SitesBLAST
Comparing RR42_RS23090 FitnessBrowser__Cup4G11:RR42_RS23090 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)
1eyyA Crystal structure of the NADP+ dependent aldehyde dehydrogenase from vibrio harveyi. (see paper)
48% identity, 95% coverage: 17:521/533 of query aligns to 1:502/504 of 1eyyA
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)
29% identity, 56% coverage: 6:304/533 of query aligns to 8:288/490 of Q9HTJ1
- GAWN 150:153 (≠ GASN 156:159) binding
- K162 (≠ D170) active site, Charge relay system
- KPSE 176:179 (≠ KAHP 184:187) binding
- G209 (= G221) binding
- GTST 230:233 (≠ SRAG 242:245) binding
- E252 (= E265) active site, Proton acceptor
- C286 (= C302) binding covalent; modified: Cysteine sulfenic acid (-SOH)
Sites not aligning to the query:
- 387 binding
- 464 active site, Charge relay system
4cazA Crystal structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa in complex with nadh
29% identity, 56% coverage: 6:304/533 of query aligns to 7:287/489 of 4cazA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302)
- 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 (≠ F155), G149 (= G156), W151 (≠ S158), N152 (= N159), K175 (= K184), E178 (≠ P187), G208 (= G221), G212 (≠ A225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249), E251 (= E265), L252 (≠ M266), C285 (= C302)
Sites not aligning to the query:
- active site: 386, 463
- 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: 386, 388
2woxA Betaine aldehyde dehydrogenase from pseudomonas aeruginosa with NAD(p) h-catalytic thiol adduct. (see paper)
29% identity, 56% coverage: 6:304/533 of query aligns to 7:287/489 of 2woxA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I148 (≠ F155), G149 (= G156), W151 (≠ S158), N152 (= N159), K175 (= K184), S177 (≠ H186), E178 (≠ P187), G208 (= G221), G212 (≠ A225), F226 (= F239), T227 (= T240), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249), E251 (= E265), L252 (≠ M266), C285 (= C302)
Sites not aligning to the query:
2wmeA Crystallographic structure of betaine aldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
29% identity, 56% coverage: 6:304/533 of query aligns to 7:287/489 of 2wmeA
- active site: N152 (= N159), K175 (= K184), E251 (= E265), C285 (= C302)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G149 (= G156), W151 (≠ S158), K175 (= K184), S177 (≠ H186), E178 (≠ P187), G208 (= G221), G212 (≠ A225), F226 (= F239), G228 (= G241), G229 (≠ S242), T232 (≠ G245), V236 (≠ L249)
Sites not aligning to the query:
5u0mA Fatty aldehyde dehydrogenase from marinobacter aquaeolei vt8 and cofactor complex (see paper)
27% identity, 74% coverage: 2:393/533 of query aligns to 1:358/488 of 5u0mA
- active site: N148 (= N159), K171 (= K184), E246 (= E265), C280 (= C302)
- binding nicotinamide-adenine-dinucleotide: F144 (= F155), Y147 (≠ S158), N148 (= N159), K171 (= K184), S173 (≠ H186), E174 (≠ P187), G207 (≠ A225), T222 (= T240), G223 (= G241), S224 (= S242), V227 (≠ G245), E246 (= E265), M247 (= M266), G248 (≠ S267), C280 (= C302)
Sites not aligning to the query:
5u0lA X-ray crystal structure of fatty aldehyde dehydrogenase enzymes from marinobacter aquaeolei vt8 complexed with a substrate (see paper)
27% identity, 74% coverage: 2:393/533 of query aligns to 1:358/488 of 5u0lA
Sites not aligning to the query:
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
26% identity, 88% coverage: 24:493/533 of query aligns to 491:945/959 of 5ur2B
Sites not aligning to the query:
- binding N-propargylglycine-modified flavin adenine dinucleotide: 174, 215, 216, 249, 278, 279, 280, 281, 283, 300, 301, 302, 303, 306, 329, 330, 331, 332, 356, 357, 358, 379, 398, 403, 405
Q8NMB0 Vanillin dehydrogenase; Aromatic aldehyde dehydrogenase; EC 1.2.1.67; EC 1.2.1.64; EC 1.2.1.96 from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
27% identity, 90% coverage: 8:488/533 of query aligns to 14:473/484 of Q8NMB0
- N157 (= N159) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 2.3-fold decreased affinity for vanillin compared to the wild type.
- K180 (= K184) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 11-fold decreased affinity for NADP(+) and 5-fold decreased affinity for vanillin compared to the wild type.
- E199 (= E206) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 78% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 5-fold decreased affinity for NAD(+), 2.5-fold decreased affinity for NADP(+) and 1.5-fold decreased affinity for vanillin compared to the wild type.
