SitesBLAST
Comparing WP_038210510.1 NCBI__GCF_000745855.1:WP_038210510.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
28% identity, 78% coverage: 153:755/773 of query aligns to 56:571/708 of Q46444
- E101 (≠ D199) binding pyrroloquinoline quinone
- C147 (= C245) modified: Disulfide link with 148
- C148 (vs. gap) modified: Disulfide link with 147
- R153 (= R246) binding pyrroloquinoline quinone
- T198 (= T315) binding pyrroloquinoline quinone
- GA 214:215 (≠ VV 331:332) binding pyrroloquinoline quinone
- E216 (≠ D333) binding Ca(2+)
- T274 (≠ N381) binding pyrroloquinoline quinone
- N294 (= N401) binding Ca(2+)
- D339 (= D445) binding Ca(2+)
- K366 (= K473) binding pyrroloquinoline quinone
- NW 425:426 (= NW 573:574) 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
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)
27% identity, 79% coverage: 151:760/773 of query aligns to 16:544/684 of 1yiqA
- active site: E178 (≠ D333), N255 (= N401), D300 (= D445)
- binding calcium ion: E178 (≠ D333), N255 (= N401), D300 (= D445)
- binding pyrroloquinoline quinone: E63 (≠ Q200), C109 (= C245), C110 (vs. gap), R115 (= R246), T160 (= T315), G175 (≠ W330), G176 (≠ V331), A177 (≠ V332), E178 (≠ D333), T235 (≠ N381), W237 (= W383), K327 (= K473), D390 (≠ N573), W391 (= W574), F477 (≠ E672), A542 (= A758)
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
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
27% identity, 79% coverage: 151:760/773 of query aligns to 45:573/718 of Q4W6G0
- C138 (= C245) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (= R246) binding pyrroloquinoline quinone
- T189 (= T315) binding pyrroloquinoline quinone
- GA 205:206 (≠ VV 331:332) binding pyrroloquinoline quinone
- E207 (≠ D333) binding Ca(2+)
- T264 (≠ N381) binding pyrroloquinoline quinone
- N284 (= N401) binding Ca(2+)
- D329 (= D445) binding Ca(2+)
- K356 (= K473) binding pyrroloquinoline quinone
- W415 (≠ V569) binding substrate
- DW 419:420 (≠ NW 573:574) 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
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
28% identity, 78% coverage: 153:755/773 of query aligns to 25:540/670 of 1kb0A
- active site: E185 (≠ D333), N263 (= N401), D308 (= D445)
- binding calcium ion: E185 (≠ D333), N263 (= N401), D308 (= D445)
- binding pyrroloquinoline quinone: E70 (≠ D199), C116 (= C245), C117 (vs. gap), R122 (= R246), T167 (= T315), G182 (≠ W330), G183 (≠ V331), A184 (≠ V332), E185 (≠ D333), T243 (≠ N381), W245 (= W383), D308 (= D445), K335 (= K473), N394 (= N573), W395 (= W574), W479 (≠ L677)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C245), C117 (vs. gap), E185 (≠ D333), D308 (= D445), P389 (≠ N568)
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
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, 78% coverage: 156:755/773 of query aligns to 39:543/690 of Q8GR64
- E81 (≠ D199) binding pyrroloquinoline quinone
- C127 (= C245) modified: Disulfide link with 128
- C128 (vs. gap) modified: Disulfide link with 127
- R133 (= R246) binding pyrroloquinoline quinone
- T177 (= T315) binding pyrroloquinoline quinone
- GA 193:194 (≠ VV 331:332) binding pyrroloquinoline quinone
- E195 (≠ D333) binding Ca(2+)
- T252 (≠ N381) binding pyrroloquinoline quinone
- N272 (= N401) binding Ca(2+)
- D317 (= D445) binding Ca(2+)
- K344 (= K473) binding pyrroloquinoline quinone
- NW 404:405 (= NW 573:574) 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)
27% identity, 78% coverage: 156:755/773 of query aligns to 17:521/664 of 1kv9A
- active site: E173 (≠ D333), N250 (= N401), D295 (= D445)
- binding acetone: E173 (≠ D333), D295 (= D445)
- binding calcium ion: E173 (≠ D333), N250 (= N401), D295 (= D445)
- binding heme c: A101 (≠ F241), R102 (≠ W242)
- binding pyrroloquinoline quinone: E59 (≠ D199), C105 (= C245), C106 (vs. gap), R111 (= R246), T155 (= T315), G170 (≠ W330), A172 (≠ V332), E173 (≠ D333), T230 (≠ N381), W232 (= W383), K322 (= K473), N382 (= N573), W383 (= W574), W460 (vs. gap)
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
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)
25% identity, 81% coverage: 132:755/773 of query aligns to 29:584/757 of O05542
- Q35 (≠ R138) modified: Pyrrolidone carboxylic acid
Sites not aligning to the query:
8gy2A Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
25% identity, 80% coverage: 138:755/773 of query aligns to 1:550/723 of 8gy2A
