SitesBLAST
Comparing RR42_RS23750 FitnessBrowser__Cup4G11:RR42_RS23750 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2eiwA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-proline
27% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2eiwA
Sites not aligning to the query:
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2j5nA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding glycine: S323 (≠ T344), G477 (= G511), A478 (≠ G512), F485 (= F521)
- binding nicotinamide-adenine-dinucleotide: I180 (= I203), A181 (≠ G204), P182 (≠ C205), W183 (≠ C206), N184 (≠ T207), I189 (≠ N212), K207 (= K230), E210 (≠ P233), G240 (= G270), F258 (= F287), T259 (= T288), G260 (= G289), S261 (= S290), V264 (vs. gap), E288 (= E309), T289 (≠ K310), C322 (= C343), E417 (= E448), F419 (= F450)
2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2ej6A
Sites not aligning to the query:
2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2eitA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding alanine: S323 (≠ T344), G477 (= G511), A478 (≠ G512), F485 (= F521)
- binding nicotinamide-adenine-dinucleotide: I180 (= I203), A181 (≠ G204), W183 (≠ C206), N184 (≠ T207), I189 (≠ N212), K207 (= K230), E210 (≠ P233), G240 (= G270), E241 (≠ A271), G244 (≠ Q274), F258 (= F287), T259 (= T288), G260 (= G289), S261 (= S290), V264 (vs. gap), E288 (= E309), G290 (≠ A311), C322 (= C343), E417 (= E448), F419 (= F450)
2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2eiiA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding nicotinamide-adenine-dinucleotide: I180 (= I203), A181 (≠ G204), P182 (≠ C205), W183 (≠ C206), N184 (≠ T207), I189 (≠ N212), K207 (= K230), E210 (≠ P233), G240 (= G270), E241 (≠ A271), G244 (≠ Q274), F258 (= F287), T259 (= T288), G260 (= G289), S261 (= S290), V264 (vs. gap), E288 (= E309), T289 (≠ K310), C322 (= C343), E417 (= E448), F419 (= F450)
- binding valine: F185 (= F208), S323 (≠ T344), G477 (= G511), A478 (≠ G512), F485 (= F521)
Sites not aligning to the query:
2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2ehuA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding nicotinamide-adenine-dinucleotide: I180 (= I203), A181 (≠ G204), P182 (≠ C205), W183 (≠ C206), N184 (≠ T207), I189 (≠ N212), K207 (= K230), E210 (≠ P233), G240 (= G270), F258 (= F287), T259 (= T288), G260 (= G289), S261 (= S290), V264 (vs. gap), E288 (= E309), T289 (≠ K310), C322 (= C343), E417 (= E448), F419 (= F450)
- binding serine: F185 (= F208), C322 (= C343), S323 (≠ T344), G477 (= G511), A478 (≠ G512), F485 (= F521)
2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP (see paper)
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2ehqA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I180 (= I203), A181 (≠ G204), P182 (≠ C205), W183 (≠ C206), N184 (≠ T207), I189 (≠ N212), K207 (= K230), A209 (≠ H232), E210 (≠ P233), V239 (≠ D269), G240 (= G270), E241 (≠ A271), F258 (= F287), T259 (= T288), G260 (= G289), S261 (= S290), V264 (vs. gap), E288 (= E309), T289 (≠ K310), C322 (= C343), E417 (= E448), F419 (= F450)
2bhqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound product glutamate. (see paper)
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2bhqA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding glutamic acid: F185 (= F208), I189 (≠ N212), K321 (≠ M342), C322 (= C343), S323 (≠ T344), T476 (= T510), G477 (= G511), A478 (≠ G512), F485 (= F521)
2bhpA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD. (see paper)
26% identity, 61% coverage: 195:535/560 of query aligns to 172:499/516 of 2bhpA
- active site: N184 (≠ T207), K207 (= K230), E288 (= E309), C322 (= C343), E417 (= E448), T497 (≠ A533)
