SitesBLAST
Comparing WP_029002104.1 NCBI__GCF_000430725.1:WP_029002104.1 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)
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)
55% identity, 99% coverage: 3:491/494 of query aligns to 1:481/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
55% identity, 99% coverage: 5:491/494 of query aligns to 2:480/481 of 3jz4A
- active site: N156 (= N160), K179 (= K183), E254 (= E261), C288 (= C295), E385 (= E396), E462 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P158), W155 (= W159), K179 (= K183), A181 (= A185), S182 (≠ E186), A212 (≠ R216), G216 (≠ V223), G232 (= G239), S233 (= S240), I236 (≠ V243), C288 (= C295), K338 (= K345), E385 (= E396), F387 (= F398)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
50% identity, 100% coverage: 3:494/494 of query aligns to 18:501/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (= I156), A171 (≠ T157), P172 (= P158), W173 (= W159), K197 (= K183), A230 (≠ T219), F248 (= F237), G250 (= G239), S251 (= S240), V254 (= V243), M257 (≠ H246), L273 (= L262), C306 (= C295), K356 (= K345), E403 (= E396), F405 (= F398)
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)
53% identity, 98% coverage: 10:493/494 of query aligns to 58:535/535 of P51649
- C93 (≠ S48) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G131) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P135) 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 (≠ S192) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N210) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ V223) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 239:244) binding NAD(+)
- R334 (= R289) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N290) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C295) modified: Disulfide link with 342, In inhibited form
- C342 (= C297) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P326) natural variant: N -> S
- P382 (= P336) to L: in SSADHD; 2% of activity
- V406 (= V360) to I: in dbSNP:rs143741652
- G409 (= G363) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A456) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- G533 (= G491) 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
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
52% identity, 99% coverage: 5:493/494 of query aligns to 2:482/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I156), T153 (= T157), P154 (= P158), K179 (= K183), A212 (≠ T219), K213 (≠ P220), F230 (= F237), T231 (= T238), G232 (= G239), S233 (= S240), V236 (= V243), W239 (≠ H246), G256 (= G263)
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
53% identity, 98% coverage: 10:493/494 of query aligns to 8:485/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
53% identity, 98% coverage: 10:493/494 of query aligns to 8:485/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
40% identity, 97% coverage: 13:489/494 of query aligns to 5:473/476 of 5x5uA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E380 (= E396), E457 (= E473)
- binding glycerol: D15 (= D23), A16 (= A24), A17 (≠ L25), G19 (≠ A27)
- binding nicotinamide-adenine-dinucleotide: P149 (= P158), P207 (= P220), A208 (= A221), S211 (≠ D224), G227 (= G239), S228 (= S240), V231 (= V243), R329 (= R341), R330 (≠ A342), E380 (= E396), F382 (= F398)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
40% identity, 97% coverage: 13:489/494 of query aligns to 5:473/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
38% identity, 96% coverage: 12:486/494 of query aligns to 1:471/477 of 6j76A
- active site: N148 (= N160), E246 (= E261), C280 (= C295), E458 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I156), T145 (= T157), A146 (≠ P158), W147 (= W159), N148 (= N160), K171 (= K183), T173 (≠ A185), S174 (≠ E186), G204 (≠ T219), G208 (≠ V223), T223 (= T238), G224 (= G239), S225 (= S240), A228 (≠ V243), S231 (≠ H246), I232 (≠ L247), E246 (= E261), L247 (= L262), C280 (= C295), E381 (= E396), F383 (= F398), H447 (≠ F462)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 95% coverage: 16:486/494 of query aligns to 8:471/477 of 2opxA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E381 (= E396), A458 (≠ E473)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F105 (≠ Y114), F152 (= F161), N284 (≠ V296), F312 (≠ V324), G313 (= G325), R318 (≠ N329), D320 (≠ T331), I321 (≠ S332), A322 (≠ Q333), Y362 (= Y377), F440 (≠ L455), F440 (≠ L455), E441 (≠ A456)
4go4A Crystal structure of pnpe in complex with nicotinamide adenine dinucleotide
38% identity, 96% coverage: 11:486/494 of query aligns to 1:471/487 of 4go4A
- active site: N149 (= N160), K172 (= K183), E247 (= E261), C281 (= C295), E381 (= E396), E458 (= E473)
- binding nicotinamide-adenine-dinucleotide: I145 (= I156), V146 (≠ T157), W148 (= W159), N149 (= N160), F154 (≠ M165), K172 (= K183), G205 (≠ R216), G209 (≠ P220), Q210 (≠ A221), F223 (= F237), T224 (= T238), G225 (= G239), S226 (= S240), T229 (≠ V243), E247 (= E261), G249 (= G263), C281 (= C295), E381 (= E396), F383 (= F398)
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)
38% identity, 95% coverage: 16:486/494 of query aligns to 10:473/479 of P25553
- L150 (≠ T157) binding NAD(+)
- R161 (= R168) binding (S)-lactate
- KPSE 176:179 (≠ KPAE 183:186) binding NAD(+)
- F180 (≠ D187) mutation to T: Can bind and use NADP(+) as coenzyme. 16-fold increase in catalytic efficiency with NAD(+) as coenzyme.
