SitesBLAST
Comparing WP_012404681.1 NCBI__GCF_000020045.1:WP_012404681.1 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)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
86% identity, 99% coverage: 6:481/482 of query aligns to 1:476/476 of 5x5uA
- active site: N151 (= N156), K174 (= K179), E249 (= E254), C283 (= C288), E380 (= E385), E457 (= E462)
- binding glycerol: D15 (= D20), A16 (= A21), A17 (= A22), G19 (= G24)
- binding nicotinamide-adenine-dinucleotide: P149 (= P154), P207 (= P212), A208 (= A213), S211 (= S216), G227 (= G232), S228 (= S233), V231 (= V236), R329 (= R334), R330 (= R335), E380 (= E385), F382 (= F387)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
86% identity, 99% coverage: 6:481/482 of query aligns to 1:476/476 of 5x5tA
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)
41% identity, 99% coverage: 2:479/482 of query aligns to 3:480/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
41% identity, 99% coverage: 2:479/482 of query aligns to 2:479/481 of 3jz4A
- active site: N156 (= N156), K179 (= K179), E254 (= E254), C288 (= C288), E385 (= E385), E462 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P154), W155 (= W155), K179 (= K179), A181 (≠ P181), S182 (≠ E182), A212 (≠ P212), G216 (≠ S216), G232 (= G232), S233 (= S233), I236 (≠ V236), C288 (= C288), K338 (≠ A338), E385 (= E385), F387 (= F387)
8of1A Structure of aldh5f1 from moss physcomitrium patens in complex with NAD+ in the contracted conformation
40% identity, 97% coverage: 13:479/482 of query aligns to 31:497/505 of 8of1A
- binding nicotinamide-adenine-dinucleotide: I170 (≠ F152), A171 (≠ T153), P172 (= P154), W173 (= W155), K197 (= K179), A230 (≠ P212), F248 (= F230), G250 (= G232), S251 (= S233), V254 (= V236), M257 (≠ Q239), L273 (= L255), C306 (= C288), K356 (≠ A338), E403 (= E385), F405 (= F387)
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)
40% identity, 99% coverage: 4:478/482 of query aligns to 55:531/535 of P51649
- C93 (≠ A44) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G127) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P131) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ R133) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R164) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C174) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KAPE 179:182) binding NAD(+)
- T233 (= T184) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ P188) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ G206) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S216) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTPVG 232:237) binding NAD(+)
- R334 (= R282) binding substrate; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N283) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C288) modified: Disulfide link with 342, In inhibited form
- C342 (≠ S290) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D319) natural variant: N -> S
- P382 (= P329) to L: in SSADHD; 2% of activity
- V406 (= V353) to I: in dbSNP:rs143741652
- G409 (= G356) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ P445) 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)
39% identity, 99% coverage: 4:478/482 of query aligns to 5:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
39% identity, 99% coverage: 4:478/482 of query aligns to 5:481/485 of 2w8qA
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565 (see paper)
39% identity, 97% coverage: 11:479/482 of query aligns to 11:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F152), T153 (= T153), P154 (= P154), K179 (= K179), A212 (≠ P212), K213 (≠ A213), F230 (= F230), T231 (= T231), G232 (= G232), S233 (= S233), V236 (= V236), W239 (≠ Q239), G256 (= G256)
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)
35% identity, 98% coverage: 7:479/482 of query aligns to 4:481/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 153:156) binding NADPH
- K162 (= K165) active site, Charge relay system
- KPSE 176:179 (≠ KAPE 179:182) binding NADPH
- G209 (≠ P212) binding NADPH
- GTST 230:233 (≠ STPV 233:236) binding NADPH
- E252 (= E254) active site, Proton acceptor
- C286 (= C288) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E385) binding NADPH
- E464 (= E462) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
34% identity, 98% coverage: 7:479/482 of query aligns to 3:480/489 of 4cazA
