SitesBLAST
Comparing Pf6N2E2_1752 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1752 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)
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
92% identity, 100% coverage: 1:725/726 of query aligns to 1:715/718 of Q4W6G0
- 1:29 (vs. 1:39, 54% identical) signal peptide
- C138 (= C148) modified: Disulfide link with 139
- C139 (= C149) modified: Disulfide link with 138
- R144 (= R154) binding
- T189 (= T199) binding
- GA 205:206 (= GA 215:216) binding
- E207 (= E217) binding
- T264 (= T274) binding
- N284 (= N294) binding
- D329 (= D339) binding
- K356 (= K366) binding
- W415 (= W425) binding
- DW 419:420 (= DW 429:430) binding
- C635 (= C645) binding covalent
- C638 (= C648) binding covalent
- H639 (= H649) binding axial binding residue
- M676 (= M686) binding axial binding residue
Sites not aligning to the query:
- 30:718 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH-IIG
1yiqA Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase adhiig from pseudomonas putida hk5. Compariison to the other quinohemoprotein alcohol dehydrogenase adhiib found in the same microorganism. (see paper)
94% identity, 94% coverage: 40:723/726 of query aligns to 1:684/684 of 1yiqA
- active site: E178 (= E217), N255 (= N294), D300 (= D339)
- binding calcium ion: E178 (= E217), N255 (= N294), D300 (= D339)
- binding heme c: Y605 (= Y644), C606 (= C645), Q608 (= Q647), C609 (= C648), H610 (= H649), L623 (= L662), L626 (= L665), K630 (= K669), F634 (= F673), I637 (= I676), L638 (= L677), R642 (= R681), D645 (= D684), G646 (= G685), M647 (= M686), P648 (= P687), F650 (= F689)
- binding pyrroloquinoline quinone: E63 (= E102), C109 (= C148), C110 (= C149), R115 (= R154), T160 (= T199), G175 (= G214), G176 (= G215), A177 (= A216), E178 (= E217), T235 (= T274), W237 (= W276), K327 (= K366), D390 (= D429), W391 (= W430), F477 (= F516), A542 (= A581)
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
50% identity, 92% coverage: 44:711/726 of query aligns to 1:658/664 of 1kv9A
- active site: E173 (= E217), N250 (= N294), D295 (= D339)
- binding acetone: E173 (= E217), D295 (= D339)
- binding calcium ion: E173 (= E217), N250 (= N294), D295 (= D339)
- binding heme c: A101 (= A144), R102 (≠ G145), F590 (≠ Y644), C591 (= C645), C594 (= C648), H595 (= H649), I605 (≠ L659), P606 (= P660), L608 (= L662), S611 (≠ L665), T615 (≠ K669), F619 (= F673), V623 (≠ L677), L631 (≠ D684), M633 (= M686), F636 (= F689)
- binding pyrroloquinoline quinone: E59 (= E102), C105 (= C148), C106 (= C149), R111 (= R154), T155 (= T199), G170 (= G214), A172 (= A216), E173 (= E217), T230 (= T274), W232 (= W276), K322 (= K366), N382 (≠ D429), W383 (= W430), W460 (≠ F516), V525 (≠ A581)
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
50% identity, 92% coverage: 46:711/726 of query aligns to 25:680/690 of Q8GR64
- E81 (= E102) binding
- C127 (= C148) modified: Disulfide link with 128
- C128 (= C149) modified: Disulfide link with 127
- R133 (= R154) binding
- T177 (= T199) binding
- GA 193:194 (= GA 215:216) binding
- E195 (= E217) binding
- T252 (= T274) binding
- N272 (= N294) binding
- D317 (= D339) binding
- K344 (= K366) binding
- NW 404:405 (≠ DW 429:430) binding
- V547 (≠ A581) binding
- C613 (= C645) binding covalent
