 (= F108), S111 (≠ G112), F158 (= F159), W161 (= W162), R638 (= R639)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: N154 (= N155), F156 (= F157), N157 (= N158), T183 (= T184), T230 (= T231), G231 (= G232), S232 (= S233), T235 (= T236), A256 (= A257), D257 (= D258), C294 (= C295)
6jqnA Structure of paaz, a bifunctional enzyme in complex with NADP+ and ocoa (see paper)
87% identity, 100% coverage: 2:679/681 of query aligns to 1:678/678 of 6jqnA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L484)
- binding octanoyl-coenzyme a: F562 (= F563), H565 (= H566), F576 (= F577), G583 (= G584), V595 (= V596), A604 (= A605), N605 (= N606), Y606 (= Y607), F613 (= F614), I614 (= I615)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: R19 (= R20), I153 (= I154), N154 (= N155), A155 (= A156), F156 (= F157), K180 (= K181), A182 (= A183), T183 (= T184), T230 (= T231), G231 (= G232), S232 (= S233), T235 (= T236), L239 (= L240), E255 (= E256), A256 (= A257), D257 (= D258), C294 (= C295), F396 (= F397), H471 (= H472)
6jqmA Structure of paaz with NADPH (see paper)
87% identity, 100% coverage: 2:679/681 of query aligns to 1:678/678 of 6jqmA
- active site: N157 (= N158), E255 (= E256), C294 (= C295), L483 (= L484)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: R19 (= R20), I153 (= I154), N154 (= N155), A155 (= A156), F156 (= F157), N157 (= N158), K180 (= K181), A182 (= A183), T183 (= T184), G231 (= G232), S232 (= S233), T235 (= T236), A256 (= A257), D257 (= D258), C294 (= C295), E394 (= E395), F396 (= F397)
2vroA Crystal structure of aldehyde dehydrogenase from burkholderia xenovorans lb400 (see paper)
43% identity, 69% coverage: 2:472/681 of query aligns to 4:484/521 of 2vroA
- active site: N160 (= N158), K183 (= K181), E258 (= E256), C297 (= C295), E401 (= E395)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I156 (= I154), K183 (= K181), S217 (≠ A215), S235 (= S233), T238 (= T236), L242 (= L240), F403 (= F397)
Sites not aligning to the query:
2y53A Crystal structure of e257q mutant of the box pathway encoded aldh from burkholderia xenovorans lb400 (see paper)
43% identity, 69% coverage: 2:472/681 of query aligns to 4:483/529 of 2y53A
- active site: N160 (= N158), K183 (= K181), Q258 (≠ E256), C297 (= C295), E401 (= E395)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I156 (= I154), N157 (= N155), F159 (= F157), N160 (= N158), K183 (= K181), A185 (= A183), T186 (= T184), S217 (≠ A215), F232 (= F230), G234 (= G232), S235 (= S233), A236 (= A234), T238 (= T236), A259 (= A257), D260 (= D258), C297 (= C295), F403 (= F397)
Sites not aligning to the query:
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)
24% identity, 62% coverage: 7:429/681 of query aligns to 21:433/505 of 4neaA
- active site: N166 (= N158), K189 (= K181), E264 (= E256), C298 (= C295), E399 (= E395)
- binding nicotinamide-adenine-dinucleotide: P164 (≠ A156), K189 (= K181), E192 (≠ T184), G222 (≠ A215), G226 (= G216), G242 (= G232), G243 (≠ S233), T246 (= T236), H249 (≠ Q239), I250 (≠ V242), C298 (= C295), E399 (= E395), F401 (= F397)
Sites not aligning to the query:
3b4wA Crystal structure of mycobacterium tuberculosis aldehyde dehydrogenase complexed with NAD+
25% identity, 64% coverage: 63:499/681 of query aligns to 68:475/483 of 3b4wA
- active site: N154 (= N158), K177 (= K181), E251 (= E256), C285 (= C295), E384 (= E395), E460 (≠ A478)
