SitesBLAST
Comparing 3607055 FitnessBrowser__Dino:3607055 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)
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
76% identity, 97% coverage: 22:600/600 of query aligns to 1:579/579 of 6oc6A
- active site: E171 (= E192), N255 (= N276), D297 (= D318)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), C104 (= C125), R109 (= R130), T153 (= T174), S168 (= S189), G169 (= G190), G170 (= G191), E171 (= E192), W237 (= W258), D299 (= D320), R324 (= R345), D395 (= D416), W473 (= W494), G536 (= G557), W537 (= W558)
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
63% identity, 97% coverage: 22:600/600 of query aligns to 1:563/563 of 6damA
- active site: E171 (= E192), N259 (= N276), D301 (= D318)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), C104 (= C125), R109 (= R130), T153 (= T174), S168 (= S189), G169 (= G190), G170 (= G191), E171 (= E192), T239 (= T256), W241 (= W258), D303 (= D320), R328 (= R345), N394 (≠ D416), W480 (= W494), G543 (= G557), W544 (= W558)
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
51% identity, 96% coverage: 22:598/600 of query aligns to 1:573/573 of 7ce5A
- active site: E177 (= E192), N261 (= N276), D303 (= D318)
- binding calcium ion: E177 (= E192), N261 (= N276), D303 (= D318)
- binding methanol: E177 (= E192), W533 (= W558)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), C104 (= C125), R109 (= R130), T159 (= T174), A174 (≠ S189), G175 (= G190), A176 (≠ G191), E177 (= E192), T241 (= T256), W243 (= W258), R330 (= R345), N393 (≠ D416), W469 (= W494), G532 (= G557), W533 (= W558)
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
51% identity, 96% coverage: 22:598/600 of query aligns to 1:573/573 of 7cdlC
- active site: E177 (= E192), N261 (= N276), D303 (= D318)
- binding calcium ion: E177 (= E192), N261 (= N276), D303 (= D318)
- binding pyrroloquinoline quinone: E55 (= E76), R109 (= R130), T159 (= T174), A174 (≠ S189), A176 (≠ G191), E177 (= E192), T241 (= T256), W243 (= W258), D303 (= D318), R330 (= R345), N393 (≠ D416), W469 (= W494), G532 (= G557), W533 (= W558)
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
50% identity, 98% coverage: 10:598/600 of query aligns to 21:611/631 of P12293
- C135 (= C124) modified: Disulfide link with 136
- C136 (= C125) modified: Disulfide link with 135
- C418 (= C408) modified: Disulfide link with 447
- C447 (= C437) modified: Disulfide link with 418
Sites not aligning to the query:
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
50% identity, 96% coverage: 22:598/600 of query aligns to 1:580/600 of 1lrwA
- active site: E177 (= E192), N261 (= N276), D303 (= D318)
- binding calcium ion: E177 (= E192), N261 (= N276), D303 (= D318)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), C104 (= C125), R109 (= R130), T159 (= T174), S174 (= S189), G175 (= G190), A176 (≠ G191), E177 (= E192), T241 (= T256), W243 (= W258), R331 (= R345), W476 (= W494), W540 (= W558)
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
49% identity, 96% coverage: 24:598/600 of query aligns to 3:571/571 of 4aahA
- active site: E171 (= E192), N255 (= N276), D297 (= D318)
- binding calcium ion: E171 (= E192), N255 (= N276)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), C104 (= C125), R109 (= R130), S168 (= S189), A170 (≠ G191), E171 (= E192), W237 (= W258), R324 (= R345), N387 (≠ D416), W467 (= W494), W531 (= W558)
6fkwA Europium-containing methanol dehydrogenase (see paper)
52% identity, 96% coverage: 22:598/600 of query aligns to 1:576/576 of 6fkwA
- active site: E172 (= E192), N256 (= N276), D299 (= D318), D301 (= D320)
- binding europium ion: E172 (= E192), N256 (= N276), D299 (= D318), D301 (= D320)
- binding pyrroloquinoline quinone: E55 (= E76), C104 (= C124), C105 (= C125), R110 (= R130), T154 (= T174), S169 (= S189), G170 (= G190), G171 (= G191), E172 (= E192), T236 (= T256), W238 (= W258), D301 (= D320), R326 (= R345), D388 (= D416), W467 (= W494), G531 (= G557), W532 (= W558)
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
52% identity, 96% coverage: 22:598/600 of query aligns to 1:576/577 of 4maeA
- active site: E172 (= E192), N256 (= N276), D299 (= D318)
- binding cerium (iii) ion: E172 (= E192), N256 (= N276), D299 (= D318), D301 (= D320)
- binding pyrroloquinoline quinone: E55 (= E76), C104 (= C124), C105 (= C125), R110 (= R130), T154 (= T174), S169 (= S189), G170 (= G190), G171 (= G191), E172 (= E192), T236 (= T256), W238 (= W258), D301 (= D320), R326 (= R345), D388 (= D416), W467 (= W494), G531 (= G557), W532 (= W558)
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)
50% identity, 97% coverage: 19:598/600 of query aligns to 25:607/626 of P16027
- C130 (= C124) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (= C125) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D318) mutation to E: Lower affinity for methanol.
