SitesBLAST
Comparing RR42_RS29720 FitnessBrowser__Cup4G11:RR42_RS29720 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)
51% identity, 99% coverage: 2:474/476 of query aligns to 2:473/476 of 5x5uA
- active site: N151 (= N152), K174 (= K175), E249 (= E250), C283 (= C284), E380 (= E381), E457 (= E458)
- binding glycerol: D15 (≠ G15), A16 (≠ G17), A17 (≠ G18), G19 (≠ R20)
- binding nicotinamide-adenine-dinucleotide: P149 (= P150), P207 (= P208), A208 (≠ H209), S211 (= S212), G227 (= G228), S228 (= S229), V231 (= V232), R329 (= R330), R330 (= R331), E380 (= E381), F382 (= F383)
5x5tA Crystal structure of alpha-ketoglutarate semialdehyde dehydrogenase (kgsadh) from azospirillum brasilense (see paper)
51% identity, 99% coverage: 2:474/476 of query aligns to 2:473/476 of 5x5tA
3jz4A Crystal structure of e. Coli NADP dependent enzyme (see paper)
41% identity, 98% coverage: 9:473/476 of query aligns to 14:477/481 of 3jz4A
- active site: N156 (= N152), K179 (= K175), E254 (= E250), C288 (= C284), E385 (= E381), E462 (= E458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: P154 (= P150), W155 (= W151), K179 (= K175), A181 (≠ P177), S182 (≠ E178), A212 (≠ P208), G216 (≠ S212), G232 (= G228), S233 (= S229), I236 (≠ V232), C288 (= C284), K338 (≠ E334), E385 (= E381), F387 (= F383)
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, 98% coverage: 9:473/476 of query aligns to 15:478/482 of P25526
8c54A Cryo-em structure of nadh bound sla dehydrogenase rlgabd from rhizobium leguminosarum bv. Trifolii srd1565
40% identity, 98% coverage: 8:473/476 of query aligns to 13:477/482 of 8c54A
- binding 1,4-dihydronicotinamide adenine dinucleotide: I152 (≠ F148), T153 (= T149), P154 (= P150), K179 (= K175), A212 (≠ P208), K213 (≠ H209), F230 (= F226), T231 (= T227), G232 (= G228), S233 (= S229), V236 (= V232), W239 (≠ K235), G256 (= G252)
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)
41% identity, 95% coverage: 25:474/476 of query aligns to 78:531/535 of P51649
- C93 (≠ A40) to F: in SSADHD; 3% of activity; dbSNP:rs765561257
- G176 (= G123) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (vs. gap) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P127) to L: 48% of activity; dbSNP:rs3765310
- R213 (= R160) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C170) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KGPE 175:178) binding
- T233 (≠ S180) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ I184) to S: 65% of activity; dbSNP:rs62621664
- N255 (= N202) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ S212) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSVDVG 228:233) binding
- R334 (= R278) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (= N279) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (= C284) modified: Disulfide link with 342, In inhibited form
- C342 (≠ A286) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
- N372 (≠ P315) natural variant: N -> S
- P382 (= P325) to L: in SSADHD; 2% of activity
- V406 (= V349) to I: in dbSNP:rs143741652
- G409 (= G352) to D: in SSADHD; <1% of activity; dbSNP:rs118203984
- S498 (≠ A441) 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)
41% identity, 94% coverage: 25:473/476 of query aligns to 28:480/485 of 2w8rA
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
41% identity, 94% coverage: 25:473/476 of query aligns to 28:480/485 of 2w8qA
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)
37% identity, 99% coverage: 2:473/476 of query aligns to 4:479/490 of Q9HTJ1
- GAWN 150:153 (≠ TPWN 149:152) binding
- K162 (= K161) active site, Charge relay system
- KPSE 176:179 (≠ KGPE 175:178) binding
- G209 (≠ P208) binding
- GTST 230:233 (≠ SVDV 229:232) binding
- E252 (= E250) active site, Proton acceptor
- C286 (= C284) binding covalent; modified: Cysteine sulfenic acid (-SOH)
- E387 (= E381) binding
- E464 (= E458) active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
37% identity, 99% coverage: 2:473/476 of query aligns to 3:478/489 of 4cazA