- C616 (= C648) binding covalent
- H617 (= H649) binding axial binding residue
- M655 (= M686) binding axial binding residue
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
49% identity, 91% coverage: 46:705/726 of query aligns to 14:661/670 of 1kb0A
- active site: E185 (= E217), N263 (= N294), D308 (= D339)
- binding calcium ion: E185 (= E217), N263 (= N294), D308 (= D339)
- binding heme c: N598 (≠ Y644), C599 (= C645), C602 (= C648), H603 (= H649), L617 (= L662), M620 (≠ L665), F631 (≠ I676), A637 (≠ R681), R640 (≠ D684), M642 (= M686), P643 (= P687), F645 (= F689)
- binding pyrroloquinoline quinone: E70 (= E102), C116 (= C148), C117 (= C149), R122 (= R154), T167 (= T199), G182 (= G214), G183 (= G215), A184 (= A216), E185 (= E217), T243 (= T274), W245 (= W276), D308 (= D339), K335 (= K366), N394 (≠ D429), W395 (= W430), W479 (≠ F516), G543 (= G580), V544 (≠ A581)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C148), C117 (= C149), E185 (= E217), D308 (= D339), P389 (≠ F424)
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)
48% identity, 91% coverage: 46:705/726 of query aligns to 45:697/708 of Q46444
- E101 (= E102) binding
- C147 (= C148) modified: Disulfide link with 148
- C148 (= C149) modified: Disulfide link with 147
- R153 (= R154) binding
- T198 (= T199) binding
- GA 214:215 (= GA 215:216) binding
- E216 (= E217) binding
- T274 (= T274) binding
- N294 (= N294) binding
- D339 (= D339) binding
- K366 (= K366) binding
- NW 425:426 (≠ DW 429:430) binding
- V575 (≠ A581) binding
- C635 (= C645) binding covalent
- C638 (= C648) binding covalent
- H639 (= H649) binding axial binding residue
- M678 (= M686) binding axial binding residue
Sites not aligning to the query:
O05542 Alcohol dehydrogenase (quinone), dehydrogenase subunit; ADH; Alcohol dehydrogenase (quinone), acceptor subunit; Alcohol dehydrogenase (quinone), subunit I; Ethanol:Q2 reductase; G3-ADH subunit I; Quinohemoprotein alcohol dehydrogenase; Quinohemoprotein-cytochrome c complex; Ubiquinol oxidase; EC 1.1.5.5 from Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) (see paper)
45% identity, 91% coverage: 57:715/726 of query aligns to 50:725/757 of O05542
Sites not aligning to the query:
- 1:34 signal peptide
- 35 modified: Pyrrolidone carboxylic acid
8gy2A Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
45% identity, 91% coverage: 57:715/726 of query aligns to 16:691/723 of 8gy2A
- binding calcium ion: E181 (= E217), N263 (= N294), D308 (= D339)
- binding heme c: D104 (≠ G145), F618 (≠ Y644), C619 (= C645), C622 (= C648), H623 (= H649), L633 (= L659), P634 (= P660), L636 (= L662), S639 (≠ K664), V652 (≠ L677), Y660 (≠ D684), M662 (= M686), F665 (= F689)
- binding pyrroloquinoline quinone: C107 (= C148), C108 (= C149), D163 (≠ T199), G179 (= G215), A180 (= A216), E181 (= E217), W245 (= W276), N263 (= N294), D308 (= D339), K335 (= K366), F398 (≠ W430), W489 (≠ F516)
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
38% identity, 77% coverage: 46:606/726 of query aligns to 2:556/562 of 6zcvA
- active site: E172 (= E217), N254 (= N294), D296 (= D339)
- binding calcium ion: N161 (= N206), K163 (= K208), P278 (≠ A321), D279 (= D322)
