SitesBLAST
Comparing 14270 b0124 glucose dehydrogenase (NCBI) 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)
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
29% identity, 77% coverage: 164:773/796 of query aligns to 14:521/664 of 1kv9A
- active site: E173 (≠ N355), N250 (≠ V422), D295 (= D466)
- binding acetone: E173 (≠ N355), D295 (= D466)
- binding calcium ion: E173 (≠ N355), N250 (≠ V422), D295 (= D466)
- binding heme c: A101 (≠ T256), R102 (≠ N257)
- binding pyrroloquinoline quinone: E59 (= E217), C105 (≠ F260), C106 (≠ Q261), R111 (= R266), T155 (= T336), G170 (≠ V352), A172 (≠ D354), E173 (≠ N355), T230 (≠ N402), W232 (= W404), K322 (= K493), N382 (≠ E591), W383 (= W592), W460 (≠ F705)
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
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
29% identity, 77% coverage: 164:773/796 of query aligns to 36:543/690 of Q8GR64
- E81 (= E217) binding
- C127 (≠ F260) modified: Disulfide link with 128
- C128 (≠ Q261) modified: Disulfide link with 127
- R133 (= R266) binding
- T177 (= T336) binding
- GA 193:194 (≠ TD 353:354) binding
- E195 (≠ N355) binding
- T252 (≠ N402) binding
- N272 (≠ V422) binding
- D317 (= D466) binding
- K344 (= K493) binding
- NW 404:405 (≠ EW 591:592) binding
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
- 547 binding
- 613 binding covalent
- 616 binding covalent
- 617 binding axial binding residue
- 655 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)
26% identity, 84% coverage: 117:783/796 of query aligns to 7:577/718 of Q4W6G0
- C138 (≠ F260) modified: Disulfide link with 139
- C139 (≠ Q261) modified: Disulfide link with 138
- R144 (= R266) binding
- T189 (≠ P335) binding
- GA 205:206 (≠ SV 351:352) binding
- E207 (≠ N355) binding
- T264 (≠ N402) binding
- N284 (≠ T424) binding
- D329 (= D466) binding
- K356 (= K493) binding
- W415 (≠ L587) binding
- DW 419:420 (≠ EW 591:592) binding
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)
26% identity, 78% coverage: 167:783/796 of query aligns to 21:548/684 of 1yiqA
- active site: E178 (≠ N355), N255 (≠ T424), D300 (= D466)
- binding calcium ion: E178 (≠ N355), N255 (≠ T424), D300 (= D466)
- binding pyrroloquinoline quinone: E63 (= E217), C109 (≠ F260), C110 (≠ Q261), R115 (= R266), T160 (≠ P335), G175 (= G350), G176 (≠ S351), A177 (≠ V352), E178 (≠ N355), T235 (≠ N402), W237 (= W404), K327 (= K493), D390 (≠ E591), W391 (= W592), F477 (= F705), A542 (≠ S777)
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
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
27% identity, 76% coverage: 168:768/796 of query aligns to 14:522/571 of 4aahA
- active site: E171 (≠ D354), N255 (≠ V422), D297 (= D466)
- binding calcium ion: E171 (≠ D354), N255 (≠ V422)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (= C265), C104 (vs. gap), R109 (= R266), S168 (= S351), A170 (≠ T353), E171 (≠ D354), W237 (= W404), R324 (≠ K493), N387 (≠ E591), W467 (≠ L712)
Sites not aligning to the query:
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
25% identity, 77% coverage: 164:773/796 of query aligns to 10:536/597 of 2d0vA
- active site: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding calcium ion: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding pyrroloquinoline quinone: E55 (= E217), R109 (= R266), T159 (≠ P335), S174 (≠ V352), G175 (≠ T353), A176 (≠ D354), E177 (≠ N355), T241 (vs. gap), W243 (= W404), R331 (≠ K493), N394 (≠ E591), W476 (≠ L712)
Sites not aligning to the query:
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
25% identity, 76% coverage: 167:773/796 of query aligns to 13:536/600 of 1lrwA
