SitesBLAST
Comparing CA265_RS16605 FitnessBrowser__Pedo557:CA265_RS16605 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)
O74766 Probable delta-1-pyrroline-5-carboxylate dehydrogenase; P5C dehydrogenase; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
52% identity, 98% coverage: 6:539/544 of query aligns to 7:545/548 of O74766
- S391 (≠ Q385) modified: Phosphoserine
- S394 (≠ K388) modified: Phosphoserine
- S396 (≠ K390) modified: Phosphoserine
4lemC Crystal structure of the delta-pyrroline-5-carboxylate dehydrogenase from mycobacterium tuberculosis (see paper)
52% identity, 99% coverage: 7:544/544 of query aligns to 7:544/544 of 4lemC
- active site: N191 (= N191), K213 (= K213), E294 (= E294), C328 (= C328), E426 (= E426), A511 (= A511)
- binding cobalamin: I187 (≠ L187), F247 (≠ P247), H273 (≠ E273)
- binding magnesium ion: A386 (= A386), K387 (= K387), A389 (≠ D389), V392 (= V392)
4ihiA Crystal structure of the delta-pyrroline-5-carboxylate dehydrogenase from mycobacterium tuberculosis bound with NAD (see paper)
52% identity, 99% coverage: 7:542/544 of query aligns to 6:534/535 of 4ihiA
- active site: N190 (= N191), K212 (= K213), E293 (= E294), C327 (= C328), E418 (≠ K419), A503 (= A511)
- binding nicotinamide-adenine-dinucleotide: I186 (≠ L187), T187 (= T188), P188 (= P189), F189 (= F190), N190 (= N191), I194 (= I195), K212 (= K213), S214 (≠ A215), G245 (= G246), S249 (≠ G250), T264 (= T265), G265 (= G266), S266 (= S267), T269 (≠ V270), E293 (= E294), T294 (= T295), C327 (= C328), F420 (= F428)
P30038 Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; P5C dehydrogenase; Aldehyde dehydrogenase family 4 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Homo sapiens (Human) (see 5 papers)
48% identity, 97% coverage: 13:541/544 of query aligns to 34:562/563 of P30038
- C348 (= C328) active site, Nucleophile
- S352 (= S332) to L: in HYRPRO2; allele ALDH4A1*3; loss of enzyme activity; dbSNP:rs137852937; mutation to A: Reduced affinity for NAD. No effect on enzyme activity.
- V470 (≠ I449) to I: in dbSNP:rs2230709
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 16 P → L: in allele ALDH4A1*4; dbSNP:rs146450609
3v9hA Crystal structure of human 1-pyrroline-5-carboxylate dehydrogenase mutant s352a (see paper)
48% identity, 97% coverage: 13:541/544 of query aligns to 12:540/541 of 3v9hA
Q8CHT0 Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial; P5C dehydrogenase; Aldehyde dehydrogenase family 4 member A1; L-glutamate gamma-semialdehyde dehydrogenase; EC 1.2.1.88 from Mus musculus (Mouse) (see paper)
47% identity, 97% coverage: 12:541/544 of query aligns to 32:561/562 of Q8CHT0
- E313 (= E294) active site, Proton acceptor
- C347 (= C328) active site, Nucleophile
4e3xB Crystal structure of mus musculus 1-pyrroline-5-carboxylate dehydrogenase cryoprotected in proline (see paper)
47% identity, 97% coverage: 13:541/544 of query aligns to 17:545/546 of 4e3xB
- active site: N194 (= N191), K216 (= K213), E297 (= E294), C331 (= C328), E430 (= E426), P515 (≠ A511)
- binding proline: F193 (= F190), F195 (= F192), K275 (≠ Q272), L285 (≠ I282), D286 (≠ H283), F288 (≠ Y285), T290 (≠ S287), F291 (≠ Y288), C331 (= C328), S332 (= S329), D376 (= D372), G495 (= G491), S496 (≠ A492), F503 (= F499), A508 (≠ G504)
4lh3A Structure of mouse 1-pyrroline-5-carboxylate dehydrogenase (aldh4a1) complexed with glutarate (see paper)
47% identity, 97% coverage: 13:541/544 of query aligns to 4:532/533 of 4lh3A
- active site: N181 (= N191), K203 (= K213), E284 (= E294), C318 (= C328), E417 (= E426), P502 (≠ A511)
- binding glutaric acid: F182 (= F192), K317 (= K327), C318 (= C328), S319 (= S329), G482 (= G491), S483 (≠ A492), F490 (= F499)
4lh0A Structure of mouse 1-pyrroline-5-carboxylate dehydrogenase (aldh4a1) complexed with glyoxylate (see paper)
47% identity, 97% coverage: 13:541/544 of query aligns to 4:532/533 of 4lh0A
7merA Structure of aldh4a1 complexed with trans-4-hydroxy-l-proline (see paper)
47% identity, 97% coverage: 13:541/544 of query aligns to 3:531/532 of 7merA
- active site: N180 (= N191), K202 (= K213), E283 (= E294), C317 (= C328), E416 (= E426), P501 (≠ A511)
