SitesBLAST
Comparing WP_009763662.1 NCBI__GCF_000262405.1:WP_009763662.1 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)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
81% identity, 97% coverage: 15:495/495 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I165), T153 (= T166), P154 (= P167), K179 (= K192), A212 (= A225), K213 (= K226), F230 (= F243), T231 (= T244), G232 (= G245), S233 (= S246), V236 (= V249), W239 (= W252), G256 (= G269)
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)
63% identity, 97% coverage: 13:490/495 of query aligns to 1:478/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
63% identity, 96% coverage: 15:490/495 of query aligns to 2:477/481 of 3jz4A
- active site: N156 (= N169), K179 (= K192), E254 (= E267), C288 (= C301), E385 (= E398), E462 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P167), W155 (= W168), K179 (= K192), A181 (= A194), S182 (≠ A195), A212 (= A225), G216 (= G229), G232 (= G245), S233 (= S246), I236 (≠ V249), C288 (= C301), K338 (= K351), E385 (= E398), F387 (= F400)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
52% identity, 98% coverage: 12:495/495 of query aligns to 17:500/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I165), A171 (≠ T166), P172 (= P167), W173 (= W168), K197 (= K192), A230 (= A225), F248 (= F243), G250 (= G245), S251 (= S246), V254 (= V249), M257 (≠ W252), L273 (= L268), C306 (= C301), K356 (= K351), E403 (= E398), F405 (= F400)
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)
54% identity, 96% coverage: 19:495/495 of query aligns to 57:535/535 of P51649
- C93 (≠ L57) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G140) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P144) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ A146) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R177) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C187) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAA 192:195) binding NAD(+)
- T233 (= T197) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A201) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S219) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G229) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTGVG 245:250) binding NAD(+)
- R334 (= R295) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N296) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C301) modified: Disulfide link with 342, In inhibited form
- C342 (= C303) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ R332) natural variant: N -> S
- P382 (= P342) to L: in SSADHD; 2% of activity
- V406 (≠ L366) to I: in dbSNP:rs143741652
- G409 (= G369) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A458) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (≠ A493) to R: in SSADHD; <1% of activity; dbSNP:rs72552284
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
54% identity, 96% coverage: 19:495/495 of query aligns to 7:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
54% identity, 96% coverage: 19:495/495 of query aligns to 7:485/485 of 2w8qA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
40% identity, 95% coverage: 24:491/495 of query aligns to 3:476/477 of 6j76A
- active site: N148 (= N169), E246 (= E267), C280 (= C301), E458 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I165), T145 (= T166), A146 (≠ P167), W147 (= W168), N148 (= N169), K171 (= K192), T173 (≠ A194), S174 (≠ A195), G204 (≠ A225), G208 (= G229), T223 (= T244), G224 (= G245), S225 (= S246), A228 (≠ V249), S231 (≠ W252), I232 (≠ L253), E246 (= E267), L247 (= L268), C280 (= C301), E381 (= E398), F383 (= F400), H447 (≠ F464)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 95% coverage: 24:492/495 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N169), K174 (= K192), E249 (= E267), C283 (= C301), E380 (= E398), E457 (= E475)
- binding glycerol: D15 (= D33), A16 (= A34), A17 (≠ P35), G19 (= G37)
- binding nicotinamide-adenine-dinucleotide: P149 (= P167), P207 (≠ A225), A208 (≠ K226), S211 (≠ G229), G227 (= G245), S228 (= S246), V231 (= V249), R329 (= R347), R330 (≠ A348), E380 (= E398), F382 (= F400)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 95% coverage: 24:492/495 of query aligns to 6:474/476 of 5x5tA
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
37% identity, 95% coverage: 26:494/495 of query aligns to 6:479/494 of 5izdA
- active site: N149 (= N169), K172 (= K192), E247 (= E267), C281 (= C301), E381 (= E398), E458 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ I165), T146 (= T166), W148 (= W168), K172 (= K192), P173 (= P193), S174 (≠ A194), S175 (≠ A195), R204 (≠ E224), G205 (≠ A225), G209 (= G229), D210 (≠ E230), G225 (= G245), S226 (= S246), T229 (≠ V249)
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)
35% identity, 94% coverage: 26:492/495 of query aligns to 10:477/479 of P25553
- L150 (≠ T166) binding NAD(+)
- R161 (= R177) binding (S)-lactate
- KPSE 176:179 (≠ KPAA 192:195) binding NAD(+)
- F180 (≠ Q196) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ E230) binding NAD(+)
