SitesBLAST

P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
29% identity, 40% coverage: 115:282/423 of query aligns to 145:313/497 of P17202

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SPW 156:158 (≠ SRP 128:130) binding
Y160 (≠ V132) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
W167 (≠ L139) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
KPSE 182:185 (≠ -HSN 157:159) binding
L186 (≠ R160) binding
SSAT 236:239 (≠ GRGL 209:212) binding
V251 (vs. gap) binding in other chain
L258 (= L228) binding
W285 (≠ T254) mutation to A: Decreases binding affinity for betaine aldehyde.

Sites not aligning to the query:

28 binding
96 binding
390 binding
441 A→I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
450 C→S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
460 binding

4yweA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
30% identity, 42% coverage: 108:284/423 of query aligns to 126:303/476 of 4yweA

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active site: N147 (≠ R129), K170 (≠ R150), E245 (≠ H227), C279 (= C260)
binding calcium ion: D174 (≠ E154)

Sites not aligning to the query:

4jz6A Crystal structure of a salicylaldehyde dehydrogenase from pseudomonas putida g7 complexed with salicylaldehyde (see paper)
28% identity, 41% coverage: 115:287/423 of query aligns to 136:308/484 of 4jz6A

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active site: N150 (≠ R129), K173 (≠ R150), E251 (≠ H227), C285 (= C260)
binding salicylaldehyde: G151 (≠ P130), V154 (≠ T133), R247 (≠ P223), C248 (≠ V224), I284 (= I259), C285 (= C260), M286 (≠ G261)

Sites not aligning to the query:

active site: 380, 458
binding salicylaldehyde: 97, 447, 455

O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 39% coverage: 115:277/423 of query aligns to 150:313/505 of O24174

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N164 (≠ R129) mutation to A: Slightly reduced affinity for NAD, 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald), but 2-fold decrease in catalytic efficiency.
W172 (≠ A137) mutation to A: Slightly reduced affinity for NAD, enhanced affinity for both betaine aldehyde (Bet-ald) (10-fold) and gamma-4-aminobutyraldehyde (GAB-ald) (2-fold).; mutation to F: Slightly reduced affinity for NAD, but 6-fold enhanced affinity for both gamma-4-aminobutyraldehyde (GAB-ald) and betaine aldehyde (Bet-ald) and 2-fold increase in catalytic efficiency towards GAB-ald.

4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
29% identity, 40% coverage: 115:282/423 of query aligns to 143:311/495 of 4v37A

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4v37A

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active site: N157 (= N131), K180 (vs. gap), E255 (≠ H227), A289 (≠ C260)
binding nicotinamide-adenine-dinucleotide: I153 (= I125), S154 (= S128), P155 (≠ R129), W156 (≠ P130), N157 (= N131), M162 (≠ A136), K180 (vs. gap), S182 (= S158), E183 (≠ N159), G213 (≠ D187), G217 (≠ V191), A218 (≠ G192), T232 (≠ R207), G233 (= G208), S234 (≠ G209), T237 (≠ L212), E255 (≠ H227), L256 (= L228), A289 (≠ C260)

Sites not aligning to the query:

active site: 388, 465
binding 3-aminopropan-1-ol: 448, 454
binding nicotinamide-adenine-dinucleotide: 388, 390

3rhhD Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from bacillus halodurans c-125 complexed with NADP
30% identity, 41% coverage: 116:287/423 of query aligns to 142:311/480 of 3rhhD

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active site: N155 (≠ R129), K178 (≠ R150), E251 (≠ H227), C285 (= C260)
binding nadp nicotinamide-adenine-dinucleotide phosphate: I151 (= I125), P153 (≠ E127), F154 (≠ S128), K178 (≠ R150), P179 (≠ G151), A180 (≠ G152), T181 (≠ S153), G211 (≠ E189), G215 (vs. gap), D216 (≠ G192), F229 (≠ P206), G231 (= G208), G232 (= G209), T235 (≠ L212)

Sites not aligning to the query:

active site: 378, 456

Query Sequence

>PP_4811 FitnessBrowser__Putida:PP_4811
MTESVLDYMTRLGRAAREASRVIGRASTAQKNRALQAAADALDAARAELTAANELDLAAG
RASGLEPALLDRLALTPARIDGMITGLRQVASLPDPVGAIRDMSYRPSGIQVGKMRTPLG
VIGIIYESRPNVTIDAASLCLKSGNATILRGGSEAIHSNRAIATCIQRGLAEAGLPAAVV
QVVETTDREAVGALISMPEFVDVIVPRGGRGLIERISRDARVPVIKHLDGICHIYVSQHA
DLDKAWNVAFNAKTYRYGICGAMETLLVDQQVAERFLPEMARRFVEKGVELRGCERTQAI
ISAKPATEADWHTEYLDAILSIRVVDGLNQAIEHINHYGSHHTDSIISEHQGEARQFMAE
VDSASVMLNTPTCFADGFEYGLGAEIGISTDKLHARGPVGLEGLTCEKYVVIGDGQLRGQ
GSC

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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