SitesBLAST
Comparing WP_069333644.1 NCBI__GCF_003046325.1:WP_069333644.1 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)
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
27% identity, 80% coverage: 160:780/781 of query aligns to 16:555/664 of 1kv9A
- active site: E173 (≠ V348), N250 (= N414), D295 (= D458)
- binding acetone: E173 (≠ V348), D295 (= D458)
- binding calcium ion: E173 (≠ V348), N250 (= N414), D295 (= D458)
- binding heme c: A101 (≠ Q255), R102 (≠ H256)
- binding pyrroloquinoline quinone: E59 (≠ Q211), C105 (= C259), C106 (vs. gap), R111 (= R260), T155 (= T326), G170 (≠ N345), A172 (≠ S347), E173 (≠ V348), T230 (≠ S395), W232 (= W396), K322 (= K485), N382 (= N583), W383 (= W584), W460 (≠ V691), V525 (≠ S761)
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)
27% identity, 80% coverage: 160:780/781 of query aligns to 38:577/690 of Q8GR64
- E81 (≠ Q211) binding pyrroloquinoline quinone
- C127 (= C259) modified: Disulfide link with 128
- C128 (vs. gap) modified: Disulfide link with 127
- R133 (= R260) binding pyrroloquinoline quinone
- T177 (= T326) binding pyrroloquinoline quinone
- GA 193:194 (≠ FS 346:347) binding pyrroloquinoline quinone
- E195 (≠ V348) binding Ca(2+)
- T252 (≠ S395) binding pyrroloquinoline quinone
- N272 (= N414) binding Ca(2+)
- D317 (= D458) binding Ca(2+)
- K344 (= K485) binding pyrroloquinoline quinone
- NW 404:405 (= NW 583:584) binding pyrroloquinoline quinone
- V547 (≠ S761) 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
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)
26% identity, 77% coverage: 159:757/781 of query aligns to 51:584/757 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
26% identity, 77% coverage: 159:757/781 of query aligns to 17:550/723 of 8gy2A
- binding calcium ion: E181 (≠ V348), N263 (= N414), D308 (= D458)
- binding heme c: D104 (= D253)
- binding pyrroloquinoline quinone: C107 (vs. gap), C108 (vs. gap), D163 (≠ E320), G179 (≠ F346), A180 (≠ S347), E181 (≠ V348), W245 (= W396), N263 (= N414), D308 (= D458), K335 (= K485), F398 (≠ W584), W489 (≠ G695)
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)
31% identity, 49% coverage: 117:498/781 of query aligns to 8:369/718 of Q4W6G0
- C138 (= C259) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (= R260) binding pyrroloquinoline quinone
- T189 (= T326) binding pyrroloquinoline quinone
- GA 205:206 (≠ FS 346:347) binding pyrroloquinoline quinone
- E207 (≠ V348) binding Ca(2+)
- T264 (≠ N394) binding pyrroloquinoline quinone
- N284 (= N414) binding Ca(2+)
- D329 (= D458) binding Ca(2+)
- K356 (= K485) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:29 signal peptide
- 30:718 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH-IIG
- 415 binding substrate
- 419:420 binding pyrroloquinoline quinone
- 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)
32% identity, 44% coverage: 159:498/781 of query aligns to 19:340/684 of 1yiqA
- active site: E178 (≠ V348), N255 (= N414), D300 (= D458)
- binding calcium ion: E178 (≠ V348), N255 (= N414), D300 (= D458)
- binding pyrroloquinoline quinone: E63 (≠ Q211), C109 (= C259), C110 (vs. gap), R115 (= R260), T160 (= T326), G175 (≠ N345), G176 (≠ F346), A177 (≠ S347), E178 (≠ V348), T235 (≠ N394), W237 (= W396), K327 (= K485)
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: 390, 391, 477, 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)
26% identity, 85% coverage: 99:762/781 of query aligns to 3:555/587 of C5AXV8
- D319 (= D460) mutation to S: Loss of efficient ethanol oxidation with La(3+).