- binding calcium ion: E181 (≠ D333), N263 (= N401), D308 (= D445)
- binding heme c: D104 (≠ Q243)
- binding pyrroloquinoline quinone: C107 (vs. gap), C108 (vs. gap), D163 (≠ T315), G179 (≠ V331), A180 (≠ V332), E181 (≠ D333), W245 (= W383), N263 (= N401), D308 (= D445), K335 (= K473), F398 (≠ W574), W489 (≠ L677)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
25% identity, 78% coverage: 153:755/773 of query aligns to 10:541/588 of 7o6zB
- binding methanol: E173 (≠ D333), W263 (vs. gap), D314 (= D445)
- binding Neodymium Ion: E173 (≠ D333), N259 (= N401), D314 (= D445), D316 (= D447)
- binding pyrroloquinoline quinone: E55 (≠ V198), C105 (= C265), C106 (≠ R266), R111 (vs. gap), T155 (= T315), G170 (≠ W330), G171 (≠ V331), D172 (≠ V332), E173 (≠ D333), W241 (= W383), D316 (= D447), R341 (≠ K473), D403 (≠ N573), W481 (≠ Y692)
Sites not aligning to the query:
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
25% identity, 78% coverage: 153:755/773 of query aligns to 10:541/588 of 7o6zA
Sites not aligning to the query:
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
25% identity, 80% coverage: 153:773/773 of query aligns to 10:562/563 of 6damA
- active site: E171 (≠ P340), N259 (= N401), D301 (= D445)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), C104 (= C245), R109 (= R246), T153 (= T315), S168 (≠ R337), G169 (= G338), G170 (≠ E339), E171 (≠ P340), T239 (≠ N381), W241 (= W383), D303 (= D447), R328 (≠ K473), N394 (= N573), W480 (≠ Y692), G543 (≠ A758), W544 (≠ Y759)
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: 153:755/773 of query aligns to 36:566/617 of A0A3F2YLY8
- C129 (≠ R244) modified: Disulfide link with 130
- C130 (= C245) modified: Disulfide link with 129
- R135 (= R246) binding pyrroloquinoline quinone
- T179 (= T315) binding pyrroloquinoline quinone
- S194 (≠ R337) binding pyrroloquinoline quinone
- G195 (= G338) binding pyrroloquinoline quinone
- G196 (≠ E339) binding pyrroloquinoline quinone
- E197 (≠ P340) binding La(3+)
- T265 (≠ N381) binding pyrroloquinoline quinone
- W267 (= W383) binding pyrroloquinoline quinone
- N285 (= N401) binding La(3+)
- D327 (= D445) binding La(3+)
- D329 (= D447) binding La(3+)
- R354 (≠ K473) binding pyrroloquinoline quinone
- C412 (≠ H565) modified: Disulfide link with 441
- N420 (= N573) binding pyrroloquinoline quinone
- C441 (≠ P594) modified: Disulfide link with 412
- W506 (≠ Y692) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 570 binding pyrroloquinoline quinone
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, 76% coverage: 168:755/773 of query aligns to 46:554/601 of C5B120
- R130 (= R246) binding pyrroloquinoline quinone
- T174 (= T315) binding pyrroloquinoline quinone
- S189 (≠ R337) binding pyrroloquinoline quinone
- G190 (= G338) binding pyrroloquinoline quinone
- G191 (≠ E339) binding pyrroloquinoline quinone
- E192 (≠ P340) binding La(3+)
- W258 (vs. gap) binding pyrroloquinoline quinone
- N276 (≠ T403) binding La(3+)
- D318 (= D445) binding La(3+)
- D320 (= D447) 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 (≠ K473) binding pyrroloquinoline quinone
- W494 (≠ L677) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:21 signal peptide
- 558 binding pyrroloquinoline quinone
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
27% identity, 44% coverage: 152:489/773 of query aligns to 9:347/597 of 2d0vA
- active site: E177 (≠ D333), N261 (= N401), D303 (= D445)
- binding calcium ion: E177 (≠ D333), N261 (= N401), D303 (= D445)
- binding pyrroloquinoline quinone: E55 (≠ Q200), R109 (= R246), T159 (= T315), S174 (≠ W330), G175 (≠ V331), A176 (≠ V332), E177 (≠ D333), T241 (≠ N381), W243 (= W383), R331 (≠ K473)
Sites not aligning to the query:
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
26% identity, 76% coverage: 168:755/773 of query aligns to 25:533/579 of 6oc6A
- active site: E171 (≠ P340), N255 (≠ T403), D297 (= D445)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (= C245), C104 (vs. gap), R109 (= R246), T153 (= T315), S168 (≠ R337), G169 (= G338), G170 (≠ E339), E171 (≠ P340), W237 (vs. gap), D299 (= D447), R324 (≠ K473), D395 (≠ I563), W473 (≠ L677)
Sites not aligning to the query:
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)
25% identity, 43% coverage: 160:489/773 of query aligns to 46:360/587 of C5AXV8
- D319 (= D447) mutation to S: Loss of efficient ethanol oxidation with La(3+).