- binding nicotinamide-adenine-dinucleotide: I150 (= I154), V151 (≠ N155), W153 (≠ F157), N154 (= N158), K177 (= K181), I210 (vs. gap), G213 (= G216), T228 (= T231), G229 (= G232), S230 (= S233), V233 (≠ T236), E236 (≠ Q239), E251 (= E256), L252 (≠ A257), C285 (= C295), E384 (= E395), F386 (= F397)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
27% identity, 64% coverage: 48:484/681 of query aligns to 50:468/477 of 2opxA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C295), E381 (= E395), A458 (≠ G474)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ I104), F152 (= F159), N284 (≠ T296), F312 (≠ V324), G313 (= G325), R318 (≠ E330), D320 (vs. gap), I321 (≠ V332), A322 (≠ K333), Y362 (≠ F374), F440 (≠ S456), F440 (≠ S456), E441 (≠ S457)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
26% identity, 70% coverage: 6:479/681 of query aligns to 12:463/481 of 3jz4A
- active site: N156 (= N158), K179 (= K181), E254 (= E256), C288 (= C295), E385 (= E395), E462 (≠ A478)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (≠ A156), W155 (≠ F157), K179 (= K181), A181 (= A183), S182 (≠ T184), A212 (= A215), G216 (≠ L219), G232 (= G232), S233 (= S233), I236 (≠ T236), C288 (= C295), K338 (≠ D345), E385 (= E395), F387 (= F397)
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)
27% identity, 64% coverage: 48:484/681 of query aligns to 50:468/477 of 2impA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C295), E381 (= E395), A458 (≠ G474)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I154), L148 (≠ N155), P149 (≠ A156), W150 (≠ F157), K174 (= K181), E177 (≠ T184), F178 (≠ A185), G207 (vs. gap), G211 (= G216), Q212 (≠ D217), S228 (= S233), A231 (≠ T236), K234 (≠ Q239), R334 (≠ D345)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
27% identity, 64% coverage: 48:484/681 of query aligns to 50:468/477 of 2iluA
- active site: N151 (= N158), K174 (= K181), E249 (= E256), C283 (= C295), E381 (= E395), A458 (≠ G474)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I154), L148 (≠ N155), P149 (≠ A156), W150 (≠ F157), K174 (= K181), S176 (≠ A183), E177 (≠ T184), R206 (vs. gap), G207 (vs. gap), G211 (= G216), Q212 (≠ D217), S228 (= S233), A231 (≠ T236), K234 (≠ Q239), I235 (≠ L240), N328 (= N339), R334 (≠ D345), F383 (= F397)
P25526 Succinate-semialdehyde dehydrogenase [NADP(+)] GabD; SSDH; Glutarate-semialdehyde dehydrogenase; EC 1.2.1.79; EC 1.2.1.- from Escherichia coli (strain K12) (see paper)
26% identity, 70% coverage: 6:479/681 of query aligns to 13:464/482 of P25526
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)
26% identity, 64% coverage: 48:484/681 of query aligns to 52:470/479 of P25553
- L150 (≠ N155) binding
- R161 (≠ E166) binding
- KPSE 176:179 (≠ KPAT 181:184) binding
- F180 (≠ A185) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D217) binding
- S230 (= S233) binding
- E251 (= E256) binding
- N286 (≠ T296) 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 (≠ D345) binding
- E443 (≠ S457) binding
- H449 (= H463) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4pxnA Structure of zm aldh7 in complex with NAD (see paper)
26% identity, 51% coverage: 149:496/681 of query aligns to 152:484/498 of 4pxnA
- active site: N161 (= N158), K184 (= K181), E262 (= E256), C296 (= C295), E392 (= E395), E472 (= E483)
- binding nicotinamide-adenine-dinucleotide: I157 (= I154), T158 (≠ N155), A159 (= A156), F160 (= F157), N161 (= N158), K184 (= K181), T221 (≠ A215), G224 (= G216), Q225 (≠ D217), F238 (= F230), T239 (= T231), G240 (= G232), S241 (= S233), A244 (≠ T236), V248 (= V242), E262 (= E256), L263 (≠ A257), S264 (≠ D258), C296 (= C295), E392 (= E395), F394 (= F397), F461 (≠ H472)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