- binding 4-hydroxyproline: E134 (= E144), F181 (= F192), I184 (= I195), S318 (= S329), G481 (= G491), S482 (≠ A492), F489 (= F499)
3v9lA Crystal structure of mouse 1-pyrroline-5-carboxylate dehydrogenase complexed with NAD+ (see paper)
47% identity, 97% coverage: 13:541/544 of query aligns to 5:533/534 of 3v9lA
- active site: N182 (= N191), K204 (= K213), E285 (= E294), C319 (= C328), E418 (= E426), P503 (≠ A511)
- binding nicotinamide-adenine-dinucleotide: I178 (≠ L187), S179 (≠ T188), N182 (= N191), I186 (= I195), K204 (= K213), G237 (= G246), P238 (= P247), G241 (= G250), F255 (= F264), T256 (= T265), G257 (= G266), S258 (= S267), T261 (≠ V270), E285 (= E294), G287 (= G296), C319 (= C328), E418 (= E426), F420 (= F428), F491 (= F499)
3v9kA Crystal structure of mouse 1-pyrroline-5-carboxylate dehydrogenase complexed with the product glutamate (see paper)
47% identity, 97% coverage: 13:541/544 of query aligns to 5:533/534 of 3v9kA
- active site: N182 (= N191), K204 (= K213), E285 (= E294), C319 (= C328), E418 (= E426), P503 (≠ A511)
- binding glutamic acid: F183 (= F192), K318 (= K327), C319 (= C328), S320 (= S329), G483 (= G491), S484 (≠ A492), F491 (= F499)
7mesA Structure of aldh4a1 complexed with trans-4-hydroxy-d-proline (see paper)
47% identity, 96% coverage: 13:532/544 of query aligns to 3:522/523 of 7mesA
- active site: N180 (= N191), K202 (= K213), E283 (= E294), C317 (= C328), E416 (= E426), P501 (≠ A511)
- binding nicotinamide-adenine-dinucleotide: I176 (≠ L187), S177 (≠ T188), K202 (= K213), G235 (= G246), G239 (= G250), F253 (= F264), S256 (= S267), T259 (≠ V270)
- binding (4S)-4-hydroxy-D-proline: T123 (≠ N133), Q126 (= Q136), E134 (= E144), F181 (= F192), E311 (= E322), S318 (= S329), F356 (= F366), G481 (= G491), S482 (≠ A492), F489 (= F499)
4oe4B Crystal structure of yeast aldh4a1 complexed with NAD+ (see paper)
49% identity, 86% coverage: 28:496/544 of query aligns to 4:467/481 of 4oe4B
- active site: N170 (= N191), K192 (= K213), E275 (= E294), C309 (= C328), E399 (= E426)
- binding nicotinamide-adenine-dinucleotide: V166 (≠ L187), S167 (≠ T188), P168 (= P189), F169 (= F190), K192 (= K213), P225 (≠ G246), S246 (= S267), V249 (= V270)
2j5nA 1-pyrroline-5-carboxylate dehydrogenase from thermus thermophirus with bound inhibitor glycine and NAD.
33% identity, 95% coverage: 13:530/544 of query aligns to 8:516/516 of 2j5nA
- active site: N184 (= N191), K207 (= K213), E288 (= E294), C322 (= C328), E417 (= E426), T497 (≠ A511)
- binding glycine: S323 (= S329), G477 (= G491), A478 (= A492), F485 (= F499)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ L187), A181 (≠ T188), P182 (= P189), W183 (≠ F190), N184 (= N191), I189 (= I195), K207 (= K213), E210 (≠ D216), G240 (= G246), F258 (= F264), T259 (= T265), G260 (= G266), S261 (= S267), V264 (= V270), E288 (= E294), T289 (= T295), C322 (= C328), E417 (= E426), F419 (= F428)
2ej6A Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound d-proline
33% identity, 95% coverage: 13:530/544 of query aligns to 8:516/516 of 2ej6A
- active site: N184 (= N191), K207 (= K213), E288 (= E294), C322 (= C328), E417 (= E426), T497 (≠ A511)
- binding d-proline: E137 (= E144), F185 (= F192), S323 (= S329), G477 (= G491), A478 (= A492), F485 (= F499)
2eitA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-alanine and NAD
33% identity, 95% coverage: 13:530/544 of query aligns to 8:516/516 of 2eitA
- active site: N184 (= N191), K207 (= K213), E288 (= E294), C322 (= C328), E417 (= E426), T497 (≠ A511)
- binding alanine: S323 (= S329), G477 (= G491), A478 (= A492), F485 (= F499)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ L187), A181 (≠ T188), W183 (≠ F190), N184 (= N191), I189 (= I195), K207 (= K213), E210 (≠ D216), G240 (= G246), E241 (≠ P247), G244 (= G250), F258 (= F264), T259 (= T265), G260 (= G266), S261 (= S267), V264 (= V270), E288 (= E294), G290 (= G296), C322 (= C328), E417 (= E426), F419 (= F428)
2eiiA Crystal analysis of delta1-pyrroline-5-carboxylate dehydrogenase from thermus thermophilus with bound l-valine and NAD.
