SitesBLAST
Comparing PP_0213 FitnessBrowser__Putida:PP_0213 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)
82% identity, 100% coverage: 1:480/480 of query aligns to 1:482/482 of P25526
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
82% identity, 100% coverage: 2:480/480 of query aligns to 1:481/481 of 3jz4A
- active site: N156 (= N157), K179 (= K180), E254 (= E255), C288 (= C289), E385 (= E384), E462 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I152 (= I153), P154 (= P155), W155 (= W156), N156 (= N157), K179 (= K180), A181 (= A182), S182 (= S183), S211 (= S212), A212 (= A213), G213 (= G214), G216 (= G217), F230 (= F231), T231 (= T232), G232 (= G233), S233 (= S234), I236 (= I237), E254 (= E255), L255 (= L256), C288 (= C289), K338 (= K339), E385 (= E384), F387 (= F386)
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)
57% identity, 99% coverage: 5:477/480 of query aligns to 55:531/535 of P51649
- C93 (≠ M45) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G128) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ P132) to Y: 83% of activity; dbSNP:rs2760118
- P182 (≠ H134) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R165) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C175) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KPAS 180:183) binding
- T233 (= T185) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (= A189) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S207) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (= G217) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSTEIG 233:238) binding
- R334 (= R283) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N284) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C289) modified: Disulfide link with 342, In inhibited form
- C342 (= C291) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (= N320) natural variant: N -> S
- P382 (= P330) to L: in SSADHD; 2% of activity
- V406 (= V354) to I: in dbSNP:rs143741652
- G409 (= G357) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (= S444) 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, 99% coverage: 5:477/480 of query aligns to 5:481/485 of 2w8rA
- active site: N155 (= N157), K178 (= K180), E256 (= E255), A290 (≠ C289), E388 (= E384), E465 (= E461)
- binding adenosine-5'-diphosphate: I151 (= I153), T152 (= T154), P153 (= P155), W154 (= W156), K178 (= K180), P179 (= P181), A180 (= A182), E181 (≠ S183), A214 (= A213), K215 (≠ G214), F232 (= F231), S235 (= S234), T238 (≠ I237)
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
56% identity, 99% coverage: 5:477/480 of query aligns to 5:481/485 of 2w8qA
- active site: N155 (= N157), K178 (= K180), E256 (= E255), A290 (≠ C289), E388 (= E384), E465 (= E461)
- binding succinic acid: Y109 (= Y111), F156 (= F158), R163 (= R165), E256 (= E255), R284 (= R283), A290 (≠ C289), V291 (= V290), S448 (= S444), F454 (= F450)
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
43% identity, 97% coverage: 12:478/480 of query aligns to 6:474/476 of 5x5uA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E380 (= E384), E457 (= E461)
- binding glycerol: D15 (= D21), A16 (= A22), A17 (≠ D23), G19 (= G25)
- binding nicotinamide-adenine-dinucleotide: P149 (= P155), W150 (= W156), N151 (= N157), P207 (≠ A213), A208 (≠ G214), S211 (≠ G217), F225 (= F231), T226 (= T232), G227 (= G233), S228 (= S234), V231 (≠ I237), L235 (= L241), E249 (= E255), L250 (= L256), C283 (= C289), R329 (≠ K335), R330 (≠ A336), E380 (= E384), F382 (= F386)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
43% identity, 97% coverage: 12:478/480 of query aligns to 6:474/476 of 5x5tA
6j76A Structure of 3,6-anhydro-l-galactose dehydrogenase in complex with nap (see paper)
39% identity, 98% coverage: 12:479/480 of query aligns to 3:476/477 of 6j76A
- active site: N148 (= N157), E246 (= E255), C280 (= C289), E458 (= E461)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I144 (= I153), T145 (= T154), A146 (≠ P155), W147 (= W156), N148 (= N157), K171 (= K180), P172 (= P181), T173 (≠ A182), S174 (= S183), G203 (≠ S212), G204 (≠ A213), R205 (≠ G214), G208 (= G217), N209 (≠ G218), T223 (= T232), G224 (= G233), S225 (= S234), A228 (≠ I237), S231 (≠ Q240), I232 (≠ L241), E246 (= E255), L247 (= L256), G248 (= G257), C280 (= C289), E381 (= E384), F383 (= F386), H447 (≠ F450)
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
38% identity, 97% coverage: 14:479/480 of query aligns to 8:476/477 of 2opxA
- active site: N151 (= N157), K174 (= K180), E249 (= E255), C283 (= C289), E381 (= E384), A458 (≠ E461)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: Q97 (≠ A103), L98 (≠ E104), V101 (≠ G107), F105 (≠ Y111), F152 (= F158), F155 (≠ A161), D273 (≠ I279), I277 (≠ R283), N284 (≠ V290), F312 (≠ I318), G313 (= G319), R318 (≠ E324), D320 (vs. gap), I321 (≠ T326), A322 (≠ T327), K359 (≠ N364), Y362 (≠ F365), F440 (≠ I443), F440 (≠ I443), E441 (≠ S444)
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, 97% coverage: 14:479/480 of query aligns to 10:478/479 of P25553