SitesBLAST
Comparing GFF3407 FitnessBrowser__WCS417:GFF3407 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)
92% identity, 99% coverage: 1:587/591 of query aligns to 1:587/595 of Q88JH0
- Q87 (= Q87) binding pyrroloquinoline quinone
- C131 (= C131) modified: Disulfide link with 132
- C132 (= C132) modified: Disulfide link with 131
- R137 (= R137) binding pyrroloquinoline quinone
- S181 (= S181) binding pyrroloquinoline quinone
- G197 (= G197) binding pyrroloquinoline quinone
- G198 (= G198) binding pyrroloquinoline quinone
- E199 (= E199) binding Pr(3+)
- W263 (= W263) binding pyrroloquinoline quinone
- N281 (= N281) binding Pr(3+)
- D323 (= D323) binding Pr(3+)
- D325 (= D325) binding Pr(3+)
- R350 (= R350) binding pyrroloquinoline quinone
- F412 (= F412) 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 (= N417) binding pyrroloquinoline quinone
- W493 (= W493) binding pyrroloquinoline quinone
- A557 (= A557) binding pyrroloquinoline quinone
- W561 (= W561) 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
94% identity, 95% coverage: 28:587/591 of query aligns to 1:560/562 of 6zcvA
- active site: E172 (= E199), N254 (= N281), D296 (= D323)
- binding calcium ion: N161 (= N188), K163 (= K190), P278 (= P305), D279 (= D306)
- binding pyrroloquinoline quinone: Q60 (= Q87), C104 (= C131), C105 (= C132), I108 (= I135), R110 (= R137), S154 (= S181), G170 (= G197), G171 (= G198), E172 (= E199), W236 (= W263), D298 (= D325), R323 (= R350), N390 (= N417), W466 (= W493), G529 (= G556), A530 (= A557)
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)
64% identity, 99% coverage: 7:590/591 of query aligns to 4:587/587 of C5AXV8
- D319 (= D325) 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)
53% identity, 94% coverage: 29:584/591 of query aligns to 37:614/623 of Q9Z4J7
- D45 (= D37) binding Ca(2+)
- T48 (≠ N40) binding Ca(2+)
- D51 (≠ Q43) binding Ca(2+)
- E95 (≠ Q87) binding pyrroloquinoline quinone
- C139 (= C131) modified: Disulfide link with 140
- CC 139:140 (= CC 131:132) 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 (= C132) modified: Disulfide link with 139
- R145 (= R137) binding pyrroloquinoline quinone
- T189 (≠ S181) binding pyrroloquinoline quinone
- HGS 207:209 (≠ TGV 193:195) binding pyrroloquinoline quinone
- E213 (= E199) binding Ca(2+)
- N300 (= N281) binding Ca(2+)
- D350 (= D323) binding Ca(2+)
- R378 (= R350) binding pyrroloquinoline quinone
- W523 (= W493) binding pyrroloquinoline quinone
- A587 (= A557) binding pyrroloquinoline quinone
Sites not aligning to the query:
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
53% identity, 94% coverage: 29:584/591 of query aligns to 3:580/582 of 1flgA
- active site: E179 (= E199), N266 (= N281), D316 (= D323)
- binding calcium ion: D11 (= D37), T14 (≠ N40), D17 (≠ Q43), E179 (= E199), N266 (= N281), D316 (= D323)
- binding pyrroloquinoline quinone: E61 (≠ Q87), C105 (= C131), C106 (= C132), R111 (= R137), T155 (≠ S181), S176 (≠ A196), G177 (= G197), D178 (≠ G198), W248 (= W263), R344 (= R350), N413 (= N417), W414 (= W418), W489 (= W493), G552 (= G556), A553 (= A557)
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
40% identity, 94% coverage: 7:564/591 of query aligns to 2:554/690 of Q8GR64
- E81 (≠ Q87) binding pyrroloquinoline quinone
- C127 (= C131) modified: Disulfide link with 128
- C128 (= C132) modified: Disulfide link with 127
- R133 (= R137) binding pyrroloquinoline quinone