- E258 (= E265) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). 24% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 3.5-fold decreased affinity for NAD(+), 5-fold decreased affinity for NADP(+) and 3.7-fold decreased affinity for vanillin compared to the wild type.
- C292 (= C302) mutation to A: Less than 50% of the activity of the wild-type with vanillin as substrate in the presence of NAD(+). Less than 10% of the activity of the wild-type with vanillin as substrate in the presence of NADP(+). 4.5-fold decreased affinity for NAD(+), 7-fold decreased affinity for NADP(+) and 8-fold decreased affinity for vanillin compared to the wild type.
3ju8A Crystal structure of succinylglutamic semialdehyde dehydrogenase from pseudomonas aeruginosa.
29% identity, 55% coverage: 9:303/533 of query aligns to 7:280/486 of 3ju8A
- active site: N147 (= N159), K170 (= K184), E245 (= E265), C279 (= C302)
- binding nicotinamide-adenine-dinucleotide: G144 (= G156), Y146 (≠ S158), N147 (= N159), L152 (≠ V166), K170 (= K184), S172 (≠ H186), F220 (= F239), T221 (= T240), G222 (= G241), S223 (= S242), T226 (≠ G245), E245 (= E265), M246 (= M266), G247 (≠ S267), C279 (= C302)
Sites not aligning to the query:
3ty7B Crystal structure of aldehyde dehydrogenase family protein from staphylococcus aureus
24% identity, 62% coverage: 2:330/533 of query aligns to 4:307/454 of 3ty7B
Sites not aligning to the query:
4itbA Structure of bacterial enzyme in complex with cofactor and substrate (see paper)
28% identity, 53% coverage: 21:302/533 of query aligns to 2:261/453 of 4itbA
- active site: N130 (= N159), K153 (= K184), E227 (= E265), C261 (= C302)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: V126 (vs. gap), M127 (vs. gap), P128 (vs. gap), W129 (≠ S158), N130 (= N159), K153 (= K184), A155 (≠ P190), S156 (≠ G191), A186 (≠ G221), V189 (≠ I224), G205 (= G241), S206 (= S242), A209 (≠ G245), S212 (≠ A248), L228 (≠ M266), C261 (= C302)
- binding 4-oxobutanoic acid: E227 (= E265), C261 (= C302)
Sites not aligning to the query:
4v37A Crystal structure of betaine aldehyde dehydrogenase from spinach showing a thiohemiacetal with 3-aminopropionaldehyde
28% identity, 48% coverage: 21:275/533 of query aligns to 23:265/495 of 4v37A
- active site: N157 (= N159), K180 (= K184), E255 (= E265)
- binding nicotinamide-adenine-dinucleotide: I153 (≠ F155), S154 (≠ G156), P155 (≠ A157), W156 (≠ S158), N157 (= N159), M162 (≠ V166), K180 (= K184), S182 (≠ H186), E183 (≠ P187), G213 (= G221), G217 (≠ A225), A218 (≠ Q226), T232 (= T240), G233 (= G241), S234 (= S242), T237 (≠ G245), E255 (= E265), L256 (≠ M266)
Sites not aligning to the query:
P17202 Aminoaldehyde dehydrogenase BADH; 4-trimethylammoniobutyraldehyde dehydrogenase BADH; Aminobutyraldehyde dehydrogenase BADH; Betaine aldehyde dehydrogenase; SoBADH; EC 1.2.1.-; EC 1.2.1.47; EC 1.2.1.19; EC 1.2.1.8 from Spinacia oleracea (Spinach) (see 3 papers)
28% identity, 48% coverage: 21:275/533 of query aligns to 25:267/497 of P17202
- I28 (= I24) binding
- D96 (≠ E91) binding
- SPW 156:158 (≠ GAS 156:158) binding
- Y160 (≠ F160) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-(trimethylamino)butanal.
- W167 (≠ G169) mutation to A: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- KPSE 182:185 (≠ KAHP 184:187) binding
- L186 (≠ A188) binding
- SSAT 236:239 (≠ SRAG 242:245) binding
- V251 (≠ S257) binding in other chain
- L258 (≠ M266) binding
Sites not aligning to the query:
- 285 W→A: Decreases binding affinity for betaine aldehyde.
- 390 binding
- 441 A→I: Decreases binding affinity for betaine aldehyde; increases binding affinity for 4-aminobutanal.
- 450 C→S: Loss of partial inactivation by betaine aldehyde in the absence of NAD(+).
- 456 binding ; W→A: Decreases binding affinity for betaine aldehyde.