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
25% identity, 78% coverage: 153:763/781 of query aligns to 5:547/588 of 7o6zB
- binding methanol: E173 (≠ D344), W263 (≠ D418), D314 (= D458)
- binding Neodymium Ion: E173 (≠ D344), N259 (= N414), D314 (= D458), D316 (= D460)
- binding pyrroloquinoline quinone: E55 (≠ Q211), C105 (≠ R260), C106 (≠ G261), R111 (= R266), T155 (= T318), G170 (≠ A341), G171 (≠ V342), D172 (≠ N343), E173 (≠ D344), W241 (= W396), D316 (= D460), R341 (≠ K485), D403 (≠ N583), W481 (≠ I696), G544 (= G760), W545 (≠ S761)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
25% identity, 78% coverage: 153:763/781 of query aligns to 5:547/588 of 7o6zA
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
26% identity, 80% coverage: 156:776/781 of query aligns to 8:562/563 of 6damA
- active site: E171 (≠ D344), N259 (= N414), D301 (= D458)
- binding pyrroloquinoline quinone: E55 (≠ Q211), C103 (≠ T258), C104 (= C259), R109 (= R266), T153 (= T326), S168 (≠ A341), G169 (≠ V342), G170 (≠ N343), E171 (≠ D344), T239 (vs. gap), W241 (= W396), D303 (= D460), R328 (≠ K485), N394 (= N583), W480 (≠ I696), G543 (= G760), W544 (vs. gap)
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)
25% identity, 78% coverage: 156:763/781 of query aligns to 34:572/617 of A0A3F2YLY8
- C129 (≠ T258) modified: Disulfide link with 130
- C130 (= C259) modified: Disulfide link with 129
- R135 (= R266) binding pyrroloquinoline quinone
- T179 (= T326) binding pyrroloquinoline quinone
- S194 (≠ A341) binding pyrroloquinoline quinone
- G195 (≠ V342) binding pyrroloquinoline quinone
- G196 (≠ N343) binding pyrroloquinoline quinone
- E197 (≠ D344) binding La(3+)
- T265 (vs. gap) binding pyrroloquinoline quinone
- W267 (= W396) binding pyrroloquinoline quinone
- N285 (= N414) binding La(3+)
- D327 (= D458) binding La(3+)
- D329 (= D460) binding La(3+)
- R354 (≠ K485) binding pyrroloquinoline quinone
- C412 (≠ Y575) modified: Disulfide link with 441
- N420 (= N583) binding pyrroloquinoline quinone
- C441 (vs. gap) modified: Disulfide link with 412
- W506 (≠ I696) binding pyrroloquinoline quinone
- W570 (≠ S761) binding pyrroloquinoline quinone
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
23% identity, 77% coverage: 159:757/781 of query aligns to 11:536/600 of 1lrwA
- active site: E177 (≠ D344), N261 (= N414), D303 (= D458)
- binding calcium ion: E177 (≠ D344), N261 (= N414), D303 (= D458)
- binding pyrroloquinoline quinone: E55 (≠ Q211), C103 (= C259), C104 (vs. gap), R109 (= R260), T159 (= T326), S174 (≠ A341), G175 (≠ V342), A176 (≠ N343), E177 (≠ D344), T241 (≠ N394), W243 (= W396), R331 (≠ K485), W476 (≠ I696)
Sites not aligning to the query:
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
24% identity, 76% coverage: 173:763/781 of query aligns to 25:539/579 of 6oc6A
- active site: E171 (≠ D344), N255 (= N414), D297 (= D458)
- binding pyrroloquinoline quinone: E55 (≠ Q211), C103 (= C259), C104 (≠ R260), R109 (= R266), T153 (= T326), S168 (≠ A341), G169 (≠ V342), G170 (≠ N343), E171 (≠ D344), W237 (= W396), D299 (= D460), R324 (≠ K485), D395 (≠ N583), W473 (≠ K690), G536 (= G760), W537 (≠ S761)