- T177 (≠ S181) binding pyrroloquinoline quinone
- GA 193:194 (≠ GG 197:198) binding pyrroloquinoline quinone
- E195 (= E199) binding Ca(2+)
- T252 (≠ P262) binding pyrroloquinoline quinone
- N272 (= N281) binding Ca(2+)
- D317 (= D323) binding Ca(2+)
- K344 (≠ R350) binding pyrroloquinoline quinone
- NW 404:405 (= NW 417:418) binding pyrroloquinoline quinone
- V547 (≠ A557) binding pyrroloquinoline quinone
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
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
41% identity, 91% coverage: 27:564/591 of query aligns to 1:532/664 of 1kv9A
- active site: E173 (= E199), N250 (= N281), D295 (= D323)
- binding acetone: E173 (= E199), D295 (= D323)
- binding calcium ion: E173 (= E199), N250 (= N281), D295 (= D323)
- binding heme c: A101 (≠ D127), R102 (≠ I128)
- binding pyrroloquinoline quinone: E59 (≠ Q87), C105 (= C131), C106 (= C132), R111 (= R137), T155 (≠ S181), G170 (≠ A196), A172 (≠ G198), E173 (= E199), T230 (≠ P262), W232 (= W263), K322 (≠ R350), N382 (= N417), W383 (= W418), W460 (≠ L492), V525 (≠ A557)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 623, 631, 633, 636
A0A3F2YLY8 Lanthanide-dependent methanol dehydrogenase XoxF; Lanthanide-dependent MDH; Ln(3+)-dependent MDH; EC 1.1.2.10 from Methylotuvimicrobium buryatense (Methylomicrobium buryatense) (see paper)
39% identity, 94% coverage: 1:556/591 of query aligns to 1:569/617 of A0A3F2YLY8
- C129 (= C131) modified: Disulfide link with 130
- C130 (= C132) modified: Disulfide link with 129
- R135 (= R137) binding pyrroloquinoline quinone
- T179 (≠ S181) binding pyrroloquinoline quinone
- S194 (≠ A196) binding pyrroloquinoline quinone
- G195 (= G197) binding pyrroloquinoline quinone
- G196 (= G198) binding pyrroloquinoline quinone
- E197 (= E199) binding La(3+)
- T265 (≠ A261) binding pyrroloquinoline quinone
- W267 (= W263) binding pyrroloquinoline quinone
- N285 (= N281) binding La(3+)
- D327 (= D323) binding La(3+)
- D329 (= D325) binding La(3+)
- R354 (= R350) binding pyrroloquinoline quinone
- C412 (≠ A409) modified: Disulfide link with 441
- N420 (= N417) binding pyrroloquinoline quinone
- C441 (≠ G438) modified: Disulfide link with 412
- W506 (= W493) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 570 binding pyrroloquinoline quinone
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
39% identity, 94% coverage: 31:584/591 of query aligns to 1:562/563 of 6damA
- active site: E171 (= E199), N259 (= N281), D301 (= D323)
- binding pyrroloquinoline quinone: E55 (≠ Q87), C103 (= C131), C104 (= C132), R109 (= R137), T153 (≠ S181), S168 (≠ A196), G169 (= G197), G170 (= G198), E171 (= E199), T239 (≠ A261), W241 (= W263), D303 (= D325), R328 (= R350), N394 (= N417), W480 (= W493), G543 (= G556), W544 (= W561)
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
39% identity, 91% coverage: 46:581/591 of query aligns to 31:563/670 of 1kb0A
- active site: E185 (= E199), N263 (= N281), D308 (= D323)
- binding calcium ion: E185 (= E199), N263 (= N281), D308 (= D323)
- binding pyrroloquinoline quinone: E70 (≠ Q87), C116 (= C131), C117 (= C132), R122 (= R137), T167 (≠ S181), G182 (≠ A196), G183 (= G197), A184 (≠ G198), E185 (= E199), T243 (≠ P262), W245 (= W263), D308 (= D323), K335 (≠ R350), N394 (= N417), W395 (= W418), W479 (≠ L492), G543 (= G556), V544 (≠ A557)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C131), C117 (= C132), E185 (= E199), D308 (= D323), P389 (≠ F412)