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
29% identity, 42% coverage: 167:494/773 of query aligns to 24:343/571 of 4aahA
- active site: E171 (≠ D333), N255 (= N401), D297 (= D445)
- binding calcium ion: E171 (≠ D333), N255 (= N401)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), C104 (= C245), R109 (= R246), S168 (≠ W330), A170 (≠ V332), E171 (≠ D333), W237 (= W383), R324 (≠ K473)
Sites not aligning to the query:
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
26% identity, 43% coverage: 156:486/773 of query aligns to 13:344/596 of 5xm3A
- active site: E177 (≠ D333), N261 (= N401), D303 (= D445)
- binding magnesium ion: E177 (≠ D333), N261 (= N401)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), R109 (= R246), T159 (= T315), S174 (≠ W330), G175 (≠ V331), A176 (≠ V332), E177 (≠ D333), T241 (≠ N381), W243 (= W383), R331 (≠ K473)
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)
27% identity, 48% coverage: 151:521/773 of query aligns to 42:412/611 of I0JWN7
- C138 (= C245) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (= R246) binding pyrroloquinoline quinone
- T188 (= T315) binding pyrroloquinoline quinone
- S203 (≠ W330) binding pyrroloquinoline quinone
- G204 (≠ V331) binding pyrroloquinoline quinone
- G205 (≠ V332) binding pyrroloquinoline quinone
- E206 (≠ D333) binding Ce(3+); binding Eu(3+)
- T270 (≠ N381) binding pyrroloquinoline quinone
- W272 (= W383) binding pyrroloquinoline quinone
- N290 (≠ T403) binding Ce(3+); binding Eu(3+)
- D333 (= D445) binding Ce(3+); binding Eu(3+)
- D335 (= D447) binding Ce(3+); binding Eu(3+)
- R360 (≠ K473) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 414 modified: Disulfide link with 443
- 443 modified: Disulfide link with 414
- 501 binding pyrroloquinoline quinone
- 566 binding pyrroloquinoline quinone
6fkwA Europium-containing methanol dehydrogenase (see paper)
27% identity, 48% coverage: 151:521/773 of query aligns to 8:378/576 of 6fkwA
- active site: E172 (≠ D333), N256 (≠ T403), D299 (= D445), D301 (= D447)
- binding europium ion: E172 (≠ D333), N256 (≠ T403), D299 (= D445), D301 (= D447)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C104 (= C245), C105 (vs. gap), R110 (= R246), T154 (= T315), S169 (≠ W330), G170 (≠ V331), G171 (≠ V332), E172 (≠ D333), T236 (≠ N381), W238 (= W383), D301 (= D447), R326 (≠ K473)
Sites not aligning to the query:
Query Sequence
>WP_038210510.1 NCBI__GCF_000745855.1:WP_038210510.1
MLVVSRVWALLVALMGLGLALGGARLLLLGGSPYYVAAGLVLLWAALQMWRRRRSSALWV
AALAVLTLPWALWESGLDFWALFPRLMAPLALAAVSLLLAPRAPEGGSAAPWRLAGAVFA
LLFVLGFGLAFMPHGVVRPDASMAYTPPGGDNRPVDWSAYGRTTEGRRDAPFDQINRETV
SQLKLAWSYRTGDTQPGVDQNTPLQIGDLVYSCTRNDKLIALDADSGQERWVFDPQAKSP
FWQRCRGLGYWKAPQEAAAAPEGACRERIVQTTIDARLIELDARTGKPCEEFGDKGTVSL
AHGMGTVRPGFYFQTSAPLVARDLIVVGGWVVDNQMRGEPSGVIRAFSARTGELVWAWDL
GNPDITKLPPEGQTYTPGTPNMWTTAAYDDKLGLIYAPLGNATPDYFGQGRPAHSDEYNA
TLVALDVATGRPRWKFQTVHHDIWDYDLPSQPALIDLPDGKGGTVPAVLQTTKRGQLFLL
DRATGQPLAEVAEKPVTQEGAVPEETLSPTQPYSVGMPTVGAERLDERRMWGMTMFDQLL
CRIEFRTLRYDGDFTPPGLQRAIEHPGNVGGLNWGSVSVDTANQRVFLNDIRVPSVFQLV
PRDDYPAFAKKYPPVSDGHGPSTQAGTPYGIYTTIWFSRLGVPCVQPPFGTLTAIDLKTR
KVAWQVPAGTAEQLGPLGVRLGLPMPIGMPTYAGTLATAGGLVFFAGTQDFYLRAYDAQT
GAEVWKHAMPVGSSATPMTYVSPRTGKQYVVISAGGAAYSKERGDYVMAFALP
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