- binding pyrroloquinoline quinone: Q60 (≠ E102), C104 (= C148), C105 (= C149), I108 (≠ V152), R110 (= R154), S154 (≠ T199), G170 (= G215), G171 (≠ A216), E172 (= E217), W236 (= W276), D298 (≠ T341), R323 (≠ K366), N390 (≠ D429), W466 (≠ N517), G529 (= G580), A530 (= A581)
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
37% identity, 74% coverage: 56:593/726 of query aligns to 9:560/563 of 6damA
- active site: E171 (= E217), N259 (= N294), D301 (= D339)
- binding pyrroloquinoline quinone: E55 (= E102), C103 (= C148), C104 (= C149), R109 (= R154), T153 (= T199), S168 (≠ G214), G169 (= G215), G170 (≠ A216), E171 (= E217), T239 (= T274), W241 (= W276), D303 (≠ T341), R328 (≠ K366), N394 (≠ D429), W480 (≠ N517), G543 (= G580), W544 (vs. gap)
6fkwA Europium-containing methanol dehydrogenase (see paper)
37% identity, 74% coverage: 48:582/726 of query aligns to 1:533/576 of 6fkwA
- active site: E172 (= E217), N256 (= N294), D299 (= D339), D301 (≠ T341)
- binding europium ion: E172 (= E217), N256 (= N294), D299 (= D339), D301 (≠ T341)
- binding pyrroloquinoline quinone: E55 (= E102), C104 (= C148), C105 (= C149), R110 (= R154), T154 (= T199), S169 (≠ G214), G170 (= G215), G171 (≠ A216), E172 (= E217), T236 (= T274), W238 (= W276), D301 (≠ T341), R326 (≠ K366), D388 (= D429), W467 (≠ N517), G531 (= G580), W532 (≠ A581)
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
37% identity, 74% coverage: 48:582/726 of query aligns to 1:533/577 of 4maeA
- active site: E172 (= E217), N256 (= N294), D299 (= D339)
- binding cerium (iii) ion: E172 (= E217), N256 (= N294), D299 (= D339), D301 (≠ T341)
- binding pyrroloquinoline quinone: E55 (= E102), C104 (= C148), C105 (= C149), R110 (= R154), T154 (= T199), S169 (≠ G214), G170 (= G215), G171 (≠ A216), E172 (= E217), T236 (= T274), W238 (= W276), D301 (≠ T341), R326 (≠ K366), D388 (= D429), W467 (≠ N517), G531 (= G580), W532 (≠ A581)
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)
36% identity, 75% coverage: 45:590/726 of query aligns to 36:596/623 of Q9Z4J7
- D45 (≠ A54) binding
- T48 (≠ E57) binding
- D51 (≠ N60) binding
- E95 (= E102) binding
- C139 (= C148) modified: Disulfide link with 140
- CC 139:140 (= CC 148:149) 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 (= C149) modified: Disulfide link with 139
- R145 (= R154) binding
- T189 (= T199) binding
- HGS 207:209 (≠ -GN 212:213) binding
- E213 (= E217) binding
- N300 (= N294) binding
- D350 (= D339) binding
- R378 (≠ K366) binding
- W523 (= W508) binding
- A587 (= A581) binding
Sites not aligning to the query:
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
36% identity, 75% coverage: 45:590/726 of query aligns to 2:562/582 of 1flgA
- active site: E179 (= E217), N266 (= N294), D316 (= D339)
- binding calcium ion: D11 (≠ A54), T14 (≠ E57), D17 (≠ N60), E179 (= E217), N266 (= N294), D316 (= D339)
- binding pyrroloquinoline quinone: E61 (= E102), C105 (= C148), C106 (= C149), R111 (= R154), T155 (= T199), S176 (≠ G214), G177 (= G215), D178 (≠ A216), W248 (= W276), R344 (≠ K366), N413 (≠ D429), W414 (= W430), W489 (= W508), G552 (= G580), A553 (= A581)
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
37% identity, 71% coverage: 68:580/726 of query aligns to 21:536/579 of 6oc6A
- active site: E171 (= E217), N255 (= N294), D297 (= D339)
