SitesBLAST
Comparing AZOBR_RS04835 FitnessBrowser__azobra:AZOBR_RS04835 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)
6fkwA Europium-containing methanol dehydrogenase (see paper)
53% identity, 99% coverage: 1:555/559 of query aligns to 16:576/576 of 6fkwA
- active site: E172 (= E157), N256 (= N241), D299 (= D283), D301 (= D285)
- binding europium ion: E172 (= E157), N256 (= N241), D299 (= D283), D301 (= D285)
- binding pyrroloquinoline quinone: E55 (= E40), C104 (= C89), C105 (= C90), R110 (= R95), T154 (= T139), S169 (≠ A154), G170 (= G155), G171 (= G156), E172 (= E157), T236 (= T221), W238 (= W223), D301 (= D285), R326 (= R310), D388 (= D372), W467 (= W448), G531 (= G512), W532 (= W513)
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
53% identity, 99% coverage: 1:555/559 of query aligns to 16:576/577 of 4maeA
- active site: E172 (= E157), N256 (= N241), D299 (= D283)
- binding cerium (iii) ion: E172 (= E157), N256 (= N241), D299 (= D283), D301 (= D285)
- binding pyrroloquinoline quinone: E55 (= E40), C104 (= C89), C105 (= C90), R110 (= R95), T154 (= T139), S169 (≠ A154), G170 (= G155), G171 (= G156), E172 (= E157), T236 (= T221), W238 (= W223), D301 (= D285), R326 (= R310), D388 (= D372), W467 (= W448), G531 (= G512), W532 (= W513)
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
49% identity, 99% coverage: 5:557/559 of query aligns to 20:579/579 of 6oc6A
- active site: E171 (= E157), N255 (= N241), D297 (= D283)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), C104 (= C90), R109 (= R95), T153 (= T139), S168 (≠ A154), G169 (= G155), G170 (= G156), E171 (= E157), W237 (= W223), D299 (= D285), R324 (= R310), D395 (= D372), W473 (= W448), G536 (= G512), W537 (= W513)
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
47% identity, 99% coverage: 4:555/559 of query aligns to 19:588/588 of 7o6zB
- binding methanol: E173 (= E157), W263 (= W245), D314 (= D283)
- binding Neodymium Ion: E173 (= E157), N259 (= N241), D314 (= D283), D316 (= D285)
- binding pyrroloquinoline quinone: E55 (= E40), C105 (= C89), C106 (= C90), R111 (= R95), T155 (= T139), G170 (≠ A154), G171 (= G155), D172 (≠ G156), E173 (= E157), W241 (= W223), D316 (= D285), R341 (= R310), D403 (= D372), W481 (= W448), G544 (= G512), W545 (= W513)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
47% identity, 99% coverage: 4:555/559 of query aligns to 19:588/588 of 7o6zA
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
46% identity, 99% coverage: 5:556/559 of query aligns to 20:562/563 of 6damA
- active site: E171 (= E157), N259 (= N241), D301 (= D283)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), C104 (= C90), R109 (= R95), T153 (= T139), S168 (≠ A154), G169 (= G155), G170 (= G156), E171 (= E157), T239 (= T221), W241 (= W223), D303 (= D285), R328 (= R310), N394 (≠ D372), W480 (= W448), G543 (= G512), W544 (= W513)
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
45% identity, 99% coverage: 1:555/559 of query aligns to 16:573/573 of 7ce5A
- active site: E177 (= E157), N261 (= N241), D303 (= D283)
- binding calcium ion: E177 (= E157), N261 (= N241), D303 (= D283)
- binding methanol: E177 (= E157), W533 (= W513)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), C104 (= C90), R109 (= R95), T159 (= T139), A174 (= A154), G175 (= G155), A176 (≠ G156), E177 (= E157), T241 (= T221), W243 (= W223), R330 (= R310), N393 (≠ D372), W469 (= W448), G532 (= G512), W533 (= W513)
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
45% identity, 99% coverage: 1:555/559 of query aligns to 16:573/573 of 7cdlC
- active site: E177 (= E157), N261 (= N241), D303 (= D283)
