SitesBLAST
Comparing GFF2149 FitnessBrowser__WCS417:GFF2149 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)
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
25% identity, 77% coverage: 166:784/802 of query aligns to 39:543/690 of Q8GR64
- E81 (= E213) binding pyrroloquinoline quinone
- C127 (= C260) modified: Disulfide link with 128
- C128 (vs. gap) modified: Disulfide link with 127
- R133 (= R261) binding pyrroloquinoline quinone
- T177 (≠ S344) binding pyrroloquinoline quinone
- GA 193:194 (≠ VA 360:361) binding pyrroloquinoline quinone
- E195 (≠ D362) binding Ca(2+)
- T252 (≠ N410) binding pyrroloquinoline quinone
- N272 (≠ S430) binding Ca(2+)
- D317 (= D474) binding Ca(2+)
- K344 (= K503) binding pyrroloquinoline quinone
- NW 404:405 (= NW 602:603) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
- 547 binding pyrroloquinoline quinone
- 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)
25% identity, 77% coverage: 166:784/802 of query aligns to 17:521/664 of 1kv9A
- active site: E173 (≠ D362), N250 (≠ S430), D295 (= D474)
- binding acetone: E173 (≠ D362), D295 (= D474)
- binding calcium ion: E173 (≠ D362), N250 (≠ S430), D295 (= D474)
- binding heme c: A101 (≠ V256), R102 (≠ W257)
- binding pyrroloquinoline quinone: E59 (= E213), C105 (= C260), C106 (vs. gap), R111 (= R261), T155 (≠ S344), G170 (≠ R359), A172 (= A361), E173 (≠ D362), T230 (≠ N410), W232 (= W412), K322 (= K503), N382 (= N602), W383 (= W603), W460 (≠ E701)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 623, 631, 633, 636
- binding pyrroloquinoline quinone: 525
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)
25% identity, 77% coverage: 166:784/802 of query aligns to 59:571/708 of Q46444
- E101 (= E213) binding pyrroloquinoline quinone
- C147 (= C260) modified: Disulfide link with 148
- C148 (vs. gap) modified: Disulfide link with 147
- R153 (= R261) binding pyrroloquinoline quinone
- T198 (≠ S344) binding pyrroloquinoline quinone
- GA 214:215 (≠ VA 360:361) binding pyrroloquinoline quinone
- E216 (≠ D362) binding Ca(2+)
- T274 (≠ N410) binding pyrroloquinoline quinone
- N294 (≠ S430) binding Ca(2+)
- D339 (= D474) binding Ca(2+)
- K366 (= K503) binding pyrroloquinoline quinone
- NW 425:426 (= NW 602:603) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:31 signal peptide
- 575 binding pyrroloquinoline quinone
- 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)
25% identity, 77% coverage: 166:784/802 of query aligns to 28:540/670 of 1kb0A
- active site: E185 (≠ D362), N263 (≠ S430), D308 (= D474)
- binding calcium ion: E185 (≠ D362), N263 (≠ S430), D308 (= D474)
- binding pyrroloquinoline quinone: E70 (= E213), C116 (= C260), C117 (vs. gap), R122 (= R261), T167 (≠ S344), G182 (≠ R359), G183 (≠ V360), A184 (= A361), E185 (≠ D362), T243 (≠ N410), W245 (= W412), D308 (= D474), K335 (= K503), N394 (= N602), W395 (= W603), W479 (≠ L706)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C260), C117 (vs. gap), E185 (≠ D362), D308 (= D474), P389 (≠ S597)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
- binding pyrroloquinoline quinone: 543, 544
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 77% coverage: 165:784/802 of query aligns to 12:541/588 of 7o6zB
- binding methanol: E173 (≠ M368), W263 (vs. gap), D314 (= D474)