28% identity, 70% coverage: 21:500/681 of query aligns to 25:479/489 of 4cazA
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C295), E386 (= E395), E463 (= E483)
- binding [[(2R,3S,4R,5R)-5-[(3R)-3-aminocarbonyl-3,4-dihydro-2H-pyridin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanidyl-phosphoryl] [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl phosphate: I148 (= I154), G149 (≠ N155), W151 (≠ F157), N152 (= N158), K175 (= K181), E178 (≠ T184), G208 (≠ A215), G212 (≠ L219), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ S233), T232 (= T236), V236 (= V242), E251 (= E256), L252 (≠ A257), C285 (= C295), E386 (= E395), F388 (= F397)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
28% identity, 70% coverage: 21:500/681 of query aligns to 25:479/489 of 2woxA
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C295), E386 (= E395), E463 (= E483)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I154), G149 (≠ N155), W151 (≠ F157), N152 (= N158), K175 (= K181), S177 (≠ A183), E178 (≠ T184), G208 (≠ A215), G212 (≠ L219), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ S233), T232 (= T236), V236 (= V242), E251 (= E256), L252 (≠ A257), C285 (= C295), E386 (= E395), F388 (= F397)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
28% identity, 70% coverage: 21:500/681 of query aligns to 25:479/489 of 2wmeA
- active site: N152 (= N158), K175 (= K181), E251 (= E256), C285 (= C295), E386 (= E395), E463 (= E483)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ N155), W151 (≠ F157), K175 (= K181), S177 (≠ A183), E178 (≠ T184), G208 (≠ A215), G212 (≠ L219), F226 (= F230), G228 (= G232), G229 (≠ S233), T232 (= T236), V236 (= V242)
Q9HTJ1 NAD/NADP-dependent betaine aldehyde dehydrogenase; BADH; EC 1.2.1.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
28% identity, 70% coverage: 21:500/681 of query aligns to 26:480/490 of Q9HTJ1
- GAWN 150:153 (≠ NAFN 155:158) binding
- K162 (= K167) active site, Charge relay system
- KPSE 176:179 (≠ KPAT 181:184) binding
- G209 (≠ A215) binding
- GTST 230:233 (≠ SART 233:236) binding
- E252 (= E256) active site, Proton acceptor
- C286 (= C295) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E395) binding
- E464 (= E483) active site, Charge relay system
8hapB Crystal structure of thermostable acetaldehyde dehydrogenase from hyperthermophilic archaeon sulfolobus tokodaii (see paper)
26% identity, 60% coverage: 51:456/681 of query aligns to 34:426/466 of 8hapB
- binding 2'-monophosphoadenosine-5'-diphosphate: I136 (= I154), L137 (≠ N155), F139 (= F157), K163 (= K181), S165 (≠ A183), I166 (≠ T184), S196 (≠ A215), G200 (≠ L219), G216 (= G232), S217 (= S233), T220 (= T236), I224 (≠ V242)
Query Sequence
>BWI76_RS13085 FitnessBrowser__Koxy:BWI76_RS13085
MQQLASYLSGTWQTGRGHARTIHHAISGDALWEVTSAGLDMAQARRFAIERGGKALQAMT
FIERSAMLKAVARHLLEQKAALYAISAETGATRSDSWVDIEGGIGTLFTYAGLGSRELPD
DTLWPEDELIPLSKQGGFAARHVLTSKSGVAVHINAFNFPCWGMLEKLAPTWLAGMPAII
KPATATAQLTQAMVKMIVDSGLVPEGAISLICGGAGDLLDHLDSQDVVTFTGSARTGQQL
RVHPNLVAKSIPFTMEADSLNCCVLGDDVTPEQPEFALFIREVVREMTAKAGQKCTAIRR
IIVPQAQVKAVSDALIARLQNVVVGDPAQEGVKMGALVNYEQRQDVQDNVNRLVAAGCDV
LLGGQADLRAAGAFFPPTLLFCPQPDETPAVHAIEAFGPVATLMPYQNIEHAMSLARAGE
GSLAGTLVTASGELARAFILGAARTHGRIQILNESSSAESTGHGSPLPQLVHGGPGRAGG
GEELGGLRAVKHYMQRTAIQGSPTMLAAIGQQWVRGAEVVEDRIHPFRKYFEEIQPGDSL
LTPRRTLTEADIVNFACLSGDHFYAHMDKIAAAESIFGERVVHGYFLISAAAGLFVDAGV
GPVIANYGMENLRFIEPVKPGDTIQVRLTCKRKTVKRQRSAEEKATGVVEWAVEIFNQHQ
QAVALYSILTLVARQQGDFAG
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