SitesBLAST
Comparing 3609503 Dshi_2887 succinic semialdehyde dehydrogenase (RefSeq) 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)
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, 98% coverage: 11:492/492 of query aligns to 2:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
63% identity, 98% coverage: 11:492/492 of query aligns to 1:481/481 of 3jz4A
- active site: N156 (= N166), K179 (= K189), E254 (= E265), C288 (= C299), E385 (= E396), E462 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P164), W155 (= W165), K179 (= K189), A181 (= A191), S182 (≠ E192), A212 (≠ S223), G216 (= G227), G232 (= G243), S233 (= S244), I236 (≠ V247), C288 (= C299), K338 (= K349), E385 (= E396), F387 (= F398)
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
65% identity, 97% coverage: 12:490/492 of query aligns to 2:479/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (= I162), T153 (= T163), P154 (= P164), K179 (= K189), A212 (≠ S223), K213 (≠ S224), F230 (= F241), T231 (= T242), G232 (= G243), S233 (= S244), V236 (= V247), W239 (≠ I250), G256 (= G267)
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)
56% identity, 96% coverage: 16:489/492 of query aligns to 57:531/535 of P51649
- C93 (≠ L54) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G137) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P141) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H143) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R174) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C184) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (= KPAE 189:192) binding
- T233 (= T194) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A198) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ A216) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G227) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTQVG 243:248) binding
- R334 (= R293) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N294) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C299) modified: Disulfide link with 342, In inhibited form
- C342 (= C301) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ D330) natural variant: N -> S
- P382 (= P340) to L: in SSADHD; 2% of activity
- V406 (= V364) to I: in dbSNP:rs143741652
- G409 (= G367) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S456) binding ; 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)
56% identity, 96% coverage: 16:489/492 of query aligns to 7:481/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 96% coverage: 16:489/492 of query aligns to 7:481/485 of 2w8qA
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
41% identity, 95% coverage: 26:490/492 of query aligns to 11:474/476 of 5x5uA
- active site: N151 (= N166), K174 (= K189), E249 (= E265), C283 (= C299), E380 (= E396), E457 (= E473)
- binding glycerol: D15 (= D30), A16 (= A31), A17 (≠ D32), G19 (= G34)
- binding nicotinamide-adenine-dinucleotide: P149 (= P164), P207 (≠ S223), A208 (≠ S224), S211 (≠ G227), G227 (= G243), S228 (= S244), V231 (= V247), R329 (≠ P345), R330 (≠ A346), E380 (= E396), F382 (= F398)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
41% identity, 95% coverage: 26:490/492 of query aligns to 11:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
37% identity, 96% coverage: 21:491/492 of query aligns to 3:476/477 of 6j76A
- active site: N148 (= N166), E246 (= E265), C280 (= C299), E458 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I162), T145 (= T163), A146 (≠ P164), W147 (= W165), N148 (= N166), K171 (= K189), T173 (≠ A191), S174 (≠ E192), G204 (≠ S223), G208 (= G227), T223 (= T242), G224 (= G243), S225 (= S244), A228 (≠ V247), S231 (≠ I250), I232 (≠ L251), E246 (= E265), L247 (= L266), C280 (= C299), E381 (= E396), F383 (= F398), H447 (≠ F462)
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
38% identity, 96% coverage: 20:492/492 of query aligns to 6:482/489 of 4cazA
- active site: N152 (= N166), K175 (= K189), E251 (= E265), C285 (= C299), E386 (= E396), E463 (= E473)
- 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 (= I162), G149 (≠ T163), W151 (= W165), N152 (= N166), K175 (= K189), E178 (= E192), G208 (≠ S223), G212 (= G227), F226 (= F241), T227 (= T242), G228 (= G243), G229 (≠ S244), T232 (≠ V247), V236 (≠ L251), E251 (= E265), L252 (= L266), C285 (= C299), E386 (= E396), F388 (= F398)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
38% identity, 96% coverage: 20:492/492 of query aligns to 6:482/489 of 2woxA
- active site: N152 (= N166), K175 (= K189), E251 (= E265), C285 (= C299), E386 (= E396), E463 (= E473)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (= I162), G149 (≠ T163), W151 (= W165), N152 (= N166), K175 (= K189), S177 (≠ A191), E178 (= E192), G208 (≠ S223), G212 (= G227), F226 (= F241), T227 (= T242), G228 (= G243), G229 (≠ S244), T232 (≠ V247), V236 (≠ L251), E251 (= E265), L252 (= L266), C285 (= C299), E386 (= E396), F388 (= F398)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
38% identity, 96% coverage: 20:492/492 of query aligns to 6:482/489 of 2wmeA