- binding Neodymium Ion: E173 (≠ M368), N259 (≠ S430), D314 (= D474), D316 (= D476)
- binding pyrroloquinoline quinone: E55 (= E213), C105 (≠ I283), C106 (≠ M284), R111 (≠ P289), T155 (≠ V336), G170 (≠ Q365), G171 (≠ T366), D172 (= D367), E173 (≠ M368), W241 (= W412), D316 (= D476), R341 (≠ K503), D403 (≠ N602), W481 (≠ L721)
Sites not aligning to the query:
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 77% coverage: 165:784/802 of query aligns to 12:541/588 of 7o6zA
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)
24% identity, 80% coverage: 145:784/802 of query aligns to 32:584/757 of O05542
- Q35 (≠ P148) modified: Pyrrolidone carboxylic acid
Sites not aligning to the query:
8gy2A Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
24% identity, 79% coverage: 152:784/802 of query aligns to 5:550/723 of 8gy2A
- binding calcium ion: E181 (≠ D362), N263 (≠ S430), D308 (= D474)
- binding heme c: D104 (≠ Q258)
- binding pyrroloquinoline quinone: C107 (vs. gap), C108 (vs. gap), D163 (≠ S344), G179 (≠ V360), A180 (= A361), E181 (≠ D362), W245 (= W412), N263 (≠ S430), D308 (= D474), K335 (= K503), F398 (≠ W603), W489 (≠ L706)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
24% identity, 78% coverage: 158:784/802 of query aligns to 42:567/718 of Q4W6G0
- C138 (≠ Y265) modified: Disulfide link with 139
- C139 (≠ F266) modified: Disulfide link with 138
- R144 (≠ A290) binding pyrroloquinoline quinone
- T189 (≠ S344) binding pyrroloquinoline quinone
- GA 205:206 (≠ VA 360:361) binding pyrroloquinoline quinone
- E207 (≠ D362) binding Ca(2+)
- T264 (≠ N410) binding pyrroloquinoline quinone
- N284 (≠ S430) binding Ca(2+)
- D329 (= D474) binding Ca(2+)
- K356 (= K503) binding pyrroloquinoline quinone
- W415 (≠ L598) binding substrate
- DW 419:420 (≠ NW 602:603) 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)
24% identity, 78% coverage: 158:784/802 of query aligns to 13:538/684 of 1yiqA
- active site: E178 (≠ D362), N255 (≠ S430), D300 (= D474)
- binding calcium ion: E178 (≠ D362), N255 (≠ S430), D300 (= D474)
- binding pyrroloquinoline quinone: E63 (= E213), C109 (≠ Y265), C110 (≠ F266), R115 (≠ A290), T160 (≠ S344), G175 (≠ R359), G176 (≠ V360), A177 (= A361), E178 (≠ D362), T235 (≠ N410), W237 (= W412), K327 (= K503), D390 (≠ N602), W391 (= W603), F477 (≠ E701)
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
- binding pyrroloquinoline quinone: 542
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)
24% identity, 77% coverage: 170:784/802 of query aligns to 46:550/587 of C5AXV8
- D319 (= D476) mutation to S: Loss of efficient ethanol oxidation with La(3+).
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)
24% identity, 77% coverage: 166:784/802 of query aligns to 39:566/617 of A0A3F2YLY8
- C129 (= C260) modified: Disulfide link with 130
- C130 (vs. gap) modified: Disulfide link with 129
- R135 (= R261) binding pyrroloquinoline quinone
- T179 (≠ S344) binding pyrroloquinoline quinone
- S194 (≠ P369) binding pyrroloquinoline quinone
- G195 (= G370) binding pyrroloquinoline quinone
- G196 (= G371) binding pyrroloquinoline quinone
- E197 (≠ V372) binding La(3+)
- T265 (≠ N410) binding pyrroloquinoline quinone
- W267 (= W412) binding pyrroloquinoline quinone