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)
39% identity, 91% coverage: 46:581/591 of query aligns to 62:594/708 of Q46444
- E101 (≠ Q87) binding pyrroloquinoline quinone
- C147 (= C131) modified: Disulfide link with 148
- C148 (= C132) modified: Disulfide link with 147
- R153 (= R137) binding pyrroloquinoline quinone
- T198 (≠ S181) binding pyrroloquinoline quinone
- GA 214:215 (≠ GG 197:198) binding pyrroloquinoline quinone
- E216 (= E199) binding Ca(2+)
- T274 (≠ P262) binding pyrroloquinoline quinone
- N294 (= N281) binding Ca(2+)
- D339 (= D323) binding Ca(2+)
- K366 (≠ R350) binding pyrroloquinoline quinone
- NW 425:426 (= NW 417:418) binding pyrroloquinoline quinone
- V575 (≠ A557) 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
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
38% identity, 97% coverage: 10:583/591 of query aligns to 14:596/718 of Q4W6G0
- C138 (= C131) modified: Disulfide link with 139
- C139 (= C132) modified: Disulfide link with 138
- R144 (= R137) binding pyrroloquinoline quinone
- T189 (≠ S181) binding pyrroloquinoline quinone
- GA 205:206 (≠ GG 197:198) binding pyrroloquinoline quinone
- E207 (= E199) binding Ca(2+)
- T264 (≠ A261) binding pyrroloquinoline quinone
- N284 (= N281) binding Ca(2+)
- D329 (= D323) binding Ca(2+)
- K356 (≠ R350) binding pyrroloquinoline quinone
- W415 (≠ L413) binding substrate
- DW 419:420 (≠ NW 417:418) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:29 signal peptide
- 30:718 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH-IIG
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 676 binding axial binding residue
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)
38% identity, 94% coverage: 27:583/591 of query aligns to 5:567/684 of 1yiqA
- active site: E178 (= E199), N255 (= N281), D300 (= D323)
- binding calcium ion: E178 (= E199), N255 (= N281), D300 (= D323)
- binding pyrroloquinoline quinone: E63 (≠ Q87), C109 (= C131), C110 (= C132), R115 (= R137), T160 (≠ S181), G175 (≠ A196), G176 (= G197), A177 (≠ G198), E178 (= E199), T235 (≠ A261), W237 (= W263), K327 (≠ R350), D390 (≠ N417), W391 (= W418), F477 (≠ L492), A542 (= A557)
Sites not aligning to the query:
- binding heme c: 605, 606, 608, 609, 610, 623, 626, 630, 634, 637, 638, 642, 645, 646, 647, 648, 650
C5B120 Lanthanide-dependent methanol dehydrogenase; Lanthanide-dependent MDH; Ln(3+)-dependent MDH; La(3+)- and PQQ-dependent MDH; La(3+)-dependent methanol dehydrogenase; La(3+)-dependent MDH; EC 1.1.2.10 from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) (see 2 papers)
37% identity, 90% coverage: 28:556/591 of query aligns to 19:557/601 of C5B120
- R130 (= R137) binding pyrroloquinoline quinone
- T174 (≠ S181) binding pyrroloquinoline quinone
- S189 (≠ A196) binding pyrroloquinoline quinone
- G190 (= G197) binding pyrroloquinoline quinone
- G191 (= G198) binding pyrroloquinoline quinone
- E192 (= E199) binding La(3+)
- W258 (= W263) binding pyrroloquinoline quinone
- N276 (= N281) binding La(3+)
- D318 (= D323) binding La(3+)
- D320 (= D325) binding La(3+); mutation to A: Loss of methanol dehydrogenase activity. In contrast to wild-type, the mutant cells are incapable of growth with methanol and La(3+). The mutant protein is unable to bind La(3+) and is loaded with Ca(2+) regardless of whether or not La(3+) is included in the growth medium, but is inactive.