- 460 binding
4u3wA X-ray crystal structure of 2-aminomuconate 6-semialdehyde dehydrogenase from burkholderia cenocepacia
30% identity, 52% coverage: 57:335/533 of query aligns to 55:325/485 of 4u3wA
Sites not aligning to the query:
2w8rA The crystal structure of human ssadh in complex with NAD+ (see paper)
27% identity, 48% coverage: 55:308/533 of query aligns to 59:298/485 of 2w8rA
Sites not aligning to the query:
2w8qA The crystal structure of human ssadh in complex with ssa. (see paper)
27% identity, 48% coverage: 55:308/533 of query aligns to 59:298/485 of 2w8qA
Sites not aligning to the query:
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)
27% identity, 48% coverage: 55:308/533 of query aligns to 109:348/535 of P51649
- G176 (= G120) to R: in SSADHD; <1% of activity; dbSNP:rs72552281
- H180 (≠ G124) to Y: 83% of activity; dbSNP:rs2760118
- P182 (= P129) to L: 48% of activity; dbSNP:rs3765310
- R213 (≠ A167) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- C223 (= C179) to Y: in SSADHD; 5% of activity; dbSNP:rs72552282
- KPAE 228:231 (≠ KAHP 184:187) binding
- T233 (≠ H189) to M: in SSADHD; 4% of activity; dbSNP:rs1326526453
- A237 (≠ S193) to S: 65% of activity; dbSNP:rs62621664
- N255 (≠ S215) to S: in SSADHD; 17% of activity; dbSNP:rs145087265
- G268 (≠ A225) to E: in SSADHD; <1% of activity; dbSNP:rs375628463
- GSTTTG 284:289 (≠ GSRAGG 241:246) binding
- R334 (vs. gap) binding ; mutation to A: Reduces catalytic activity to less than 15% of wild-type.
- N335 (≠ T295) to K: in SSADHD; 1% of activity; dbSNP:rs72552283
- C340 (≠ Q300) modified: Disulfide link with 342, In inhibited form
- C342 (= C302) modified: Disulfide link with 340, In inhibited form; mutation to A: Loss of regulation by redox state.
Sites not aligning to the query:
- 36 G → R: no effect on succinate-semialdehyde dehydrogenase activity; dbSNP:rs4646832
- 93 C → F: in SSADHD; 3% of activity; dbSNP:rs765561257
- 372 natural variant: N -> S
- 382 P → L: in SSADHD; 2% of activity
- 406 V → I: in dbSNP:rs143741652
- 409 G → D: in SSADHD; <1% of activity; dbSNP:rs118203984
- 498 binding ; S→A: Reduces catalytic activity to less than 15% of wild-type.
- 533 G → R: in SSADHD; <1% of activity; dbSNP:rs72552284
7w5nA The crystal structure of the reduced form of gluconobacter oxydans wsh-004 sndh (see paper)
28% identity, 50% coverage: 39:304/533 of query aligns to 43:292/492 of 7w5nA
Sites not aligning to the query:
5x5uA Crystal structure of alpha-ketoglutarate-semialdehyde dehydrogenase (kgsadh) complexed with NAD (see paper)
30% identity, 57% coverage: 6:309/533 of query aligns to 6:290/476 of 5x5uA
- active site: N151 (= N159), K174 (= K184), E249 (= E265), C283 (= C302)
- binding glycerol: D15 (≠ R15), A16 (≠ G16), A17 (≠ T17), G19 (= G19)
- binding nicotinamide-adenine-dinucleotide: P149 (≠ A157), P207 (≠ G221), A208 (≠ L222), S211 (≠ A225), G227 (= G241), S228 (= S242), V231 (≠ G245)
Sites not aligning to the query:
Query Sequence
>RR42_RS23090 FitnessBrowser__Cup4G11:RR42_RS23090
MNLTGELLIGRQSVRGTHGEIRAIDPASGETLAPAFGGATRAQLDQACALAAQAFDGYRE
TPLAQRAALLEKIAANLLALGDALIARCVSESGLPRARIEGELGRTMSQLRLFAGVVRRG
DFLGLRIDPAQPQRMPLPRVDLRLRHIALGPVAVFGASNFPLAFSVAGGDTASALAAGCP
VVVKAHPAHPGTSELVGRAIQKAVEELGLPEGTFSLLFDSGLEIAQGLVSDHRIKAVGFT
GSRAGGTALMQLAAARSEPIPVYAEMSSINPVLLFPHALGNRADAIGKAFAASLTLGAGQ
FCTNPGLILAVDGPDLERFLAAAEAAIAQIPASTMLTPGIHRAYGAGVETLGCHPQVSTV
ARGQAGAQYQGQAALFSTTAQAFLEHEALRAEVFGAASLVVRCPDLATMQRVVESLEGQL
TAAIHIDEADYDTARSFLPALERRVGRILVNGFATGVEVSHAMVHGGPYPSTSDGRSTSV
GSLAIARFLRPVCYQDMPAALLPQALRAGNPLGLAVRVDGEMQPGHQPVAHTG
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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