- binding calcium ion: E177 (= E157), N261 (= N241), D303 (= D283)
- binding pyrroloquinoline quinone: E55 (= E40), R109 (= R95), T159 (= T139), A174 (= A154), A176 (≠ G156), E177 (= E157), T241 (= T221), W243 (= W223), D303 (= D283), R330 (= R310), N393 (≠ D372), W469 (= W448), G532 (= G512), W533 (= W513)
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
46% identity, 99% coverage: 1:555/559 of query aligns to 16:580/596 of 5xm3A
- active site: E177 (= E157), N261 (= N241), D303 (= D283)
- binding magnesium ion: E177 (= E157), N261 (= N241)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), R109 (= R95), T159 (= T139), S174 (≠ A154), G175 (= G155), A176 (≠ G156), E177 (= E157), T241 (= T221), W243 (= W223), R331 (= R310), N394 (≠ D372), W476 (= W448), G539 (= G512), W540 (= W513)
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
45% identity, 99% coverage: 1:555/559 of query aligns to 16:580/600 of 1lrwA
- active site: E177 (= E157), N261 (= N241), D303 (= D283)
- binding calcium ion: E177 (= E157), N261 (= N241), D303 (= D283)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), C104 (= C90), R109 (= R95), T159 (= T139), S174 (≠ A154), G175 (= G155), A176 (≠ G156), E177 (= E157), T241 (= T221), W243 (= W223), R331 (= R310), W476 (= W448), W540 (= W513)
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
44% identity, 99% coverage: 1:555/559 of query aligns to 48:611/631 of P12293
- C135 (= C89) modified: Disulfide link with 136
- C136 (= C90) modified: Disulfide link with 135
- C418 (= C364) modified: Disulfide link with 447
- C447 (= C393) modified: Disulfide link with 418
Sites not aligning to the query:
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
45% identity, 99% coverage: 1:555/559 of query aligns to 16:580/596 of 1w6sC
- active site: E177 (= E157), N261 (= N241), D303 (= D283)
- binding calcium ion: E177 (= E157), N261 (= N241)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), C104 (= C90), R109 (= R95), T159 (= T139), S174 (≠ A154), A176 (≠ G156), E177 (= E157), T241 (= T221), W243 (= W223), R331 (= R310), N394 (≠ D372), W476 (= W448), W540 (= W513)
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)
45% identity, 99% coverage: 1:555/559 of query aligns to 43:607/626 of P16027
- C130 (= C89) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (= C90) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D283) mutation to E: Lower affinity for methanol.
- C413 (= C364) modified: Disulfide link with 442
- C442 (= C393) modified: Disulfide link with 413
Sites not aligning to the query:
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
44% identity, 99% coverage: 1:555/559 of query aligns to 16:580/597 of 2d0vA
- active site: E177 (= E157), N261 (= N241), D303 (= D283)
- binding calcium ion: E177 (= E157), N261 (= N241), D303 (= D283)
- binding pyrroloquinoline quinone: E55 (= E40), R109 (= R95), T159 (= T139), S174 (≠ A154), G175 (= G155), A176 (≠ G156), E177 (= E157), T241 (= T221), W243 (= W223), R331 (= R310), N394 (≠ D372), W476 (= W448), G539 (= G512), W540 (= W513)
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
42% identity, 99% coverage: 1:555/559 of query aligns to 16:571/571 of 4aahA
- active site: E171 (= E157), N255 (= N241), D297 (= D283)
- binding calcium ion: E171 (= E157), N255 (= N241)
- binding pyrroloquinoline quinone: E55 (= E40), C103 (= C89), C104 (= C90), R109 (= R95), S168 (≠ A154), A170 (≠ G156), E171 (= E157), W237 (= W223), R324 (= R310), N387 (≠ D372), W467 (= W448), W531 (= W513)
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
38% identity, 92% coverage: 4:517/559 of query aligns to 56:579/718 of Q4W6G0