- R345 (= R350) binding pyrroloquinoline quinone
- W494 (= W493) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:21 signal peptide
- 558 binding pyrroloquinoline quinone
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
37% identity, 89% coverage: 31:556/591 of query aligns to 1:536/579 of 6oc6A
- active site: E171 (= E199), N255 (= N281), D297 (= D323)
- binding pyrroloquinoline quinone: E55 (≠ Q87), C103 (= C131), C104 (= C132), R109 (= R137), T153 (≠ S181), S168 (≠ A196), G169 (= G197), G170 (= G198), E171 (= E199), W237 (= W263), D299 (= D325), R324 (= R350), D395 (≠ N417), W473 (= W493), G536 (= G556)
Sites not aligning to the query:
I0JWN7 Lanthanide-dependent methanol dehydrogenase; Lanthanide-dependent MDH; Ln(3+)-dependent MDH; Ln-MDH; EC 1.1.2.10 from Methylacidiphilum fumariolicum (strain SolV) (see 2 papers)
37% identity, 94% coverage: 1:556/591 of query aligns to 5:565/611 of I0JWN7
- C138 (= C131) modified: Disulfide link with 139
- C139 (= C132) modified: Disulfide link with 138
- R144 (= R137) binding pyrroloquinoline quinone
- T188 (≠ S181) binding pyrroloquinoline quinone
- S203 (≠ A196) binding pyrroloquinoline quinone
- G204 (= G197) binding pyrroloquinoline quinone
- G205 (= G198) binding pyrroloquinoline quinone
- E206 (= E199) binding Ce(3+); binding Eu(3+)
- T270 (≠ A261) binding pyrroloquinoline quinone
- W272 (= W263) binding pyrroloquinoline quinone
- N290 (= N281) binding Ce(3+); binding Eu(3+)
- D333 (= D323) binding Ce(3+); binding Eu(3+)
- D335 (= D325) binding Ce(3+); binding Eu(3+)
- R360 (= R350) binding pyrroloquinoline quinone
- C414 (≠ A409) modified: Disulfide link with 443
- C443 (≠ G438) modified: Disulfide link with 414
- W501 (= W493) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 566 binding pyrroloquinoline quinone
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
38% identity, 89% coverage: 31:556/591 of query aligns to 1:531/577 of 4maeA
- active site: E172 (= E199), N256 (= N281), D299 (= D323)
- binding cerium (iii) ion: E172 (= E199), N256 (= N281), D299 (= D323), D301 (= D325)
- binding pyrroloquinoline quinone: E55 (≠ Q87), C104 (= C131), C105 (= C132), R110 (= R137), T154 (≠ S181), S169 (≠ A196), G170 (= G197), G171 (= G198), E172 (= E199), T236 (≠ A261), W238 (= W263), D301 (= D325), R326 (= R350), D388 (≠ N417), W467 (= W493), G531 (= G556)
Sites not aligning to the query:
6fkwA Europium-containing methanol dehydrogenase (see paper)
38% identity, 89% coverage: 31:556/591 of query aligns to 1:531/576 of 6fkwA
- active site: E172 (= E199), N256 (= N281), D299 (= D323), D301 (= D325)
- binding europium ion: E172 (= E199), N256 (= N281), D299 (= D323), D301 (= D325)
- binding pyrroloquinoline quinone: E55 (≠ Q87), C104 (= C131), C105 (= C132), R110 (= R137), T154 (≠ S181), S169 (≠ A196), G170 (= G197), G171 (= G198), E172 (= E199), T236 (≠ A261), W238 (= W263), D301 (= D325), R326 (= R350), D388 (≠ N417), W467 (= W493), G531 (= G556)
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)
36% identity, 89% coverage: 40:567/591 of query aligns to 50:598/757 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
36% identity, 89% coverage: 40:567/591 of query aligns to 16:564/723 of 8gy2A
- binding calcium ion: E181 (= E199), N263 (= N281), D308 (= D323)
- binding heme c: D104 (vs. gap)
- binding pyrroloquinoline quinone: C107 (= C131), C108 (= C132), D163 (≠ S181), G179 (= G197), A180 (≠ G198), E181 (= E199), W245 (= W263), N263 (= N281), D308 (= D323), K335 (≠ R350), F398 (≠ W418), W489 (≠ L492)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
Query Sequence
>GFF3407 FitnessBrowser__WCS417:GFF3407
MTQPARRQPFALSVLLGAILLSGQAMASVTDEEILQDPKNPGQIVTNGLGVQGQRYSPLD
TLNVDNVKELRPVWAFSFGGEKQRGQQAQPMIKDGVMYLTGSYSRVFAVDARTGKKLWQY
DARLPDDIRPCCDVINRGVALYGDLVFFGTLDAKLVALNKDTGKVVWSKKVADHKEGYSI
SAAPLVINGKLITGVAGGEFGVVGKIEAYDPKNGELLWSRPTVEGHMGYVYKDGKAVENG
ISGGEAGKTWPGDLWKTGGAAPWLGGYYDPETNLLLFGTGNPAPWNSHLRPGDNLYSSSR
LALNPDDGTIKWHFQTTPHDGWDYDGVNELVSFNYTEGGKEIKAAATADRNGFFYVLDRT
NGKFIRGFPFVDKITWATGLDKDGRPIYNDASRPGAPGSEAKGTSVFVAPAFLGAKNWMP
MAYNRDTGLFYVPSNEWGMDMWNEGIAYKKGAAFLGAGFTIKPLNEDYIGVLRAIDPKTG
KEVWRHKNFAPLWGGVLTTKGNLVFTGTPEGFLQAFNAKTGEKVWEFQTGSGVLGSPVTW
EMDGEQYVSVLSGWGGAVPLWGGEVAKRIKDFNQGGMLWTFKLPKELVAKH
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