- active site: N152 (= N166), K175 (= K189), E251 (= E265), C285 (= C299), E386 (= E396), E463 (= E473)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T163), W151 (= W165), K175 (= K189), S177 (≠ A191), E178 (= E192), G208 (≠ S223), G212 (= G227), F226 (= F241), G228 (= G243), G229 (≠ S244), T232 (≠ V247), V236 (≠ L251)
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)
38% identity, 96% coverage: 20:492/492 of query aligns to 7:483/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 163:166) binding
- K162 (= K175) active site, Charge relay system
- KPSE 176:179 (≠ KPAE 189:192) binding
- G209 (≠ S223) binding
- GTST 230:233 (≠ STQV 244:247) binding
- E252 (= E265) active site, Proton acceptor
- C286 (= C299) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E396) binding
- E464 (= E473) active site, Charge relay system
4pz2B Structure of zm aldh2-6 (rf2f) in complex with NAD (see paper)
40% identity, 96% coverage: 15:488/492 of query aligns to 6:484/494 of 4pz2B
- active site: N159 (= N166), K182 (= K189), E258 (= E265), C292 (= C299), E392 (= E396), D469 (≠ E473)
- binding nicotinamide-adenine-dinucleotide: I155 (= I162), I156 (≠ T163), P157 (= P164), W158 (= W165), N159 (= N166), M164 (= M171), K182 (= K189), A184 (= A191), E185 (= E192), G215 (≠ D222), G219 (= G227), F233 (= F241), T234 (= T242), G235 (= G243), S236 (= S244), V239 (= V247), E258 (= E265), L259 (= L266), C292 (= C299), E392 (= E396), F394 (= F398)
4pxlA Structure of zm aldh2-3 (rf2c) in complex with NAD (see paper)
39% identity, 96% coverage: 20:489/492 of query aligns to 6:477/486 of 4pxlA
- active site: N154 (= N166), K177 (= K189), E253 (= E265), C287 (= C299), E384 (= E396), D461 (≠ E473)
- binding nicotinamide-adenine-dinucleotide: I150 (= I162), V151 (≠ T163), P152 (= P164), W153 (= W165), K177 (= K189), E180 (= E192), G210 (≠ D222), G214 (= G227), A215 (≠ K228), F228 (= F241), G230 (= G243), S231 (= S244), V234 (= V247), E253 (= E265), G255 (= G267), C287 (= C299), Q334 (≠ A346), K337 (= K349), E384 (= E396), F386 (= F398)
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)
36% identity, 98% coverage: 12:492/492 of query aligns to 12:495/501 of Q56YU0
- G152 (≠ I149) mutation to E: In ref1-7; reduced activity on sinapaldehyde.
- G416 (≠ V413) mutation to R: In ref1-6; reduced activity on sinapaldehyde.
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, 96% coverage: 18:491/492 of query aligns to 16:494/505 of 4neaA
- active site: N166 (= N166), K189 (= K189), E264 (= E265), C298 (= C299), E399 (= E396), E476 (= E473)
- binding nicotinamide-adenine-dinucleotide: P164 (= P164), K189 (= K189), E192 (= E192), G222 (≠ S223), G226 (= G227), G242 (= G243), G243 (≠ S244), T246 (≠ V247), H249 (≠ I250), I250 (≠ L251), C298 (= C299), E399 (= E396), F401 (= F398)
7radA Crystal structure analysis of aldh1b1
37% identity, 97% coverage: 14:492/492 of query aligns to 7:488/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I162), I159 (≠ T163), P160 (= P164), W161 (= W165), N162 (= N166), M167 (= M171), K185 (= K189), E188 (= E192), G218 (≠ D222), G222 (= G227), A223 (≠ K228), T237 (= T242), G238 (= G243), S239 (= S244), V242 (= V247), E261 (= E265), L262 (= L266), C295 (= C299), E392 (= E396), F394 (= F398)
- 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 (= E117), F163 (= F167), E285 (≠ A289), F289 (≠ R293), N450 (≠ I454), V452 (≠ S456)
7mjdA Crystal structure analysis of aldh1b1
37% identity, 97% coverage: 14:492/492 of query aligns to 7:488/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I162), I159 (≠ T163), P160 (= P164), W161 (= W165), N162 (= N166), M167 (= M171), K185 (= K189), E188 (= E192), G218 (≠ D222), G222 (= G227), F236 (= F241), T237 (= T242), G238 (= G243), S239 (= S244), V242 (= V247), E261 (= E265), L262 (= L266), C295 (= C299), E392 (= E396), F394 (= F398)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (= E117), E285 (≠ A289), F289 (≠ R293), N450 (≠ I454), V452 (≠ S456)
7mjcA Crystal structure analysis of aldh1b1
37% identity, 97% coverage: 14:492/492 of query aligns to 7:488/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I162), I159 (≠ T163), P160 (= P164), W161 (= W165), N162 (= N166), K185 (= K189), E188 (= E192), G218 (≠ D222), G222 (= G227), T237 (= T242), G238 (= G243), S239 (= S244), V242 (= V247), E261 (= E265), L262 (= L266), C295 (= C299), E392 (= E396), F394 (= F398)
Query Sequence
>3609503 Dshi_2887 succinic semialdehyde dehydrogenase (RefSeq)
MLDTVTELREHLKDPALLASKAYFAGAWTDADSGATFPVTNPARGDVIAHVPDLGRAETA
RAIAAADAAQKPWAARTAKDRAQVLRRWFDLIVGNADDLARILTAEMGKPLAEARGEVMY
GASFVEWFAEEAKRLYGETIPGHLPDARIQVIRQPIGVVGAITPWNFPIAMITRKAAPAL
AAGCAFLSKPAEDTPLSALALAVLAERAGIPAGLFAVLPSSDSSAIGKEFCENHTVRKLT
FTGSTQVGRILLAQAADQVKKCSMELGGNAPFIVFDDADLDKAVEGAMACKFRNAGQTCV
CANRIYVQDGVYDAFAEKLAAAVEELKVGDGAAEGVTIGPLINMPAVEKVQDHLDDLRAK
GGTVVTGGETHPLGGTFFTPTVVTGVTQEMKVAREETFGPVAPLFRFTEEDEVIAMANDT
IFGLAGYFYARDIGRITRVSEALEYGIVGINTGIISTEGAPFGGVKQSGLGREGSRHGID
EYLEMKYICLSI
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