- N285 (≠ S430) binding La(3+)
- D327 (= D474) binding La(3+)
- D329 (= D476) binding La(3+)
- R354 (≠ K503) binding pyrroloquinoline quinone
- C412 (≠ F594) modified: Disulfide link with 441
- N420 (= N602) binding pyrroloquinoline quinone
- C441 (≠ Q627) modified: Disulfide link with 412
- W506 (≠ L721) 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)
24% identity, 79% coverage: 166:802/802 of query aligns to 13:562/563 of 6damA
- active site: E171 (≠ V372), N259 (≠ S430), D301 (= D474)
- binding pyrroloquinoline quinone: E55 (≠ D208), C103 (= C260), C104 (vs. gap), R109 (= R261), T153 (≠ S344), S168 (≠ P369), G169 (= G370), G170 (= G371), E171 (≠ V372), T239 (≠ N410), W241 (= W412), D303 (= D476), R328 (≠ K503), N394 (= N602), W480 (≠ L721), G543 (≠ R787), W544 (≠ Q788)
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)
24% identity, 77% coverage: 167:784/802 of query aligns to 48:562/611 of I0JWN7
- C138 (= C260) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (= R261) binding pyrroloquinoline quinone
- T188 (≠ S344) binding pyrroloquinoline quinone
- S203 (≠ P369) binding pyrroloquinoline quinone
- G204 (= G370) binding pyrroloquinoline quinone
- G205 (= G371) binding pyrroloquinoline quinone
- E206 (≠ V372) binding Ce(3+); binding Eu(3+)
- T270 (≠ N410) binding pyrroloquinoline quinone
- W272 (= W412) binding pyrroloquinoline quinone
- N290 (≠ S432) binding Ce(3+); binding Eu(3+)
- D333 (= D474) binding Ce(3+); binding Eu(3+)
- D335 (= D476) binding Ce(3+); binding Eu(3+)
- R360 (≠ K503) binding pyrroloquinoline quinone
- C414 (≠ F594) modified: Disulfide link with 443
- C443 (≠ A635) modified: Disulfide link with 414
- W501 (≠ L721) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 566 binding pyrroloquinoline quinone
6fkwA Europium-containing methanol dehydrogenase (see paper)
24% identity, 77% coverage: 167:784/802 of query aligns to 14:528/576 of 6fkwA
- active site: E172 (≠ V372), N256 (≠ S432), D299 (= D474), D301 (= D476)
- binding europium ion: E172 (≠ V372), N256 (≠ S432), D299 (= D474), D301 (= D476)
- binding pyrroloquinoline quinone: E55 (≠ D208), C104 (= C260), C105 (vs. gap), R110 (= R261), T154 (≠ S344), S169 (≠ P369), G170 (= G370), G171 (= G371), E172 (≠ V372), T236 (≠ N410), W238 (= W412), D301 (= D476), R326 (≠ K503), D388 (≠ N602), W467 (≠ L721)
Sites not aligning to the query:
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
24% identity, 77% coverage: 167:784/802 of query aligns to 14:528/577 of 4maeA
- active site: E172 (≠ V372), N256 (≠ S432), D299 (= D474)
- binding cerium (iii) ion: E172 (≠ V372), N256 (≠ S432), D299 (= D474), D301 (= D476)
- binding pyrroloquinoline quinone: E55 (≠ D208), C104 (= C260), C105 (vs. gap), R110 (= R261), T154 (≠ S344), S169 (≠ P369), G170 (= G370), G171 (= G371), E172 (≠ V372), T236 (≠ N410), W238 (= W412), D301 (= D476), R326 (≠ K503), D388 (≠ N602), W467 (≠ L721)
Sites not aligning to the query:
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)
23% identity, 84% coverage: 113:784/802 of query aligns to 1:553/595 of Q88JH0
- Q87 (= Q215) binding pyrroloquinoline quinone
- C131 (≠ I283) modified: Disulfide link with 132
- C132 (≠ M284) modified: Disulfide link with 131
- R137 (≠ P289) binding pyrroloquinoline quinone