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)
24% identity, 76% coverage: 173:763/781 of query aligns to 46:560/601 of C5B120
- R130 (= R266) binding pyrroloquinoline quinone
- T174 (= T326) binding pyrroloquinoline quinone
- S189 (≠ A341) binding pyrroloquinoline quinone
- G190 (≠ V342) binding pyrroloquinoline quinone
- G191 (≠ N343) binding pyrroloquinoline quinone
- E192 (≠ D344) binding La(3+)
- W258 (= W396) binding pyrroloquinoline quinone
- N276 (= N414) binding La(3+)
- D318 (= D458) binding La(3+)
- D320 (= D460) 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 (≠ K485) binding pyrroloquinoline quinone
- W494 (≠ K690) binding pyrroloquinoline quinone
- W558 (≠ S761) binding pyrroloquinoline quinone
Sites not aligning to the query:
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
23% identity, 75% coverage: 170:752/781 of query aligns to 22:522/571 of 4aahA
- active site: E171 (≠ D344), N255 (= N414), D297 (= D458)
- binding calcium ion: E171 (≠ D344), N255 (= N414)
- binding pyrroloquinoline quinone: E55 (≠ Q211), C103 (= C259), C104 (≠ R260), R109 (= R266), S168 (≠ A341), A170 (≠ N343), E171 (≠ D344), W237 (= W396), R324 (≠ K485), N387 (= N583), W467 (≠ I696)
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)
28% identity, 42% coverage: 171:500/781 of query aligns to 53:365/595 of Q88JH0
- Q87 (= Q211) binding pyrroloquinoline quinone
- C131 (≠ T258) modified: Disulfide link with 132
- C132 (= C259) modified: Disulfide link with 131
- R137 (= R260) binding pyrroloquinoline quinone
- S181 (≠ T326) binding pyrroloquinoline quinone
- G197 (≠ V342) binding pyrroloquinoline quinone
- G198 (≠ N343) binding pyrroloquinoline quinone
- E199 (≠ D344) binding Pr(3+)
- W263 (= W396) binding pyrroloquinoline quinone
- N281 (= N414) binding Pr(3+)
- D323 (= D458) binding Pr(3+)
- D325 (= D460) binding Pr(3+)
- R350 (≠ K485) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 412 F→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.; F→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.
- 417 binding pyrroloquinoline quinone
- 493 binding pyrroloquinoline quinone
- 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
28% identity, 42% coverage: 171:500/781 of query aligns to 26:338/562 of 6zcvA
- active site: E172 (≠ D344), N254 (= N414), D296 (= D458)
- binding calcium ion: N161 (≠ G333), K163 (≠ R335), P278 (≠ V440), D279 (≠ T441)
- binding pyrroloquinoline quinone: Q60 (= Q211), C104 (≠ T258), C105 (= C259), I108 (vs. gap), R110 (= R260), S154 (≠ T326), G170 (≠ V342), G171 (≠ N343), E172 (≠ D344), W236 (= W396), D298 (= D460), R323 (≠ K485)
Sites not aligning to the query:
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
27% identity, 44% coverage: 161:500/781 of query aligns to 28:350/670 of 1kb0A
- active site: E185 (≠ V348), N263 (= N414), D308 (= D458)
- binding calcium ion: E185 (≠ V348), N263 (= N414), D308 (= D458)