- Q214 (≠ D224) binding NAD(+)
- S230 (= S240) binding NAD(+)
- E251 (= E261) binding (S)-lactate
- N286 (≠ V296) 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 (≠ K345) binding NAD(+)
- E443 (≠ A456) binding (S)-lactate
- H449 (≠ F462) 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)
38% identity, 95% coverage: 16:486/494 of query aligns to 8:471/477 of 2impA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E381 (= E396), A458 (≠ E473)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), E177 (= E186), F178 (≠ D187), G207 (≠ A217), G211 (≠ V223), Q212 (≠ D224), S228 (= S240), A231 (≠ V243), K234 (≠ H246), R334 (≠ K345)
2iluA Crystal structure of lactaldehyde dehydrogenase from e. Coli: the binary complex with NADPH (see paper)
38% identity, 95% coverage: 16:486/494 of query aligns to 8:471/477 of 2iluA
- active site: N151 (= N160), K174 (= K183), E249 (= E261), C283 (= C295), E381 (= E396), A458 (≠ E473)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I147 (= I156), L148 (≠ T157), P149 (= P158), W150 (= W159), K174 (= K183), S176 (≠ A185), E177 (= E186), R206 (= R216), G207 (≠ A217), G211 (≠ V223), Q212 (≠ D224), S228 (= S240), A231 (≠ V243), K234 (≠ H246), I235 (≠ L247), N328 (= N339), R334 (≠ K345), F383 (= F398)
4o6rA Crystal structure of a putative aldehyde dehydrogenase from burkholderia cenocepacia
38% identity, 96% coverage: 11:486/494 of query aligns to 2:473/489 of 4o6rA
- active site: N150 (= N160), K173 (= K183), E248 (= E261), C282 (= C295), E383 (= E396), E460 (= E473)
- binding adenosine monophosphate: I146 (= I156), V147 (≠ T157), K173 (= K183), G206 (≠ R216), G210 (≠ P220), Q211 (≠ A221), F224 (= F237), G226 (= G239), S227 (= S240), T230 (≠ V243), R233 (≠ H246)
Q9H2A2 2-aminomuconic semialdehyde dehydrogenase; Aldehyde dehydrogenase 12; Aldehyde dehydrogenase family 8 member A1; EC 1.2.1.32 from Homo sapiens (Human) (see paper)
36% identity, 97% coverage: 10:488/494 of query aligns to 7:483/487 of Q9H2A2
- R109 (≠ Y114) mutation to A: About 65-fold loss of catalytic efficiency.
- N155 (= N160) mutation to A: Complete loss of activity.
- R451 (≠ A456) mutation to A: Complete loss of activity.
5gtlA NADPH complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 95% coverage: 16:486/494 of query aligns to 20:484/491 of 5gtlA
- active site: N165 (= N160), K188 (= K183), E263 (= E261), C297 (= C295), E394 (= E396), E471 (= E473)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I161 (= I156), P163 (= P158), K188 (= K183), A190 (= A185), E191 (= E186), Q192 (≠ D187), G221 (≠ R216), G225 (≠ P220), G241 (= G239), S242 (= S240), T245 (≠ V243), L264 (= L262), C297 (= C295), E394 (= E396), F396 (= F398)
5gtkA NAD+ complex structure of aldehyde dehydrogenase from bacillus cereus
37% identity, 95% coverage: 16:486/494 of query aligns to 20:484/491 of 5gtkA
- active site: N165 (= N160), K188 (= K183), E263 (= E261), C297 (= C295), E394 (= E396), E471 (= E473)
- binding nicotinamide-adenine-dinucleotide: I161 (= I156), I162 (≠ T157), P163 (= P158), W164 (= W159), K188 (= K183), E191 (= E186), G221 (≠ R216), G225 (≠ P220), A226 (= A221), F239 (= F237), G241 (= G239), S242 (= S240), T245 (≠ V243), Y248 (≠ H246), L264 (= L262), C297 (= C295), Q344 (≠ A342), R347 (≠ K345), E394 (= E396), F396 (= F398)
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, 97% coverage: 11:489/494 of query aligns to 16:492/505 of 4neaA
- active site: N166 (= N160), K189 (= K183), E264 (= E261), C298 (= C295), E399 (= E396), E476 (= E473)
- binding nicotinamide-adenine-dinucleotide: P164 (= P158), K189 (= K183), E192 (= E186), G222 (≠ R216), G226 (≠ P220), G242 (= G239), G243 (≠ S240), T246 (≠ V243), H249 (= H246), I250 (≠ L247), C298 (= C295), E399 (= E396), F401 (= F398)
Query Sequence
>WP_029002104.1 NCBI__GCF_000430725.1:WP_029002104.1
MSLNLRRDDLIRTQNFVNGRWCDALDANALLGVTNPADESLITRVPDSSAEDARAAVEAA
QAAFAGWRATPAKERARLLKRWNDLIVEHQEDLGRLISREQGKPLAEGRGEVLYAASYVE
WFAEEATRANGEVIPAPQRGRRMFALKEPVGVVAVITPWNFPAAMIARKIAPALAAGCTV
VAKPAEDTPLTSLALVRLAEEAGFPAGVLNIVTASRANTPAVVDEWLRDARVRKISFTGS
TPVGVHLARESAATLKKLSLELGGNAPFIVFEDADLDAAVQGLMAAKFRNGGQTCVCPNR
VYVHASVHDAFVEKLAAVVGALKVGPASNPTSQIGPMINARAVDKIERHVNDAVARGARV
VAGGHRVRNDVASGPNYYAPTVLVDAQPDMECACEETFGPVAPVFRFKDEAEVIALANDT
PFGLAAYFYSQNVARIWRVAEALETGIVGVNEGALAAEAAPFGGVKASGYGREGSTHGLD
DYLHVKYLCQGGLS
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