- active site: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding calcium ion: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (= C265), C104 (vs. gap), R109 (= R266), T159 (≠ P335), S174 (≠ V352), G175 (≠ T353), A176 (≠ D354), E177 (≠ N355), T241 (vs. gap), W243 (= W404), R331 (≠ K493), W476 (≠ L712)
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)
24% identity, 83% coverage: 116:773/796 of query aligns to 6:567/631 of P12293
- C135 (= C265) modified: Disulfide link with 136
- C136 (vs. gap) modified: Disulfide link with 135
- C418 (≠ F583) modified: Disulfide link with 447
- C447 (≠ A610) modified: Disulfide link with 418
Sites not aligning to the query:
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
24% identity, 77% coverage: 165:773/796 of query aligns to 11:529/573 of 7ce5A
- active site: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding calcium ion: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding methanol: E177 (≠ N355)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (= C265), C104 (vs. gap), R109 (= R266), T159 (≠ P330), A174 (≠ V352), G175 (≠ T353), A176 (≠ D354), E177 (≠ N355), T241 (vs. gap), W243 (= W404), R330 (≠ K493), N393 (≠ E591), W469 (≠ L712)
Sites not aligning to the query:
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
24% identity, 77% coverage: 165:773/796 of query aligns to 11:529/573 of 7cdlC
- active site: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding calcium ion: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding pyrroloquinoline quinone: E55 (= E217), R109 (= R266), T159 (≠ P330), A174 (≠ V352), A176 (≠ D354), E177 (≠ N355), T241 (vs. gap), W243 (= W404), D303 (= D466), R330 (≠ K493), N393 (≠ E591), W469 (≠ L712)
Sites not aligning to the query:
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
25% identity, 77% coverage: 164:773/796 of query aligns to 10:536/596 of 1w6sC
- active site: E177 (≠ N355), N261 (≠ T424), D303 (= D466)
- binding calcium ion: E177 (≠ N355), N261 (≠ T424)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (= C265), C104 (vs. gap), R109 (= R266), T159 (≠ P335), S174 (≠ V352), A176 (≠ D354), E177 (≠ N355), T241 (vs. gap), W243 (= W404), R331 (≠ K493), N394 (≠ E591), W476 (≠ L712)
Sites not aligning to the query:
P16027 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) (see 3 papers)
25% identity, 77% coverage: 164:773/796 of query aligns to 37:563/626 of P16027
- C130 (= C265) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (vs. gap) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D466) mutation to E: Lower affinity for methanol.
- C413 (≠ M562) modified: Disulfide link with 442
- C442 (≠ A610) modified: Disulfide link with 413
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)
30% identity, 43% coverage: 167:512/796 of query aligns to 53:388/757 of O05542
Sites not aligning to the query:
- 1:34 signal peptide
- 35 modified: Pyrrolidone carboxylic acid
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
27% identity, 43% coverage: 167:509/796 of query aligns to 13:344/563 of 6damA
- active site: E171 (≠ N355), N259 (≠ T424), D301 (= D466)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (≠ T264), C104 (= C265), R109 (= R266), T153 (≠ P335), S168 (≠ V352), G169 (≠ T353), G170 (≠ D354), E171 (≠ N355), T239 (≠ N402), W241 (= W404), D303 (= D468), R328 (≠ K493)
Sites not aligning to the query:
8gy2A Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
30% identity, 43% coverage: 167:512/796 of query aligns to 19:354/723 of 8gy2A
- binding calcium ion: E181 (≠ N355), N263 (≠ V422), D308 (= D466)
- binding heme c: D104 (vs. gap)
- binding pyrroloquinoline quinone: C107 (≠ F260), C108 (≠ Q261), D163 (≠ T336), G179 (≠ T353), A180 (≠ D354), E181 (≠ N355), W245 (= W404), N263 (≠ V422), D308 (= D466), K335 (= K493)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
- binding pyrroloquinoline quinone: 398, 489