- binding pyrroloquinoline quinone: E70 (≠ Q211), C116 (= C259), C117 (vs. gap), R122 (= R260), T167 (= T326), G182 (≠ N345), G183 (≠ F346), A184 (≠ S347), E185 (≠ V348), T243 (≠ S395), W245 (= W396), D308 (= D458), K335 (= K485)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C259), C117 (vs. gap), E185 (≠ V348), D308 (= D458)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
- binding pyrroloquinoline quinone: 394, 395, 479, 543, 544
- binding tetrahydrofuran-2-carboxylic acid: 389
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)
27% identity, 44% coverage: 161:500/781 of query aligns to 59:381/708 of Q46444
- E101 (≠ Q211) binding pyrroloquinoline quinone
- C147 (= C259) modified: Disulfide link with 148
- C148 (vs. gap) modified: Disulfide link with 147
- R153 (= R260) binding pyrroloquinoline quinone
- T198 (= T326) binding pyrroloquinoline quinone
- GA 214:215 (≠ FS 346:347) binding pyrroloquinoline quinone
- E216 (≠ V348) binding Ca(2+)
- T274 (≠ S395) binding pyrroloquinoline quinone
- N294 (= N414) binding Ca(2+)
- D339 (= D458) binding Ca(2+)
- K366 (= K485) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:31 signal peptide
- 425:426 binding pyrroloquinoline quinone
- 575 binding pyrroloquinoline quinone
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 678 binding axial binding residue
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)
26% identity, 43% coverage: 164:498/781 of query aligns to 54:391/623 of Q9Z4J7
- E95 (= E207) binding pyrroloquinoline quinone
- C139 (≠ T258) modified: Disulfide link with 140
- CC 139:140 (≠ TC 258:259) 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 (= C259) modified: Disulfide link with 139
- R145 (≠ A271) binding pyrroloquinoline quinone
- T189 (≠ S313) binding pyrroloquinoline quinone
- HGS 207:209 (≠ GGA 339:341) binding pyrroloquinoline quinone
- E213 (≠ N345) binding Ca(2+)
- N300 (= N414) binding Ca(2+)
- D350 (= D458) binding Ca(2+)
- R378 (≠ K485) 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+)
- 523 binding pyrroloquinoline quinone
- 587 binding pyrroloquinoline quinone
Query Sequence
>WP_069333644.1 NCBI__GCF_003046325.1:WP_069333644.1
MTATLTAIVLALAGLGLLIPGAWLAVLGGSWFYLVAGALMLLTGWQVFRRSSSAEWIYGG
LILGALVWSVWEVGFDWWELIPRGGIIAVLGIWLYLPFMRRQLLTEDGHPAPGLPLALPL
LAAIGVAIWSWTGDEAGHAGSLPTEVVSAEPDLGPTAPPGEWHQYGRTQYGQRYSPLEQI
NIQNVAELEQVWQYQTGDVKLPQDVTETTYQVTPLKVDDRLYICTPHNLAIALDAATGKE
AWRFDANSGLEPDRQHQTCRGVTYWRDPARAEGELCAERVYLPTADARLIALDARSGAVC
TFFADEGTLHLESGMPYTPEGFYYSTSPPVAVGGRIIIGGAVNDNFSVFSQSGVIRAFDA
NTGALLWNWDSGNPDETAPIDWMNGETYTANSPNSWSVFSVDEERGLVYIPLGNQVPDQL
GFDRSPAVEEHSSSVVALDVTTGQKAWVFQTVHHDLWDMDVPAQPVLIDLDIDGQTVPAL
VQPTKQGDIYVLNRETGEPILPVTEEPAPQEGGLPEESPAPTQPTSALSFKPAALREKDM
WGVTIYDQLACRIQYHRLNYEGRYTPPSLNGTIVYPGNFGTFNWGSVAVDPERQVMFGMP
TYLPFTVELVPAEDIPPPGANETASEQGLNRNEGAPYGVIMGPFLGPLGVPCSAPPWGYV
AGADLRTGDIAYMHRNGTVRDMTPLPLPLKVGVPGIGGPIVTRGGVAFLGAAVDDYLRAY
DVTTGEQLWQARLPAGGQSTPMTYEQDGRQFVVIVAGGHGSVGTKPGDYVIAYALPGGAE
G
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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