SitesBLAST
Comparing H281DRAFT_00328 FitnessBrowser__Burk376:H281DRAFT_00328 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)
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
40% identity, 89% coverage: 61:572/575 of query aligns to 26:556/562 of 6zcvA
- active site: E172 (= E209), N254 (= N275), D296 (= D317)
- binding calcium ion: N161 (≠ D198), K163 (≠ A200), P278 (= P299), D279 (≠ K300)
- binding pyrroloquinoline quinone: Q60 (≠ E95), C104 (= C141), C105 (= C142), I108 (= I145), R110 (= R147), S154 (= S191), G170 (= G207), G171 (= G208), E172 (= E209), W236 (= W257), D298 (= D319), R323 (= R344), N390 (= N404), W466 (≠ N481), G529 (= G545), A530 (= A546)
Q9Z4J7 Quinoprotein ethanol dehydrogenase; QEDH; Quinoprotein alcohol dehydrogenase (cytochrome c); Quinoprotein alcohol dehydrogenase (cytochrome c550); EC 1.1.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
37% identity, 90% coverage: 53:572/575 of query aligns to 53:613/623 of Q9Z4J7
- E95 (= E95) binding
- C139 (= C141) modified: Disulfide link with 140
- CC 139:140 (= CC 141:142) mutation to AA: 15-fold decrease in catalytic activity with the natural electron acceptor cytochrome c550. Does not affect, or even increases, catalytic activity with artificial electron acceptors. Shows high decreased affinity for primary alcohols, while the affinity for the secondary alcohol 2-propanol is unaltered.
- C140 (= C142) modified: Disulfide link with 139
- R145 (= R147) binding
- T189 (≠ S191) binding
- HGS 207:209 (≠ VGS 203:205) binding
- E213 (= E209) binding
- N300 (= N275) binding
- D350 (= D317) binding
- R378 (= R344) binding
- W523 (≠ N481) binding
- A587 (= A546) binding
Sites not aligning to the query:
- 1:34 signal peptide
- 45 binding
- 48 binding
- 51 binding
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
37% identity, 90% coverage: 53:572/575 of query aligns to 19:579/582 of 1flgA
- active site: E179 (= E209), N266 (= N275), D316 (= D317)
- binding calcium ion: E179 (= E209), N266 (= N275), D316 (= D317)
- binding pyrroloquinoline quinone: E61 (= E95), C105 (= C141), C106 (= C142), R111 (= R147), T155 (≠ S191), S176 (≠ A206), G177 (= G207), D178 (≠ G208), W248 (= W257), R344 (= R344), N413 (= N404), W414 (= W405), W489 (≠ N481), G552 (= G545), A553 (= A546)
Sites not aligning to the query:
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
36% identity, 91% coverage: 52:573/575 of query aligns to 18:551/664 of 1kv9A
- active site: E173 (= E209), N250 (= N275), D295 (= D317)
- binding acetone: E173 (= E209), D295 (= D317)
- binding calcium ion: E173 (= E209), N250 (= N275), D295 (= D317)
- binding heme c: A101 (≠ F137), R102 (≠ K138)
- binding pyrroloquinoline quinone: E59 (= E95), C105 (= C141), C106 (= C142), R111 (= R147), T155 (≠ S191), G170 (≠ A206), A172 (≠ G208), E173 (= E209), T230 (≠ P255), W232 (= W257), K322 (≠ R344), N382 (= N404), W383 (= W405), W460 (= W480), V525 (≠ A546)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 623, 631, 633, 636
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
36% identity, 91% coverage: 52:573/575 of query aligns to 40:573/690 of Q8GR64
- E81 (= E95) binding
- C127 (= C141) modified: Disulfide link with 128
- C128 (= C142) modified: Disulfide link with 127
- R133 (= R147) binding
- T177 (≠ S191) binding
- GA 193:194 (≠ GG 207:208) binding
- E195 (= E209) binding
- T252 (≠ P255) binding
- N272 (= N275) binding
- D317 (= D317) binding
- K344 (≠ R344) binding
- NW 404:405 (= NW 404:405) binding
- V547 (≠ A546) binding
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
- 613 binding covalent
- 616 binding covalent
- 617 binding axial binding residue
- 655 binding axial binding residue
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
37% identity, 93% coverage: 40:572/575 of query aligns to 18:565/670 of 1kb0A
- active site: E185 (= E209), N263 (= N275), D308 (= D317)
- binding calcium ion: E185 (= E209), N263 (= N275), D308 (= D317)
- binding pyrroloquinoline quinone: E70 (= E95), C116 (= C141), C117 (= C142), R122 (= R147), T167 (≠ S191), G182 (≠ A206), G183 (= G207), A184 (≠ G208), E185 (= E209), T243 (≠ P255), W245 (= W257), D308 (= D317), K335 (≠ R344), N394 (= N404), W395 (= W405), W479 (= W480), G543 (= G545), V544 (≠ A546)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C141), C117 (= C142), E185 (= E209), D308 (= D317), P389 (≠ F399)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
Q46444 Quinohemoprotein alcohol dehydrogenase; QH-ADH; Alcohol dehydrogenase (azurin); PQQ-containing alcohol dehydrogenase; PQQ-dependent ADH; Quinohaemoprotein ethanol dehydrogenase type I; QH-EDHI; EC 1.1.9.1 from Comamonas testosteroni (Pseudomonas testosteroni) (see 3 papers)
37% identity, 93% coverage: 40:572/575 of query aligns to 49:596/708 of Q46444