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
24% identity, 77% coverage: 164:773/796 of query aligns to 10:536/596 of 5xm3A
- active site: E177 (≠ N355), N261 (≠ V422), D303 (= D466)
- binding magnesium ion: E177 (≠ N355), N261 (≠ V422)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (= C265), R109 (= R266), T159 (≠ P335), S174 (≠ V352), G175 (≠ T353), A176 (≠ D354), E177 (≠ N355), T241 (vs. gap), W243 (= W404), R331 (≠ K493), N394 (≠ E591), W476 (≠ L712)
Sites not aligning to the query:
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
28% identity, 43% coverage: 168:512/796 of query aligns to 14:345/577 of 4maeA
- active site: E172 (≠ N355), N256 (≠ T424), D299 (= D466)
- binding cerium (iii) ion: E172 (≠ N355), N256 (≠ T424), D299 (= D466), D301 (= D468)
- binding pyrroloquinoline quinone: E55 (= E217), C104 (≠ T264), C105 (= C265), R110 (= R266), T154 (≠ P335), S169 (≠ V352), G170 (≠ T353), G171 (≠ D354), E172 (≠ N355), T236 (≠ N402), W238 (= W404), D301 (= D468), R326 (≠ K493)
Sites not aligning to the query:
6fkwA Europium-containing methanol dehydrogenase (see paper)
28% identity, 43% coverage: 168:512/796 of query aligns to 14:345/576 of 6fkwA
- active site: E172 (≠ N355), N256 (≠ T424), D299 (= D466), D301 (= D468)
- binding europium ion: E172 (≠ N355), N256 (≠ T424), D299 (= D466), D301 (= D468)
- binding pyrroloquinoline quinone: E55 (= E217), C104 (≠ T264), C105 (= C265), R110 (= R266), T154 (≠ P335), S169 (≠ V352), G170 (≠ T353), G171 (≠ D354), E172 (≠ N355), T236 (≠ N402), W238 (= W404), D301 (= D468), R326 (≠ K493)
Sites not aligning to the query:
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
29% identity, 43% coverage: 167:508/796 of query aligns to 28:350/670 of 1kb0A
- active site: E185 (≠ N355), N263 (≠ V422), D308 (= D466)
- binding calcium ion: E185 (≠ N355), N263 (≠ V422), D308 (= D466)
- binding pyrroloquinoline quinone: E70 (= E217), C116 (vs. gap), C117 (vs. gap), R122 (= R266), T167 (≠ P335), G182 (= G350), G183 (≠ S351), A184 (≠ V352), E185 (≠ N355), T243 (vs. gap), W245 (vs. gap), D308 (= D466), K335 (= K493)
- binding tetrahydrofuran-2-carboxylic acid: C116 (vs. gap), C117 (vs. gap), E185 (≠ N355), D308 (= D466)
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)
29% identity, 43% coverage: 167:508/796 of query aligns to 59:381/708 of Q46444
- E101 (= E217) binding
- C147 (vs. gap) modified: Disulfide link with 148
- C148 (vs. gap) modified: Disulfide link with 147
- R153 (= R266) binding
- T198 (≠ P335) binding
- GA 214:215 (≠ TD 353:354) binding
- E216 (≠ N355) binding
- T274 (vs. gap) binding
- N294 (≠ V422) binding
- D339 (= D466) binding
- K366 (= K493) binding
Sites not aligning to the query:
- 1:31 signal peptide
- 425:426 binding
- 575 binding
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 678 binding axial binding residue
Query Sequence
>14270 b0124 glucose dehydrogenase (NCBI)
MAINNTGSRRLLVTLTALFAALCGLYLLIGGGWLVAIGGSWYYPIAGLVMLGVAWMLWRS
KRAALWLYAALLLGTMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLVIPASGA
VAALVVALLISGGILTWAGFNDPQEINGTLSADATPAEAISPVADQDWPAYGRNQEGQRF
SPLKQINADNVHNLKEAWVFRTGDVKQPNDPGEITNEVTPIKVGDTLYLCTAHQRLFALD
AASGKEKWHYDPELKTNESFQHVTCRGVSYHEAKAETASPEVMADCPRRIILPVNDGRLI
AINAENGKLCETFANKGVLNLQSNMPDTKPGLYEPTSPPIITDKTIVMAGSVTDNFSTRE
TSGVIRGFDVNTGELLWAFDPGAKDPNAIPSDEHTFTFNSPNSWAPAAYDAKLDLVYLPM
GVTTPDIWGGNRTPEQERYASSILALNATTGKLAWSYQTVHHDLWDMDLPAQPTLADITV
NGQKVPVIYAPAKTGNIFVLDRRNGELVVPAPEKPVPQGAAKGDYVTPTQPFSELSFRPT
KDLSGADMWGATMFDQLVCRVMFHQMRYEGIFTPPSEQGTLVFPGNLGMFEWGGISVDPN
REVAIANPMALPFVSKLIPRGPGNPMEQPKDAKGTGTESGIQPQYGVPYGVTLNPFLSPF
GLPCKQPAWGYISALDLKTNEVVWKKRIGTPQDSMPFPMPVPVPFNMGMPMLGGPISTAG
NVLFIAATADNYLRAYNMSNGEKLWQGRLPAGGQATPMTYEVNGKQYVVISAGGHGSFGT
KMGDYIVAYALPDDVK
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