33% identity, 95% coverage: 13:530/544 of query aligns to 8:516/516 of 2eiiA
- active site: N184 (= N191), K207 (= K213), E288 (= E294), C322 (= C328), E417 (= E426), T497 (≠ A511)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ L187), A181 (≠ T188), P182 (= P189), W183 (≠ F190), N184 (= N191), I189 (= I195), K207 (= K213), E210 (≠ D216), G240 (= G246), E241 (≠ P247), G244 (= G250), F258 (= F264), T259 (= T265), G260 (= G266), S261 (= S267), V264 (= V270), E288 (= E294), T289 (= T295), C322 (= C328), E417 (= E426), F419 (= F428)
- binding valine: E137 (= E144), F185 (= F192), S323 (= S329), G477 (= G491), A478 (= A492), F485 (= F499)
2ehuA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NAD and inhibitor l-serine
33% identity, 95% coverage: 13:530/544 of query aligns to 8:516/516 of 2ehuA
- active site: N184 (= N191), K207 (= K213), E288 (= E294), C322 (= C328), E417 (= E426), T497 (≠ A511)
- binding nicotinamide-adenine-dinucleotide: I180 (≠ L187), A181 (≠ T188), P182 (= P189), W183 (≠ F190), N184 (= N191), I189 (= I195), K207 (= K213), E210 (≠ D216), G240 (= G246), F258 (= F264), T259 (= T265), G260 (= G266), S261 (= S267), V264 (= V270), E288 (= E294), T289 (= T295), C322 (= C328), E417 (= E426), F419 (= F428)
- binding serine: F185 (= F192), C322 (= C328), S323 (= S329), G477 (= G491), A478 (= A492), F485 (= F499)
2ehqA Crystal analysis of 1-pyrroline-5-carboxylate dehydrogenase from thermus with bound NADP (see paper)
33% identity, 95% coverage: 13:530/544 of query aligns to 8:516/516 of 2ehqA
- active site: N184 (= N191), K207 (= K213), E288 (= E294), C322 (= C328), E417 (= E426), T497 (≠ A511)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I180 (≠ L187), A181 (≠ T188), P182 (= P189), W183 (≠ F190), N184 (= N191), I189 (= I195), K207 (= K213), A209 (= A215), E210 (≠ D216), V239 (≠ D245), G240 (= G246), E241 (≠ P247), F258 (= F264), T259 (= T265), G260 (= G266), S261 (= S267), V264 (= V270), E288 (= E294), T289 (= T295), C322 (= C328), E417 (= E426), F419 (= F428)
Query Sequence
>CA265_RS16605 FitnessBrowser__Pedo557:CA265_RS16605
MLKGFFNVPTPVNEPINSYAPGTKERSLLKEAIADARSKQLDIPMFIGGQEVHTKNKKKV
VAPHDHQHVLATFSYGDKSHVKQAIDAALAAKADWEALAWEHRAAIFMKAADLIATKYRY
QINAATMLGQSKNAYQAEIDAACELVDFLRFNVSYMQDIYGQQPPVSPNGMWNRTEQRPL
EGFIFALTPFNFTAIAGNLPACVAMMGNVVVWKPADTQVYAANVIMQIFREAGLPDGVIN
LIFADGPEVGDVVFNHADFAGIHFTGSTKVFQEIWKTIGTNIHKYKSYPRIVGETGGKDF
ILVHPSADVAASATAIVRGAFEYQGQKCSAASRTYIPKSLWPEIKKLMIRDLASFKMGGT
EDFSNFINAVIDERSFDKLAKYIDQAKKDKGVEVIAGGNYDKSKGYFIEPTILVVDDPKY
TTMCEELFGPVLSVYVYEDQEFDQVLEIIDTTSPYALTGAILSQDRYAIEKASYALRNSA
GNFYINDKCTGAVVGQQPFGGARGSGTNDKAGAMINLLRWVSPRTIKETFNPPTDYRYPF
LAED
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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