- S181 (= S344) binding pyrroloquinoline quinone
- G197 (= G357) binding pyrroloquinoline quinone
- G198 (= G358) binding pyrroloquinoline quinone
- E199 (≠ R359) binding Pr(3+)
- W263 (= W412) binding pyrroloquinoline quinone
- N281 (≠ S430) binding Pr(3+)
- D323 (= D474) binding Pr(3+)
- D325 (= D476) binding Pr(3+)
- R350 (≠ K503) binding pyrroloquinoline quinone
- F412 (≠ S597) 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 (= N602) binding pyrroloquinoline quinone
- W493 (≠ L721) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 557 binding pyrroloquinoline quinone
- 561 W→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
23% identity, 76% coverage: 176:784/802 of query aligns to 26:526/562 of 6zcvA
- active site: E172 (≠ R359), N254 (≠ S430), D296 (= D474)
- binding calcium ion: N161 (≠ G351), K163 (vs. gap), P278 (≠ A456), D279 (≠ S457)
- binding pyrroloquinoline quinone: Q60 (= Q215), C104 (≠ I283), C105 (≠ M284), I108 (≠ S287), R110 (≠ P289), S154 (= S344), G170 (= G357), G171 (= G358), E172 (≠ R359), W236 (= W412), D298 (= D476), R323 (≠ K503), N390 (= N602), W466 (≠ L721)
Sites not aligning to the query:
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)
26% identity, 49% coverage: 170:558/802 of query aligns to 42:398/601 of C5B120
- R130 (= R261) binding pyrroloquinoline quinone
- T174 (≠ S345) binding pyrroloquinoline quinone
- S189 (≠ P369) binding pyrroloquinoline quinone
- G190 (= G370) binding pyrroloquinoline quinone
- G191 (= G371) binding pyrroloquinoline quinone
- E192 (≠ V372) binding La(3+)
- W258 (= W412) binding pyrroloquinoline quinone
- N276 (≠ S430) binding La(3+)
- D318 (= D474) binding La(3+)
- D320 (= D476) 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 (≠ K503) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:21 signal peptide
- 494 binding pyrroloquinoline quinone
- 558 binding pyrroloquinoline quinone
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
26% identity, 49% coverage: 170:558/802 of query aligns to 21:377/579 of 6oc6A
- active site: E171 (≠ V372), N255 (≠ S430), D297 (= D474)
- binding pyrroloquinoline quinone: E55 (≠ D208), C103 (= C260), C104 (vs. gap), R109 (= R261), T153 (≠ S345), S168 (≠ P369), G169 (= G370), G170 (= G371), E171 (≠ V372), W237 (= W412), D299 (= D476), R324 (≠ K503)
Sites not aligning to the query:
Query Sequence
>GFF2149 FitnessBrowser__WCS417:GFF2149
MKRASRAAGVSRLLLLGLGVIIALLGLALAIGGVKLVSLGGSWYFLIGGAIMAIAGLLIA
CRKPAGAWVFAAFLIGTAIWAVADVGLVFWPLFSRLFMFAAIGMVVALVYPLLVNKPARG
AYAVAAVLAAGVAVAAGNMFVAHPSVAPTGAGPGITPVAAGDAQKDWAHYGNTEGGSRFA
ALDQINRDTVNKLKVAWTYHTGDVAISDGNGAEDQLTPLQIGNKVFICTPHNNLIALDAD
TGKELWKNEVNAKSAVWQRCRGMAYFDATAPIAQPTQPNSSPIMPASVPAGAQCQRRLLT
NTIDARLIAVDADTGKFCEDFGTHGQVDLKAGLGNVPDSYYQLSSAPLIAGTTVVVGGRV
ADNVQTDMPGGVIRGFDVISGQMRWAFDPGNPEDKQAPADGSTYVRSTPNSWAPMSYDPL
MNTVFLPMGSSSTDIYGVERTQLNHKYGASVLALDASTGAEKWVYQTVHNDLWDFDLPMQ
PSLIDFTPPGSDKAVPAVVIGTKAGQIYVLDRATGKPLTDVQEVPVKAANIPNEPYSPTQ
PKSVGMPQIGAQTLTESDMWGATPFDQLLCRIDFKGMRYEGLYTAPGTDKSLSFPGSLGG
MNWGSISTDPVHGFIFVNDMRLGLWIQMVPSQNKAQASSGGEALNTGMGAVPLKGTPYAV
NKNRFLSVAGIPCQAPPFGTLTAIDMKTQKVAWQVPVGTVEDTGPLGIRMHLPIKIGLPT
LGGTLSTQGGLIFIAGTQDFYLRAFNSGNGDEVWKARLPVGSQGGPMTYVSPKTGKQYIV
ITAGGARQSTDRGDYVIAYALP
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