SitesBLAST
Comparing WP_015798620.1 NCBI__GCF_000023265.1:WP_015798620.1 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)
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
49% identity, 96% coverage: 18:486/487 of query aligns to 14:481/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E259), C288 (= C293), E385 (= E390), E462 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (= A185), S182 (≠ E186), A212 (≠ P217), G216 (≠ S221), G232 (= G237), S233 (= S238), I236 (≠ V241), C288 (= C293), K338 (= K343), E385 (= E390), F387 (= F392)
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)
49% identity, 96% coverage: 18:486/487 of query aligns to 15:482/482 of P25526
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
49% identity, 96% coverage: 17:484/487 of query aligns to 13:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ P217), K213 (≠ G218), F230 (= F235), T231 (= T236), G232 (= G237), S233 (= S238), V236 (= V241), W239 (≠ L244), G256 (= G261)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
47% identity, 95% coverage: 22:484/487 of query aligns to 36:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I156), A171 (≠ T157), P172 (= P158), W173 (= W159), K197 (= K183), A230 (≠ H216), F248 (= F235), G250 (= G237), S251 (= S238), V254 (= V241), M257 (≠ L244), L273 (= L260), C306 (= C293), K356 (= K343), E403 (= E390), F405 (= F392)
P51649 Succinate-semialdehyde dehydrogenase, mitochondrial; Aldehyde dehydrogenase family 5 member A1; NAD(+)-dependent succinic semialdehyde dehydrogenase; EC 1.2.1.24 from Homo sapiens (Human) (see 5 papers)
47% identity, 97% coverage: 14:483/487 of query aligns to 61:531/535 of P51649
- C93 (≠ A48) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G131) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ V135) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P137) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R168) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C178) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 183:186) binding NAD(+)
- T233 (= T188) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ T192) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S221) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEVG 237:242) binding NAD(+)
- R334 (= R287) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N288) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C293) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S295) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ R324) natural variant: N -> S
- P382 (= P334) to L: in SSADHD; 2% of activity
- V406 (≠ L358) to I: in dbSNP:rs143741652
- G409 (= G361) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S450) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
46% identity, 97% coverage: 14:483/487 of query aligns to 11:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
46% identity, 97% coverage: 14:483/487 of query aligns to 11:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 96% coverage: 14:480/487 of query aligns to 5:470/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E259), C283 (= C293), E380 (= E390), E457 (= E467)
- binding glycerol: D15 (≠ E24), A16 (= A25), A17 (= A26), G19 (= G28)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (= P217), A208 (≠ G218), S211 (= S221), G227 (= G237), S228 (= S238), V231 (= V241), R329 (≠ D339), R330 (≠ A340), E380 (= E390), F382 (= F392)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 96% coverage: 14:480/487 of query aligns to 5:470/476 of 5x5tA
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)
38% identity, 97% coverage: 16:487/487 of query aligns to 10:487/497 of P17202
- I28 (≠ E34) binding K(+)
- D96 (≠ E100) binding K(+)
- SPW 156:158 (≠ TPW 157:159) binding NAD(+)
- Y160 (≠ F161) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ R168) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KPAE 183:186) binding NAD(+)
- L186 (≠ Q187) binding K(+)
- SSAT 236:239 (≠ STEV 238:241) binding NAD(+)
- V251 (≠ L253) binding in other chain
- L258 (= L260) binding NAD(+)
- W285 (≠ R287) mutation to A: Decreases binding affinity for betaine aldehyde.
- E390 (= E390) binding NAD(+)
- A441 (≠ M441) mutation to I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- C450 (≠ S450) mutation to S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- W456 (≠ F456) binding NAD(+); mutation to A: Decreases binding affinity for betaine aldehyde.
