SitesBLAST
Comparing WP_047215054.1 NCBI__GCF_001931675.1:WP_047215054.1 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)
Q88JH0 Quinoprotein alcohol dehydrogenase PedH; Lanthanide-dependent pyrroloquinoline quinone-dependent alcohol dehydrogenase; Lanthanide-dependent PQQ-ADH; EC 1.1.2.- from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
40% identity, 97% coverage: 18:574/575 of query aligns to 9:585/595 of Q88JH0
- Q87 (≠ E95) binding pyrroloquinoline quinone
- C131 (= C141) modified: Disulfide link with 132
- C132 (= C142) modified: Disulfide link with 131
- R137 (= R147) binding pyrroloquinoline quinone
- S181 (≠ T191) binding pyrroloquinoline quinone
- G197 (= G207) binding pyrroloquinoline quinone
- G198 (= G208) binding pyrroloquinoline quinone
- E199 (= E209) binding Pr(3+)
- W263 (= W257) binding pyrroloquinoline quinone
- N281 (= N275) binding Pr(3+)
- D323 (= D317) binding Pr(3+)
- D325 (= D319) binding Pr(3+)
- R350 (= R344) binding pyrroloquinoline quinone
- F412 (= F399) mutation to I: In contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA); when associated with Ser-561 or Gln-561.; mutation to V: High decrease in affinity for ethanol, and in contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA) and can also oxidize 5-(hydroxymethyl)furfural (HMF) and 5-formylfurfural (FFF); when associated with Ala-561.
- N417 (= N404) binding pyrroloquinoline quinone
- W493 (≠ N481) binding pyrroloquinoline quinone
- A557 (= A546) binding pyrroloquinoline quinone
- W561 (= W550) mutation to A: High decrease in affinity for ethanol, and in contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA) and can also oxidize 5-(hydroxymethyl)furfural (HMF) and 5-formylfurfural (FFF); when associated with Val-412.; mutation W->S,Q: In contrast to wild-type, this mutant is able to oxidize 5-(hydroxymethyl)furoic acid (HMFA) into 5-formylfuroic acid (FFA); when associated with Ile-412.
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
42% identity, 89% coverage: 61:574/575 of query aligns to 26:558/562 of 6zcvA
- active site: E172 (= E209), N254 (= N275), D296 (= D317)
- binding calcium ion: N161 (≠ K198), K163 (≠ S200), P278 (= P299), D279 (≠ A300)
- binding pyrroloquinoline quinone: Q60 (≠ E95), C104 (= C141), C105 (= C142), I108 (≠ V145), R110 (= R147), S154 (≠ T191), G170 (= G207), G171 (= G208), E172 (= E209), W236 (= W257), D298 (= D319), R323 (= R344), N390 (= N404), W466 (≠ N481), G529 (= G545), A530 (= A546)
C5AXV8 Lanthanide-dependent ethanol dehydrogenase; Lanthanide-dependent EtDH; Ln-dependent EtDH; Lanthanide-dependent formaldehyde dehydrogenase; PQQ-dependent ethanol dehydrogenase; EC 1.1.2.-; EC 1.2.2.- from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) (see paper)
40% identity, 98% coverage: 14:574/575 of query aligns to 8:582/587 of C5AXV8
- D319 (= D319) mutation to S: Loss of efficient ethanol oxidation with La(3+).
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)
39% identity, 90% coverage: 53:572/575 of query aligns to 53:613/623 of Q9Z4J7
- E95 (= E95) binding pyrroloquinoline quinone
- 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 pyrroloquinoline quinone
- T189 (= T191) binding pyrroloquinoline quinone
- HGS 207:209 (≠ VGS 203:205) binding pyrroloquinoline quinone
- E213 (= E209) binding Ca(2+)
- N300 (= N275) binding Ca(2+)
- D350 (= D317) binding Ca(2+)
- R378 (= R344) binding pyrroloquinoline quinone
- W523 (≠ N481) binding pyrroloquinoline quinone
- A587 (= A546) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:34 signal peptide
- 45 binding Ca(2+)
- 48 binding Ca(2+)
- 51 binding Ca(2+)
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
39% 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 (= T191), S176 (= S206), G177 (= G207), D178 (≠ G208), W248 (= W257), R344 (= R344), N413 (= N404), W414 (= W405), W489 (≠ N481), G552 (= G545), A553 (= A546)
Sites not aligning to the query:
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)
38% identity, 92% coverage: 45:572/575 of query aligns to 53:596/708 of Q46444
- E101 (= E95) binding pyrroloquinoline quinone
- C147 (= C141) modified: Disulfide link with 148
- C148 (= C142) modified: Disulfide link with 147
- R153 (= R147) binding pyrroloquinoline quinone
- T198 (= T191) binding pyrroloquinoline quinone
- GA 214:215 (≠ GG 207:208) binding pyrroloquinoline quinone
- E216 (= E209) binding Ca(2+)
- T274 (≠ P255) binding pyrroloquinoline quinone
- N294 (= N275) binding Ca(2+)
- D339 (= D317) binding Ca(2+)
- K366 (≠ R344) binding pyrroloquinoline quinone
- NW 425:426 (= NW 404:405) binding pyrroloquinoline quinone
- V575 (≠ I549) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:31 signal peptide
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 678 binding axial binding residue
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
38% identity, 92% coverage: 45:572/575 of query aligns to 22:565/670 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 (= T191), G182 (≠ S206), G183 (= G207), A184 (≠ G208), E185 (= E209), T243 (≠ P255), W245 (= W257), D308 (= D317), K335 (≠ R344), N394 (= N404), W395 (= W405), W479 (= W480), G543 (= G545), V544 (≠ I549)
- 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
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
36% identity, 92% coverage: 45:572/575 of query aligns to 11:550/664 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 (= T191), G170 (≠ S206), 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, 92% coverage: 45:572/575 of query aligns to 33:572/690 of Q8GR64