- binding nicotinamide-adenine-dinucleotide: I180 (= I203), A181 (≠ G204), P182 (≠ C205), W183 (≠ C206), N184 (≠ T207), I189 (≠ N212), K207 (= K230), E210 (≠ P233), G240 (= G270), E241 (≠ A271), F258 (= F287), T259 (= T288), G260 (= G289), S261 (= S290), V264 (vs. gap), E288 (= E309), T289 (≠ K310), C322 (= C343), E417 (= E448), F419 (= F450)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
24% identity, 73% coverage: 120:528/560 of query aligns to 563:957/983 of 3hazA
- active site: N652 (≠ T207), K675 (= K230), E752 (= E309), C786 (= C343), E878 (= E448)
- binding nicotinamide-adenine-dinucleotide: I648 (= I203), S649 (≠ G204), P650 (≠ C205), W651 (≠ C206), N652 (≠ T207), I657 (≠ N212), K675 (= K230), P676 (= P231), A677 (≠ H232), G708 (= G270), G711 (≠ V273), A712 (≠ Q274), T726 (= T288), G727 (= G289), S728 (= S290), V731 (≠ N293), I735 (≠ L297), E752 (= E309), T753 (≠ K310), C786 (= C343), E878 (= E448), F880 (= F450), F948 (≠ A519)
Sites not aligning to the query:
- active site: 960
- binding flavin-adenine dinucleotide: 272, 273, 306, 333, 335, 336, 337, 338, 339, 340, 358, 359, 360, 361, 364, 387, 388, 389, 390, 435, 460, 461
1ky8A Crystal structure of the non-phosphorylating glyceraldehyde-3- phosphate dehydrogenase (see paper)
25% identity, 49% coverage: 196:469/560 of query aligns to 155:414/499 of 1ky8A
- active site: N166 (≠ T207), K189 (= K230), E261 (≠ T308), C295 (= C343), E393 (= E448)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I203), T163 (≠ G204), F165 (≠ C206), N166 (≠ T207), K189 (= K230), S191 (≠ H232), I192 (≠ P233), P221 (≠ A266), G222 (= G270), A225 (≠ V273), E226 (≠ Q274), F239 (= F287), T240 (= T288), G241 (= G289), S242 (= S290), V245 (≠ N293), E261 (≠ T308), L262 (≠ E309), G263 (≠ K310), C295 (= C343), E393 (= E448), F395 (= F450)
Sites not aligning to the query:
O57693 NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde phosphate dehydrogenase (NAD(P)); GAPN; EC 1.2.1.90 from Thermoproteus tenax (see 2 papers)
25% identity, 49% coverage: 196:469/560 of query aligns to 157:416/501 of O57693
Sites not aligning to the query:
- 72 binding ; binding ; binding
- 79 binding ; binding ; binding
- 134 binding
- 154:155 binding ; binding
- 455:456 binding
1uxuA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
25% identity, 49% coverage: 196:469/560 of query aligns to 155:414/499 of 1uxuA
- active site: N166 (≠ T207), K189 (= K230), E261 (≠ T308), C295 (= C343), E393 (= E448)
- binding glyceraldehyde-3-phosphate: N166 (≠ T207), Y167 (≠ F208), R294 (≠ M342), C295 (= C343), D296 (= D354)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I203), T163 (≠ G204), P164 (≠ C205), F165 (≠ C206), K189 (= K230), S191 (≠ H232), I192 (≠ P233), P221 (≠ A266), G222 (= G270), E226 (≠ Q274), G241 (= G289), S242 (= S290), V245 (≠ N293), E393 (= E448), F395 (= F450)
Sites not aligning to the query:
1uxtA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
25% identity, 49% coverage: 196:469/560 of query aligns to 155:414/499 of 1uxtA
- active site: N166 (≠ T207), K189 (= K230), E261 (≠ T308), C295 (= C343), E393 (= E448)
- binding nicotinamide-adenine-dinucleotide: I162 (= I203), T163 (≠ G204), F165 (≠ C206), N166 (≠ T207), K189 (= K230), S191 (≠ H232), G222 (= G270), E226 (≠ Q274), T240 (= T288), G241 (= G289), S242 (= S290), V245 (≠ N293), E261 (≠ T308), G263 (≠ K310), C295 (= C343), E393 (= E448), F395 (= F450)
Sites not aligning to the query:
1uxrA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
25% identity, 49% coverage: 196:469/560 of query aligns to 155:414/499 of 1uxrA
- active site: N166 (≠ T207), K189 (= K230), E261 (≠ T308), C295 (= C343), E393 (= E448)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I203), T163 (≠ G204), F165 (≠ C206), N166 (≠ T207), K189 (= K230), S191 (≠ H232), I192 (≠ P233), P221 (≠ A266), G222 (= G270), A225 (≠ V273), E226 (≠ Q274), F239 (= F287), T240 (= T288), G241 (= G289), S242 (= S290), V245 (≠ N293), E261 (≠ T308), L262 (≠ E309), G263 (≠ K310), C295 (= C343), E393 (= E448), F395 (= F450)