- K460 (= K460) binding K(+)
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
38% identity, 97% coverage: 16:487/487 of query aligns to 8:485/495 of 4v37A
- active site: N157 (= N160), K180 (= K183), E255 (= E259), A289 (≠ C293), E388 (= E390), E465 (= E467)
- binding 3-aminopropan-1-ol: C448 (≠ S450), W454 (≠ F456)
- binding nicotinamide-adenine-dinucleotide: I153 (= I156), S154 (≠ T157), P155 (= P158), W156 (= W159), N157 (= N160), M162 (= M165), K180 (= K183), S182 (≠ A185), E183 (= E186), G213 (= G218), G217 (≠ D222), A218 (= A223), T232 (= T236), G233 (= G237), S234 (= S238), T237 (≠ V241), E255 (= E259), L256 (= L260), A289 (≠ C293), E388 (= E390), F390 (= F392)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
39% identity, 97% coverage: 16:486/487 of query aligns to 8:482/489 of 4cazA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C293), E386 (= E390), E463 (= E467)
- 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 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), E178 (= E186), G208 (≠ H216), G212 (≠ S221), F226 (= F235), T227 (= T236), G228 (= G237), G229 (≠ S238), T232 (≠ V241), V236 (≠ L245), E251 (= E259), L252 (= L260), C285 (= C293), E386 (= E390), F388 (= F392)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
39% identity, 97% coverage: 16:486/487 of query aligns to 8:482/489 of 2woxA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C293), E386 (= E390), E463 (= E467)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I156), G149 (≠ T157), W151 (= W159), N152 (= N160), K175 (= K183), S177 (≠ A185), E178 (= E186), G208 (≠ H216), G212 (≠ S221), F226 (= F235), T227 (= T236), G228 (= G237), G229 (≠ S238), T232 (≠ V241), V236 (≠ L245), E251 (= E259), L252 (= L260), C285 (= C293), E386 (= E390), F388 (= F392)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 97% coverage: 16:486/487 of query aligns to 8:482/489 of 2wmeA
- active site: N152 (= N160), K175 (= K183), E251 (= E259), C285 (= C293), E386 (= E390), E463 (= E467)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T157), W151 (= W159), K175 (= K183), S177 (≠ A185), E178 (= E186), G208 (≠ H216), G212 (≠ S221), F226 (= F235), G228 (= G237), G229 (≠ S238), T232 (≠ V241), V236 (≠ L245)
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)
39% identity, 97% coverage: 16:486/487 of query aligns to 9:483/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 157:160) binding NADPH
- K162 (= K169) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 183:186) binding NADPH
- G209 (≠ H216) binding NADPH
- GTST 230:233 (≠ STEV 238:241) binding NADPH
- E252 (= E259) active site, Proton acceptor
- C286 (= C293) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E390) binding NADPH
- E464 (= E467) active site, Charge relay system
O24174 Betaine aldehyde dehydrogenase 1; OsBADH1; EC 1.2.1.8 from Oryza sativa subsp. japonica (Rice) (see paper)
38% identity, 96% coverage: 15:480/487 of query aligns to 11:485/505 of O24174
- N164 (= N160) 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 (≠ R168) 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.
7radA Crystal structure analysis of aldh1b1
39% identity, 97% coverage: 16:486/487 of query aligns to 15:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (≠ T157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (= E186), G218 (= G218), G222 (≠ D222), A223 (= A223), T237 (= T236), G238 (= G237), S239 (= S238), V242 (= V241), E261 (= E259), L262 (= L260), C295 (= C293), E392 (= E390), F394 (= F392)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (vs. gap), E117 (≠ Y114), F163 (= F161), E285 (≠ F283), F289 (≠ R287), N450 (≠ L448), V452 (≠ S450)
7mjdA Crystal structure analysis of aldh1b1
39% identity, 97% coverage: 16:486/487 of query aligns to 15:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (≠ T157), P160 (= P158), W161 (= W159), N162 (= N160), M167 (= M165), K185 (= K183), E188 (= E186), G218 (= G218), G222 (≠ D222), F236 (= F235), T237 (= T236), G238 (= G237), S239 (= S238), V242 (= V241), E261 (= E259), L262 (= L260), C295 (= C293), E392 (= E390), F394 (= F392)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ Y114), E285 (≠ F283), F289 (≠ R287), N450 (≠ L448), V452 (≠ S450)
7mjcA Crystal structure analysis of aldh1b1
39% identity, 97% coverage: 16:486/487 of query aligns to 15:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I156), I159 (≠ T157), P160 (= P158), W161 (= W159), N162 (= N160), K185 (= K183), E188 (= E186), G218 (= G218), G222 (≠ D222), T237 (= T236), G238 (= G237), S239 (= S238), V242 (= V241), E261 (= E259), L262 (= L260), C295 (= C293), E392 (= E390), F394 (= F392)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
41% identity, 97% coverage: 16:486/487 of query aligns to 8:481/489 of 6wsbA
- active site: N152 (= N160), E250 (= E259), C284 (= C293), E462 (= E467)
- binding nicotinamide-adenine-dinucleotide: I148 (= I156), G149 (≠ T157), A150 (≠ P158), W151 (= W159), N152 (= N160), K175 (= K183), E178 (= E186), G208 (= G218), G211 (≠ S221), A212 (≠ D222), F225 (= F235), T226 (= T236), G227 (= G237), G228 (≠ S238), T231 (≠ V241), V235 (≠ L245), E250 (= E259), L251 (= L260), G252 (= G261), C284 (= C293), E385 (= E390), F387 (= F392)
Query Sequence
>WP_015798620.1 NCBI__GCF_000023265.1:WP_015798620.1
MEERERAVVRTVPTGLYVDGAWREAADGGRFDVEDPATGEVIASVADATVDDARQAVDAA
VAHQEAWAHSAPRERAEILRRAFEAVMAAQDDLALLMTLEMGKPVAESRGEVAYAAEFLR
WFSEEAVRVHGDFYVSPDATTRVLTTRQPVGPSYLITPWNFPLAMGTRKIAPALAAGCTV
IVKPAEQTPLCTLALASIFERVGLPPGVLNVVTTSHPGPISDAIIGHPGLRKLSFTGSTE
VGSLLMRKASSGLLRLSMELGGNAPLIVFEDADLDKAVAGAVFAKMRNGGEACTSANRIL
VHESLADTFSERLATALASLKVARGTEPDASVGPLIDADALAKVSGLVEDAVAAGASLVT
GGERRGDRGYFFSPTVLRDVPPTARVFREEIFGPVAPVYRFDDDDEAIRLANDTTYGLVG
YIFTESLSRAVRTIEALETGMVGVNQGLVSNAAAPFGGVKRSGFGREGGFEGIHEYLNVK
YAALNLS
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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