- binding pyrroloquinoline quinone: E55 (= E102), C103 (= C148), C104 (= C149), R109 (= R154), T153 (= T199), S168 (≠ G214), G169 (= G215), G170 (≠ A216), E171 (= E217), W237 (= W276), D299 (≠ T341), R324 (≠ K366), D395 (= D429), W473 (≠ N517), G536 (= G580)
Sites not aligning to the query:
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
34% identity, 75% coverage: 51:597/726 of query aligns to 4:556/588 of 7o6zB
- binding methanol: E173 (= E217), W263 (= W298), D314 (= D339)
- binding Neodymium Ion: E173 (= E217), N259 (= N294), D314 (= D339), D316 (≠ T341)
- binding pyrroloquinoline quinone: E55 (= E102), C105 (= C148), C106 (= C149), R111 (= R154), T155 (= T199), G170 (= G214), G171 (= G215), D172 (≠ A216), E173 (= E217), W241 (= W276), D316 (≠ T341), R341 (≠ K366), D403 (= D429), W481 (≠ N517), G544 (= G580), W545 (≠ A581)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
34% identity, 75% coverage: 51:597/726 of query aligns to 4:556/588 of 7o6zA
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
36% identity, 74% coverage: 45:580/726 of query aligns to 1:532/573 of 7ce5A
- active site: E177 (= E217), N261 (= N294), D303 (= D339)
- binding calcium ion: E177 (= E217), N261 (= N294), D303 (= D339)
- binding methanol: E177 (= E217)
- binding pyrroloquinoline quinone: E55 (= E102), C103 (= C148), C104 (= C149), R109 (= R154), T159 (= T199), A174 (≠ G214), G175 (= G215), A176 (= A216), E177 (= E217), T241 (= T274), W243 (= W276), R330 (≠ K366), N393 (≠ D429), W469 (≠ N517), G532 (= G580)
Sites not aligning to the query:
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
36% identity, 74% coverage: 45:580/726 of query aligns to 1:532/573 of 7cdlC
- active site: E177 (= E217), N261 (= N294), D303 (= D339)
- binding calcium ion: E177 (= E217), N261 (= N294), D303 (= D339)
- binding pyrroloquinoline quinone: E55 (= E102), R109 (= R154), T159 (= T199), A174 (≠ G214), A176 (= A216), E177 (= E217), T241 (= T274), W243 (= W276), D303 (= D339), R330 (≠ K366), N393 (≠ D429), W469 (≠ N517), G532 (= G580)
Sites not aligning to the query:
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
34% identity, 81% coverage: 25:615/726 of query aligns to 11:620/631 of P12293
- C135 (= C148) modified: Disulfide link with 136
- C136 (= C149) modified: Disulfide link with 135
- C418 (≠ T421) modified: Disulfide link with 447
- C447 (≠ S450) modified: Disulfide link with 418
Sites not aligning to the query:
Query Sequence
>Pf6N2E2_1752 FitnessBrowser__pseudo6_N2E2:Pf6N2E2_1752
MRQIGHASFSGVRSTVAGIPLKSLAGALLLSLATASALASETPANVDSQRLIAADKEPGN
WMSTGRTYDEQRYSPLKRISDQNVGQLGLAWSYKLDLDRGVEATPIVVDGVMYTTGPFSV
VYALDARNGKLIWKYDPQSDRNRAGEACCDAVNRGVAVWKGKVYVGVLDGRLEAIDAKTG
QRAWSVDTRADHKRSYTITGAPRVVNGKVVIGNGGAEFGVRGYVTAYDAETGKQAWRFYT
VPGDPKLPPEDKGMAIAAKTWHGDAFVEQGGGGTAWDSFAFDPDLNLLYIGVGNGSLWDP
KWRSQAKGDNLFLSSIVAVNADTGEYVWHYQTTPGDAWDYTATQHMILAELPIDGKPRKV
LMQAPKNGFFYVIDRATGQLLSAKGIVPQSWTKGMDMKTGRPIVDDENAAYWKDGKRKLV
TPAFWGAHDWQPMSYNPNTGLVYIPAHIMSAYYEHIPEAPKRNPFKSMYQLGLRTGMMPE
NVDGLLEMAKGWSGKLIAWDPVKQQPAWEVPYVTIFNGGTLSTAGNLVFEGSADGRVIAY
AADTGKKLWEQPAASGVMAAPITYSVDGEQYVTFMAGWGGAFSTFAGALSLRAGVQPFSQ
VLTYKIGGTAKLQEPAPRPDTPKPPALSTDTAAIEAGGKLYDGYCSQCHGIHAVSGGVLP
DLRKLTPEKHQMFLGILFGGRVPDGMPSFADAFTPEQVDQIHQYLIKRAHDLQDEGLAWK
KFSAKQ
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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