- C413 (= C408) modified: Disulfide link with 442
- C442 (= C437) modified: Disulfide link with 413
Sites not aligning to the query:
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
50% identity, 96% coverage: 22:598/600 of query aligns to 1:580/597 of 2d0vA
- active site: E177 (= E192), N261 (= N276), D303 (= D318)
- binding calcium ion: E177 (= E192), N261 (= N276), D303 (= D318)
- binding pyrroloquinoline quinone: E55 (= E76), R109 (= R130), T159 (= T174), S174 (= S189), G175 (= G190), A176 (≠ G191), E177 (= E192), T241 (= T256), W243 (= W258), R331 (= R345), N394 (≠ D416), W476 (= W494), G539 (= G557), W540 (= W558)
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
49% identity, 96% coverage: 22:598/600 of query aligns to 1:580/596 of 1w6sC
- active site: E177 (= E192), N261 (= N276), D303 (= D318)
- binding calcium ion: E177 (= E192), N261 (= N276)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), C104 (= C125), R109 (= R130), T159 (= T174), S174 (= S189), A176 (≠ G191), E177 (= E192), T241 (= T256), W243 (= W258), R331 (= R345), N394 (≠ D416), W476 (= W494), W540 (= W558)
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
49% identity, 96% coverage: 22:598/600 of query aligns to 1:580/596 of 5xm3A
- active site: E177 (= E192), N261 (= N276), D303 (= D318)
- binding magnesium ion: E177 (= E192), N261 (= N276)
- binding pyrroloquinoline quinone: E55 (= E76), C103 (= C124), R109 (= R130), T159 (= T174), S174 (= S189), G175 (= G190), A176 (≠ G191), E177 (= E192), T241 (= T256), W243 (= W258), R331 (= R345), N394 (≠ D416), W476 (= W494), G539 (= G557), W540 (= W558)
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
47% identity, 96% coverage: 22:598/600 of query aligns to 1:588/588 of 7o6zB
- binding methanol: E173 (= E192), W263 (= W280), D314 (= D318)
- binding Neodymium Ion: E173 (= E192), N259 (= N276), D314 (= D318), D316 (= D320)
- binding pyrroloquinoline quinone: E55 (= E76), C105 (= C124), C106 (= C125), R111 (= R130), T155 (= T174), G170 (≠ S189), G171 (= G190), D172 (≠ G191), E173 (= E192), W241 (= W258), D316 (= D320), R341 (= R345), D403 (= D416), W481 (= W494), G544 (= G557), W545 (= W558)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
47% identity, 96% coverage: 22:598/600 of query aligns to 1:588/588 of 7o6zA
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
35% identity, 90% coverage: 19:557/600 of query aligns to 1:529/562 of 6zcvA
- active site: E172 (= E192), N254 (= N276), D296 (= D318)
- binding calcium ion: N161 (≠ K181), K163 (= K183), P278 (≠ I300), D279 (= D301)
- binding pyrroloquinoline quinone: Q60 (≠ E76), C104 (= C124), C105 (= C125), I108 (≠ V128), R110 (= R130), S154 (≠ T174), G170 (= G190), G171 (= G191), E172 (= E192), W236 (= W258), D298 (= D320), R323 (= R345), N390 (≠ D416), W466 (= W494), G529 (= G557)
Sites not aligning to the query:
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
36% identity, 92% coverage: 5:557/600 of query aligns to 13:570/718 of Q4W6G0