- active site: N152 (= N152), K175 (= K175), E251 (= E250), C285 (= C284), E386 (= E381), E463 (= E458)
- 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 (≠ F148), G149 (≠ T149), W151 (= W151), N152 (= N152), K175 (= K175), E178 (= E178), G208 (≠ P208), G212 (≠ S212), F226 (= F226), T227 (= T227), G228 (= G228), G229 (≠ S229), T232 (≠ V232), V236 (vs. gap), E251 (= E250), L252 (= L251), C285 (= C284), E386 (= E381), F388 (= F383)
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
37% identity, 99% coverage: 2:473/476 of query aligns to 3:478/489 of 2woxA
- active site: N152 (= N152), K175 (= K175), E251 (= E250), C285 (= C284), E386 (= E381), E463 (= E458)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F148), G149 (≠ T149), W151 (= W151), N152 (= N152), K175 (= K175), S177 (≠ P177), E178 (= E178), G208 (≠ P208), G212 (≠ S212), F226 (= F226), T227 (= T227), G228 (= G228), G229 (≠ S229), T232 (≠ V232), V236 (vs. gap), E251 (= E250), L252 (= L251), C285 (= C284), E386 (= E381), F388 (= F383)
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
37% identity, 99% coverage: 2:473/476 of query aligns to 3:478/489 of 2wmeA
- active site: N152 (= N152), K175 (= K175), E251 (= E250), C285 (= C284), E386 (= E381), E463 (= E458)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (≠ T149), W151 (= W151), K175 (= K175), S177 (≠ P177), E178 (= E178), G208 (≠ P208), G212 (≠ S212), F226 (= F226), G228 (= G228), G229 (≠ S229), T232 (≠ V232), V236 (vs. gap)
6wsbA Crystal structure of a betaine aldehyde dehydrogenase from burkholderia pseudomallei bound to cofactor NAD (see paper)
40% identity, 95% coverage: 21:473/476 of query aligns to 21:477/489 of 6wsbA
- active site: N152 (= N152), E250 (= E250), C284 (= C284), E462 (= E458)
- binding nicotinamide-adenine-dinucleotide: I148 (≠ F148), G149 (≠ T149), A150 (≠ P150), W151 (= W151), N152 (= N152), K175 (= K175), E178 (= E178), G208 (≠ H209), G211 (≠ S212), A212 (≠ D213), F225 (= F226), T226 (= T227), G227 (= G228), G228 (≠ S229), T231 (≠ V232), V235 (≠ L236), E250 (= E250), L251 (= L251), G252 (= G252), C284 (= C284), E385 (= E381), F387 (= F383)
8vr1A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (ctp bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8vr1A
8vr0A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (gmp bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8vr0A
8vqzA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (cmp bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8vqzA
8vqwC Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (coa bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8vqwC
- binding coenzyme a: I147 (≠ F148), W150 (= W151), K174 (= K175), S176 (≠ P177), E177 (= E178), G207 (≠ P208), G211 (≠ S212), F225 (= F226), G227 (= G228), G228 (≠ S229), S231 (≠ V232), H331 (≠ R331), F387 (= F383)
8vj3A Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (fad bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8vj3A
8uzoA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (adp bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8uzoA
8uznA Crystal structure of betaine aldehyde dehydrogenase (betb) from klebsiella aerogenes (amp bound)
36% identity, 99% coverage: 4:473/476 of query aligns to 4:477/488 of 8uznA
- binding adenosine monophosphate: I147 (≠ F148), G148 (≠ T149), K174 (= K175), S176 (≠ P177), E177 (= E178), G207 (≠ P208), G211 (≠ S212), F225 (= F226), G228 (≠ S229), S231 (≠ V232), K234 (= K235)
Query Sequence
>RR42_RS29720 FitnessBrowser__Cup4G11:RR42_RS29720
MYPELFLYINGEFIGVGGQRKSEDVTNPATREVLGRLPHATIADLAHAVATSQSAFLKWR
KSSPLQRSEILRRAASLARERADDIAQAITLDQGKPLAEARAEVVTCADHADWHAEECRR
IYGRVIPPRDTAVRQIVVREPVGVCVAFTPWNFPFNQAIRKITAAIGAGCAIVLKGPEDS
PSAIVALAKLFHDAGLPPGVLNIVWGVPHEVSDFLIQHPLVRKVSFTGSVDVGKKLAALA
GHHMKRATMELGGHAPVIVCDDADVDSAVQVTMRMKLRNAGQVCVAPTRLFVQSGIYTKF
RDQMIEAFETARLGPGIDSSTTMGPLAHARRVKEMERFVADAKARGGNVLTGGFAPELGG
SFFAPTLVDNLDDTADLMQKEPFGPIAPLAKFDTLDEAIARANSLPFGLAAFAFTERTRS
AHRLATELEAGMVNINHAGMALPETPFGGIKDSGMGSEGGTETFDGYLTTKFVTQV
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