- active site: N152 (= N156), K175 (= K179), E251 (= E254), C285 (= C288), E386 (= E385), E463 (= E462)
- 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 (≠ F152), G149 (≠ T153), W151 (= W155), N152 (= N156), K175 (= K179), E178 (= E182), G208 (≠ P212), G212 (≠ S216), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ S233), T232 (≠ V236), V236 (vs. gap), E251 (= E254), L252 (= L255), C285 (= C288), E386 (= E385), F388 (= F387)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
34% identity, 98% coverage: 7:479/482 of query aligns to 3:480/489 of 2woxA
- active site: N152 (= N156), K175 (= K179), E251 (= E254), C285 (= C288), E386 (= E385), E463 (= E462)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F152), G149 (≠ T153), W151 (= W155), N152 (= N156), K175 (= K179), S177 (≠ P181), E178 (= E182), G208 (≠ P212), G212 (≠ S216), F226 (= F230), T227 (= T231), G228 (= G232), G229 (≠ S233), T232 (≠ V236), V236 (vs. gap), E251 (= E254), L252 (= L255), C285 (= C288), E386 (= E385), F388 (= F387)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
34% identity, 98% coverage: 7:479/482 of query aligns to 3:480/489 of 2wmeA
- active site: N152 (= N156), K175 (= K179), E251 (= E254), C285 (= C288), E386 (= E385), E463 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T153), W151 (= W155), K175 (= K179), S177 (≠ P181), E178 (= E182), G208 (≠ P212), G212 (≠ S216), F226 (= F230), G228 (= G232), G229 (≠ S233), T232 (≠ V236), V236 (vs. gap)
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)
34% identity, 97% coverage: 11:477/482 of query aligns to 19:491/505 of 4neaA
- active site: N166 (= N156), K189 (= K179), E264 (= E254), C298 (= C288), E399 (= E385), E476 (= E462)
- binding nicotinamide-adenine-dinucleotide: P164 (= P154), K189 (= K179), E192 (= E182), G222 (≠ P212), G226 (≠ S216), G242 (= G232), G243 (≠ S233), T246 (≠ V236), H249 (≠ Q239), I250 (≠ L240), C298 (= C288), E399 (= E385), F401 (= F387)
5izdA Wild-type glyceraldehyde dehydrogenase from thermoplasma acidophilum in complex with NADP
33% identity, 98% coverage: 9:479/482 of query aligns to 2:475/494 of 5izdA
- active site: N149 (= N156), K172 (= K179), E247 (= E254), C281 (= C288), E381 (= E385), E458 (= E462)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: L145 (≠ F152), T146 (= T153), W148 (= W155), K172 (= K179), P173 (≠ A180), S174 (≠ P181), S175 (≠ E182), R204 (≠ D211), G205 (≠ P212), G209 (≠ S216), D210 (≠ S217), G225 (= G232), S226 (= S233), T229 (≠ V236)
8skfA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (lattice translocation disorder)
35% identity, 99% coverage: 5:479/482 of query aligns to 9:488/497 of 8skfA
- binding calcium ion: T33 (≠ V29), I34 (≠ V30), D100 (≠ E96), V187 (≠ E183)
- binding nicotinamide-adenine-dinucleotide: I156 (≠ F152), G157 (≠ T153), A158 (≠ P154), W159 (= W155), K183 (= K179), E186 (= E182), G216 (≠ P212), G220 (≠ S216), T235 (= T231), G236 (= G232), G237 (≠ S233), S240 (≠ V236), K243 (≠ Q239), E259 (= E254), C293 (= C288), F396 (= F387)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
35% identity, 98% coverage: 9:479/482 of query aligns to 4:479/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
35% identity, 98% coverage: 9:479/482 of query aligns to 4:479/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
35% identity, 98% coverage: 9:479/482 of query aligns to 4:479/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
35% identity, 98% coverage: 9:479/482 of query aligns to 4:479/488 of 8vqwC
- binding coenzyme a: I147 (≠ F152), W150 (= W155), K174 (= K179), S176 (≠ P181), E177 (= E182), G207 (≠ P212), G211 (≠ S216), F225 (= F230), G227 (= G232), G228 (≠ S233), S231 (≠ V236), H331 (≠ R335), F387 (= F387)
Query Sequence
>WP_012404681.1 NCBI__GCF_000020045.1:WP_012404681.1
MVTSSSYTDTRLLINNEWCDAASGKTLDVVNPATGKPIGKVAHAGKADLDRALEAAQKGF
EAWRKVPANERATTMRKAAGFVRERADHIARLMTQEQGKPFAEARIEVLSAADIIEWFAD
EGRRVYGRVVPSRNLNAQSLVIKEPIGPVAAFTPWNFPVNQVVRKLSAALASGCSFLVKA
PEETPASPAQLLQAFVDAGVPAGTVGLVFGDPAEISSYLIPHPVIRKVTFTGSTPVGKQL
AALAGSHMKRATMELGGHAPVIVAEDADVALAVKAAGGAKFRNAGQVCISPTRFLVHNSI
REAFAAALVKHAEGLKVGDGLAEGTQLGPLANARRLTAMASIIDNARSTGATVATGGERI
GSEGNFFAPTVLTDVPLEADVFNNEPFGPIAAIRGFDNIEDAIAEANRLPFGLAGYAFTK
SFRNVHLLSQNLEVGMLWINQPATPTPEMPFGGVKDSGYGSEGGPEAMEAYLVTKAVTVM
AV
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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