SitesBLAST

E149 (≠ S154) mutation to D: Small effect on NAD(+) interaction, but 40% loss of efficiency. Ability to use NADP(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to N: Ability to use NADP(+) and 33% decreased efficiency with NAD(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to Q: Loss of specificity for NAD(+) and loss of 25% efficiency. 15% efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200.; mutation to T: Loss of specificity and increased NADP(+) binding. Decreased catalytic efficiency. Loss of cofactor specificity and same lower efficiency with both; when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with R-178 and V-200.
V178 (≠ T186) mutation to R: Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and V-200.
I200 (= I214) mutation to G: Changed coenzyme preference from NAD(+) to NADP(+), but impaired affinities for both cofactors. No effect on the interaction with the substrate. Impaired affinities for both cofactors and decreased catalytic efficiencies; when associated with D-149, Q-149, N-149 or T-149.; mutation to V: Also able to use NADP(+) as coenzyme, but no effect on the interaction with the substrate. 15% efficiency with NAD(+); when associated with Q-149. 70% loss of efficiency with NAD(+); when associated with D-149 or N-149. Loss of cofactor specificity and same lower efficiency with both; when associated with T-149. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and R-178.
C247 (≠ A250) mutation to S: No effect on solubility, but 10% loss of activity.
C253 (vs. gap) mutation to S: No effect on solubility, but loss of activity.

Sites not aligning to the query:

45 C→S: Decreased solubility, loss of dimerization and strongly decreased activity.

4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 40% coverage: 81:250/426 of query aligns to 105:273/489 of 4cazA

query
sites
4cazA

I

I

D

V

T

T

M

G

A

A

A

D

G

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L

L

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E

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Y

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A

A

A

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L

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G

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E

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D

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N

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L

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G

G

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I

I

D

F

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D

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D

D

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L

D

D

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A

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A

active site: N152 (≠ S129), K175 (≠ R151), E251 (vs. gap)
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 (= I125), G149 (≠ I126), W151 (≠ E128), N152 (≠ S129), K175 (≠ R151), E178 (= E155), G208 (≠ D188), G212 (= G193), F226 (≠ P207), T227 (≠ R208), G228 (= G209), G229 (= G210), T232 (≠ L213), V236 (≠ L217), E251 (vs. gap), L252 (= L229)

Sites not aligning to the query:

2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 40% coverage: 81:250/426 of query aligns to 105:273/489 of 2woxA

query
sites
2woxA

I

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G

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N

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x
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L

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D

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A

active site: N152 (≠ S129), K175 (≠ R151), E251 (vs. gap)
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I125), G149 (≠ I126), W151 (≠ E128), N152 (≠ S129), K175 (≠ R151), S177 (= S154), E178 (= E155), G208 (≠ D188), G212 (= G193), F226 (≠ P207), T227 (≠ R208), G228 (= G209), G229 (= G210), T232 (≠ L213), V236 (≠ L217), E251 (vs. gap), L252 (= L229)

Sites not aligning to the query:

active site: 285, 386, 463
binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: 285, 386, 388

2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 40% coverage: 81:250/426 of query aligns to 105:273/489 of 2wmeA

query
sites
2wmeA

I

I

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G

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N

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G

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T

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V

M

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K

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x
E

L

L

D

G

G

G

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I

I

D

F

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D

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A

D

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L

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A

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A

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I

A

A

active site: N152 (≠ S129), K175 (≠ R151), E251 (vs. gap)
binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ I126), W151 (≠ E128), K175 (≠ R151), S177 (= S154), E178 (= E155), G208 (≠ D188), G212 (= G193), F226 (≠ P207), G228 (= G209), G229 (= G210), T232 (≠ L213), V236 (≠ L217)

Sites not aligning to the query:

active site: 285, 386, 463

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)
34% identity, 38% coverage: 88:250/426 of query aligns to 113:274/490 of Q9HTJ1

query
sites
Q9HTJ1

L

L

E

E

Q

Y

I

Y

A

A

A

G

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L

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G

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N

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G

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x
E

L

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G

G

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I

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F

V

P

D

D

A

A

D

D

L

L

D

D

K

R

A

A

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A

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D

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A

A

GAWN 150:153 (≠ IYES 126:129) binding
K162 (≠ A137) active site, Charge relay system
KP-SE 176:179 (≠ RGGSE 151:155) binding
G209 (≠ D188) binding
GTST 230:233 (≠ GKSL 210:213) binding
E252 (vs. gap) active site, Proton acceptor

Sites not aligning to the query:

286 binding covalent; modified: Cysteine sulfenic acid (-SOH)
387 binding
464 active site, Charge relay system

Query Sequence

>RR42_RS17530 FitnessBrowser__Cup4G11:RR42_RS17530
MNELDLKQYMDRVGQQARAASRAMARASTADKNRALLTIAAAIRRDAAHLKAVNAGDVER
ARANGQDAAFIDRLTLSDKAIDTMAAGLEQIAALADPIGEISNMKFRPTGIQVGQMRVPL
GVIGIIYESRPNVTIDAAALCLKSGNATILRGGSEAIDSNTALAALVAEGLAAAGLPPEA
VQVISTTDRAAVGRLVTMTEYVDVIVPRGGKSLIARLMAEARVPMIKHLDGICHVYIDVD
ADLDKAVRVADNAKTQRYAPCNTMETLLVARAVAAAALPPLCRIYQEKGVELRVCAATRA
TLEAAGFTGLVDATEEDWRLEYLAPVLAIRTVAGLDEAIEHINTYGSAHTDSIITENYTT
GMRFLREVDSASVMINASTRFADGFEYGLGAEIGISNDKLHARGPVGLEGLTSLKYVVFG
HGEIRT

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