- C138 (= C124) modified: Disulfide link with 139
- C139 (= C125) modified: Disulfide link with 138
- R144 (= R130) binding
- T189 (= T174) binding
- GA 205:206 (≠ GG 190:191) binding
- E207 (= E192) binding
- T264 (= T256) binding
- N284 (= N276) binding
- D329 (= D318) binding
- K356 (≠ R345) binding
- W415 (≠ L412) binding
- DW 419:420 (≠ DQ 416:417) 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)
37% identity, 89% coverage: 25:557/600 of query aligns to 12:541/684 of 1yiqA
- active site: E178 (= E192), N255 (= N276), D300 (= D318)
- binding calcium ion: E178 (= E192), N255 (= N276), D300 (= D318)
- binding pyrroloquinoline quinone: E63 (= E76), C109 (= C124), C110 (= C125), R115 (= R130), T160 (= T174), G175 (≠ S189), G176 (= G190), A177 (≠ G191), E178 (= E192), T235 (= T256), W237 (= W258), K327 (≠ R345), D390 (= D416), W391 (≠ Q417), F477 (≠ V493)
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
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)
36% identity, 91% coverage: 41:588/600 of query aligns to 66:607/708 of Q46444
- E101 (= E76) binding
- C147 (= C124) modified: Disulfide link with 148
- C148 (= C125) modified: Disulfide link with 147
- R153 (= R130) binding
- T198 (= T174) binding
- GA 214:215 (≠ GG 190:191) binding
- E216 (= E192) binding
- T274 (= T256) binding
- N294 (= N276) binding
- D339 (= D318) binding
- K366 (≠ R345) binding
- NW 425:426 (≠ DQ 416:417) binding
- V575 (≠ I561) binding
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
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
37% identity, 88% coverage: 41:568/600 of query aligns to 35:552/670 of 1kb0A
- active site: E185 (= E192), N263 (= N276), D308 (= D318)
- binding calcium ion: E185 (= E192), N263 (= N276), D308 (= D318)
- binding pyrroloquinoline quinone: E70 (= E76), C116 (= C124), C117 (= C125), R122 (= R130), T167 (= T174), G182 (≠ S189), G183 (= G190), A184 (≠ G191), E185 (= E192), T243 (= T256), W245 (= W258), D308 (= D318), K335 (≠ R345), N394 (≠ D416), W395 (≠ Q417), W479 (= W494), G543 (= G560), V544 (≠ I561)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C124), C117 (= C125), E185 (= E192), D308 (= D318), P389 (≠ A411)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
Query Sequence
>3607055 FitnessBrowser__Dino:3607055
MRRFSLLTSGIALCAATVAYANDDLITQMDDSKQWAIQTGDYKNHRYSELDEINAENVGD
LQVAWTFSTGVLRGHEGSPLVIGDTMYVHTPFPNIVYALDLSNEGKIIWKYEPKQDPDVI
PVMCCDTVNRGVAYADGKIFLHQADTKVVALDANTGDVLWEVQNGDPSIGETNTATVLPV
KDKVIVGISGGEFGVRGHVTAYDINSGELVWRAYSLGPDDDMLVDPENTTHLGKPIGENS
SLNSWEGDQWMIGGGTTWGWYAADMEENLFYYGTGNPSTWNPAQRPGDNRWTMTVMARDI
DTGMAKWFYQMTPHDEWDYDGVNENILTEQEFDGEMRKLLTRFDRNGLAYTMDRVTGELL
VAEKFDPVVNWTTGVDMDPNSETYGRPQVVAQYSTAQNGEDVNTTGICPAALGTKDQQPA
AYSPKTQVFYVPTNHVCMDYEPFRVSYTAGQPYVGATLSMYPAPDSHGGMGNFIAWDNIN
GEILWSIPEKFSVWSGALATAGDVVFYGTLEGHLKAVHADTGEELYRFKTPSGIIGNVMT
YEHDGRQYVGVLSGVGGWAGIGLAAGLTNPNDGLGAVGGYAALSDYTALGGQLTVFALPN
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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