Sites not aligning to the query:
1uxqA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
25% identity, 49% coverage: 196:469/560 of query aligns to 155:414/499 of 1uxqA
- active site: N166 (≠ T207), K189 (= K230), E261 (≠ T308), C295 (= C343), E393 (= E448)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I203), T163 (≠ G204), P164 (≠ C205), F165 (≠ C206), N166 (≠ T207), K189 (= K230), S191 (≠ H232), I192 (≠ P233), P221 (≠ A266), G222 (= G270), A225 (≠ V273), E226 (≠ Q274), T240 (= T288), G241 (= G289), S242 (= S290), V245 (≠ N293), E261 (≠ T308), L262 (≠ E309), G263 (≠ K310), C295 (= C343), E393 (= E448), F395 (= F450)
Sites not aligning to the query:
1uxnA Structural basis for allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (gapn) from thermoproteus tenax (see paper)
25% identity, 49% coverage: 196:469/560 of query aligns to 155:414/499 of 1uxnA
- active site: N166 (≠ T207), K189 (= K230), E261 (≠ T308), C295 (= C343), E393 (= E448)
- binding adenosine monophosphate: Y182 (≠ T223)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I162 (= I203), T163 (≠ G204), F165 (≠ C206), N166 (≠ T207), K189 (= K230), S191 (≠ H232), I192 (≠ P233), P221 (≠ A266), G222 (= G270), E226 (≠ Q274), F239 (= F287), T240 (= T288), G241 (= G289), S242 (= S290), V245 (≠ N293), E261 (≠ T308), L262 (≠ E309), G263 (≠ K310), C295 (= C343), E393 (= E448), F395 (= F450)
Sites not aligning to the query:
2opxA Crystal structure of lactaldehyde dehydrogenase from escherichia coli
26% identity, 53% coverage: 197:490/560 of query aligns to 139:420/477 of 2opxA
- active site: N151 (≠ T207), K174 (= K230), E249 (= E309), C283 (= C343), E381 (= E448)
- binding (3alpha,5beta,12alpha)-3,12-dihydroxycholan-24-oic acid: F152 (= F208), N284 (≠ T344), F312 (vs. gap), G313 (≠ S381), R318 (≠ A386), D320 (≠ E388), I321 (≠ L389), A322 (vs. gap), Y362 (≠ S429)
Sites not aligning to the query:
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, 53% coverage: 189:487/560 of query aligns to 139:422/484 of Q8NMB0
- N157 (≠ T207) 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 (= K230) 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 (= E252) 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 (= E309) 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 (= C343) 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.
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
24% identity, 73% coverage: 120:528/560 of query aligns to 554:948/973 of 6bsnA
- active site: N643 (≠ T207), E743 (= E309), A777 (≠ C343)
- binding proline: M630 (≠ V194), W642 (≠ C206), F644 (= F208), G718 (= G289), R776 (≠ M342), S778 (≠ T344), F871 (= F450), I930 (≠ T510), G931 (= G511), A932 (≠ G512), F939 (≠ A519)
Sites not aligning to the query:
- active site: 951
- binding dihydroflavine-adenine dinucleotide: 269, 270, 303, 330, 332, 333, 334, 335, 336, 337, 355, 356, 357, 358, 361, 384, 385, 386, 387, 432, 457, 458
- binding proline: 958, 959, 961
Query Sequence
>RR42_RS23750 FitnessBrowser__Cup4G11:RR42_RS23750
MNHALFEKHEKTLAQALDAIRTRGYWSPFNEMPSPRTYGETAAADGEAAFKAQLGQPFVL
EQAGSSGTVGAEHSPFGFALNIGYPNAEPDALIAAAQAAQLQFRKAGPKAWVGVSLEILA
RLNQASFEIAHSVMHTTGQAFMMAFQAGGPHAQDRALEAIAYAWDAMRDIPQTAYWEKPQ
GKNPPLAMEKRFTVVPRGIGLVIGCCTFPTWNSYPGLFADLATGNAVIVKPHPAAILPLA
ITVRIARQVLEEAGFDPNVVTLMATAPNDGALVQALATRDEIRLIDFTGSTANGDWLETH
ALQAQVYTEKAGVNQIVIDSADELKAVSRNIAFSLALYSGQMCTAPQNIYVPRDGIKTAQ
GTVPFEEVAQSIADAVQKLTSDPAKAVELIGAIQNKGVLDRIEQVTKLGVPLLASQRLVH
PAYPEASVSTPVLLKLDARRDEDTFTQEWFGPIAFVIATDSTRHSLELAARIARTRGALT
LSVYSTDEQVLDAADEAAVSGGVALSVNLTGGVFVNQSAAFSDFHATGANPAANASLADT
AFVANRFRVVQSRRHVPQRT
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