- S230 (= S246) binding NAD(+)
- E251 (= E267) binding (S)-lactate
- N286 (≠ V302) binding (S)-lactate; 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 (≠ K351) binding NAD(+)
- E443 (≠ A458) binding (S)-lactate
- H449 (≠ F464) binding (S)-lactate
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)
35% identity, 94% coverage: 26:492/495 of query aligns to 8:475/477 of 2impA
- active site: N151 (= N169), K174 (= K192), E249 (= E267), C283 (= C301), E381 (= E398), A458 (≠ E475)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I165), L148 (≠ T166), P149 (= P167), W150 (= W168), K174 (= K192), E177 (≠ A195), F178 (≠ Q196), G207 (≠ A225), G211 (= G229), Q212 (≠ E230), S228 (= S246), A231 (≠ V249), K234 (≠ W252), R334 (≠ K351)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
35% identity, 94% coverage: 26:492/495 of query aligns to 8:475/477 of 2iluA
- active site: N151 (= N169), K174 (= K192), E249 (= E267), C283 (= C301), E381 (= E398), A458 (≠ E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I165), L148 (≠ T166), P149 (= P167), W150 (= W168), K174 (= K192), S176 (≠ A194), E177 (≠ A195), R206 (≠ E224), G207 (≠ A225), G211 (= G229), Q212 (≠ E230), S228 (= S246), A231 (≠ V249), K234 (≠ W252), I235 (≠ L253), N328 (≠ D345), R334 (≠ K351), F383 (= F400)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
35% identity, 94% coverage: 26:492/495 of query aligns to 8:475/477 of 2opxA
- active site: N151 (= N169), K174 (= K192), E249 (= E267), C283 (= C301), E381 (= E398), A458 (≠ E475)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ S123), F152 (= F170), N284 (≠ V302), F312 (≠ L330), G313 (= G331), R318 (≠ A336), D320 (vs. gap), I321 (≠ V338), A322 (≠ T339), Y362 (≠ F379), F440 (≠ L457), F440 (≠ L457), E441 (≠ A458)
5ek6A Thermostable aldehyde dehydrogenase from pyrobaculum sp. 1860 complexed with NADP and isobutyraldehyde (see paper)
37% identity, 94% coverage: 26:489/495 of query aligns to 4:463/482 of 5ek6A
- active site: N147 (= N169), K170 (= K192), E245 (= E267), C279 (= C301), E374 (= E398), E452 (= E475)
- binding 2-methylpropanal: I152 (≠ M174), K155 (≠ R177), T222 (= T244), E245 (= E267), F441 (= F464)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I143 (= I165), T144 (= T166), W146 (= W168), N147 (= N169), I152 (≠ M174), K170 (= K192), A172 (= A194), S173 (≠ A195), P202 (≠ E224), G203 (≠ A225), G207 (= G229), F221 (= F243), T222 (= T244), G223 (= G245), E224 (≠ S246), T227 (≠ V249), I231 (≠ L253), E245 (= E267), L246 (= L268), C279 (= C301), E374 (= E398)
4h73A Thermostable aldehyde dehydrogenase from pyrobaculum sp. Complexed with NADP+
37% identity, 94% coverage: 26:489/495 of query aligns to 4:463/482 of 4h73A
- active site: N147 (= N169), K170 (= K192), E245 (= E267), C279 (= C301), E374 (= E398), E452 (= E475)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I143 (= I165), T144 (= T166), P145 (= P167), W146 (= W168), K170 (= K192), A172 (= A194), S173 (≠ A195), G203 (≠ A225), G207 (= G229), F221 (= F243), G223 (= G245), E224 (≠ S246), T227 (≠ V249)
5ekcE Thermostable aldehyde dehydrogenase from pyrobaculum sp.1860 complexed with NADP+
36% identity, 96% coverage: 17:489/495 of query aligns to 2:470/490 of 5ekcE
- active site: N154 (= N169), K177 (= K192), E252 (= E267), C286 (= C301), E381 (= E398), E459 (= E475)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I150 (= I165), T151 (= T166), P152 (= P167), W153 (= W168), K177 (= K192), S180 (≠ A195), G210 (≠ A225), G214 (= G229), F228 (= F243), G230 (= G245), E231 (≠ S246), T234 (≠ V249), N331 (≠ D345), R333 (= R347), Q334 (≠ A348)
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)
35% identity, 95% coverage: 21:490/495 of query aligns to 16:491/505 of 4neaA
- active site: N166 (= N169), K189 (= K192), E264 (= E267), C298 (= C301), E399 (= E398), E476 (= E475)
- binding nicotinamide-adenine-dinucleotide: P164 (= P167), K189 (= K192), E192 (≠ A195), G222 (≠ A225), G226 (= G229), G242 (= G245), G243 (≠ S246), T246 (≠ V249), H249 (≠ W252), I250 (≠ L253), C298 (= C301), E399 (= E398), F401 (= F400)
Q56YU0 Aldehyde dehydrogenase family 2 member C4; ALDH1a; Protein REDUCED EPIDERMAL FLUORESCENCE 1; EC 1.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 96% coverage: 15:490/495 of query aligns to 12:491/501 of Q56YU0
- G152 (≠ I152) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V415) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
Query Sequence
>WP_009763662.1 NCBI__GCF_000262405.1:WP_009763662.1
MTVHAKPVDRRVVDLKDPSLLVGQAYVAGEWIDAPDGKTIPVTDPFDGALILEVPDLGPD
AARRAIDKAHAVQKDWAKRTAKERSAILRRWYDLIVANADDLALILTTEQGKPLAEAKGE
VISNAAYIEWFAEEAKRIDGDVIPGATPSQRIVVLKQPVGVCAAITPWNFPNGMITRKVG
PALAAGCTMVLKPAAQTPLSALALAVLAERAGVPKGAFSVVTGEAKPIGEEFCHNPKVAK
ITFTGSTGVGRWLMKEAADGIKRLSLELGGNAPFIVFDDADLDAAVEGAMASKFRNAGQT
CVCANRIYVQEGVAEAFAEKLAAKAGSLKLGRGTDAGVTMGPLIDDRAVAKMEEHVRDVL
DKGGKLLVGGKRSDLGSTFFEPTVMTGVTQAMKVTKEETFAPLAPIITFKDEADVIAMAN
DSEFGLASYFYAKDMARVWRVAEALESGMVGVNTPALANEMAPFGGVKQSGLGREGSKYG
IEGFLEIKYINLAGL
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