- C138 (= C89) modified: Disulfide link with 139
- C139 (= C90) modified: Disulfide link with 138
- R144 (= R95) binding
- T189 (= T139) binding
- GA 205:206 (≠ GG 155:156) binding
- E207 (= E157) binding
- T264 (= T221) binding
- N284 (= N241) binding
- D329 (= D283) binding
- K356 (≠ R310) binding
- W415 (≠ P368) binding
- DW 419:420 (= DW 372:373) 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
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
36% identity, 98% coverage: 10:558/559 of query aligns to 28:559/562 of 6zcvA
- active site: E172 (= E157), N254 (= N241), D296 (= D283)
- binding calcium ion: N161 (≠ K146), K163 (= K148), P278 (= P265), D279 (= D266)
- binding pyrroloquinoline quinone: Q60 (≠ E40), C104 (= C89), C105 (= C90), I108 (≠ V93), R110 (= R95), S154 (≠ T139), G170 (= G155), G171 (= G156), E172 (= E157), W236 (= W223), D298 (= D285), R323 (= R310), N390 (≠ D372), W466 (= W448), G529 (= G515), A530 (= A516)
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)
38% identity, 93% coverage: 4:522/559 of query aligns to 27:550/684 of 1yiqA
- active site: E178 (= E157), N255 (= N241), D300 (= D283)
- binding calcium ion: E178 (= E157), N255 (= N241), D300 (= D283)
- binding pyrroloquinoline quinone: E63 (= E40), C109 (= C89), C110 (= C90), R115 (= R95), T160 (= T139), G175 (≠ A154), G176 (= G155), A177 (≠ G156), E178 (= E157), T235 (= T221), W237 (= W223), K327 (≠ R310), D390 (= D372), W391 (= W373), F477 (≠ L447), A542 (= A514)
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
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
38% identity, 91% coverage: 5:512/559 of query aligns to 35:543/670 of 1kb0A
- active site: E185 (= E157), N263 (= N241), D308 (= D283)
- binding calcium ion: E185 (= E157), N263 (= N241), D308 (= D283)
- binding pyrroloquinoline quinone: E70 (= E40), C116 (= C89), C117 (= C90), R122 (= R95), T167 (= T139), G182 (≠ A154), G183 (= G155), A184 (≠ G156), E185 (= E157), T243 (= T221), W245 (= W223), D308 (= D283), K335 (≠ R310), N394 (≠ D372), W395 (= W373), W479 (≠ L447), G543 (= G512)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C89), C117 (= C90), E185 (= E157), D308 (= D283), P389 (≠ A367)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
- binding pyrroloquinoline quinone: 544
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)
38% identity, 91% coverage: 5:512/559 of query aligns to 66:574/708 of Q46444
- E101 (= E40) binding
- C147 (= C89) modified: Disulfide link with 148
- C148 (= C90) modified: Disulfide link with 147
- R153 (= R95) binding
- T198 (= T139) binding
- GA 214:215 (≠ GG 155:156) binding
- E216 (= E157) binding
- T274 (= T221) binding
- N294 (= N241) binding
- D339 (= D283) binding
- K366 (≠ R310) binding
- NW 425:426 (≠ DW 372:373) binding
Sites not aligning to the query:
- 1:31 signal peptide
- 575 binding
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 678 binding axial binding residue
Query Sequence
>AZOBR_RS04835 FitnessBrowser__azobra:AZOBR_RS04835
MAAKNYTSTRYSELDEIDTNTVRDLQVSFTFSTGVVRGHEAAPLVVNDTMYVVTPYPNKL
YALDLTKPGAPAKWTFEPRPAASAQGVACCDYVNRGPAFADGRIFINTLDAQTVAVDAET
GREVWRTKLGDINKGETMTMAPLVVKGKVLVGNAGGEFGVRGWITALDAGTGKIVWRAYN
TGPDQDVLIGDDYKPFYDKEKGKDLGVGTWPPNAWEIGGGTVWGWISYDPELDLIYHGTG
NPGPWNPEQRPGDNKWTGGIFARNPDTGQARWFYQAVPHDLYDYDGINELILLDLPWQGQ
PRKVLIRPERNGYLYVIDRSSGEVLAADPYFPANSTKGVDLKTGLIEYNEEKHPRVGKVV
RDICPTAPGAKDWNPSAFSPKTGNVYIPHNNLCMDWESVEANYIAGTPYVGANVKMYAGP
GGHRGTFTAWDPAQRRKVWELKEDLPLWSGALATAGGLVFYGTMDGWFKAVDAGSGELLW
RFKTGSGIIGQPISYRGPDGRQYIAILSGVGGWAGAIVAGDLDPHDASAAKGFVNAVSDL
PQRTTKGGMLYVFALPQRR
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