SitesBLAST
Comparing WP_010959663.1 NCBI__GCF_000008325.1:WP_010959663.1 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)
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
70% identity, 96% coverage: 27:619/619 of query aligns to 1:562/563 of 6damA
- active site: E171 (= E201), N259 (= N289), D301 (= D331)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), C104 (= C134), R109 (= R139), T153 (= T183), S168 (= S198), G169 (= G199), G170 (= G200), E171 (= E201), T239 (= T269), W241 (= W271), D303 (= D333), R328 (= R362), N394 (= N428), W480 (= W514), G543 (= G577), W544 (= W578)
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)
61% identity, 96% coverage: 24:619/619 of query aligns to 19:599/601 of C5B120
- R130 (= R139) binding pyrroloquinoline quinone
- T174 (= T183) binding pyrroloquinoline quinone
- S189 (= S198) binding pyrroloquinoline quinone
- G190 (= G199) binding pyrroloquinoline quinone
- G191 (= G200) binding pyrroloquinoline quinone
- E192 (= E201) binding La(3+)
- W258 (= W271) binding pyrroloquinoline quinone
- N276 (= N289) binding La(3+)
- D318 (= D331) binding La(3+)
- D320 (= D333) 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 (= R362) binding pyrroloquinoline quinone
- W494 (= W514) binding pyrroloquinoline quinone
- W558 (= W578) binding pyrroloquinoline quinone
Sites not aligning to the query:
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
62% identity, 93% coverage: 46:619/619 of query aligns to 20:578/579 of 6oc6A
- active site: E171 (= E201), N255 (= N289), D297 (= D331)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), C104 (= C134), R109 (= R139), T153 (= T183), S168 (= S198), G169 (= G199), G170 (= G200), E171 (= E201), W237 (= W271), D299 (= D333), R324 (= R362), D395 (≠ N428), W473 (= W514), G536 (= G577), W537 (= W578)
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
50% identity, 96% coverage: 27:618/619 of query aligns to 1:573/573 of 7ce5A
- active site: E177 (= E201), N261 (= N289), D303 (= D331)
- binding calcium ion: E177 (= E201), N261 (= N289), D303 (= D331)
- binding methanol: E177 (= E201), W533 (= W578)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), C104 (= C134), R109 (= R139), T159 (= T183), A174 (≠ S198), G175 (= G199), A176 (≠ G200), E177 (= E201), T241 (= T269), W243 (= W271), R330 (= R362), N393 (= N428), W469 (= W514), G532 (= G577), W533 (= W578)
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
50% identity, 96% coverage: 27:618/619 of query aligns to 1:573/573 of 7cdlC
- active site: E177 (= E201), N261 (= N289), D303 (= D331)
- binding calcium ion: E177 (= E201), N261 (= N289), D303 (= D331)
- binding pyrroloquinoline quinone: E55 (= E81), R109 (= R139), T159 (= T183), A174 (≠ S198), A176 (≠ G200), E177 (= E201), T241 (= T269), W243 (= W271), D303 (= D331), R330 (= R362), N393 (= N428), W469 (= W514), G532 (= G577), W533 (= W578)
6fkwA Europium-containing methanol dehydrogenase (see paper)
51% identity, 96% coverage: 27:618/619 of query aligns to 1:576/576 of 6fkwA
- active site: E172 (= E201), N256 (= N289), D299 (= D331), D301 (= D333)
- binding europium ion: E172 (= E201), N256 (= N289), D299 (= D331), D301 (= D333)
- binding pyrroloquinoline quinone: E55 (= E81), C104 (= C133), C105 (= C134), R110 (= R139), T154 (= T183), S169 (= S198), G170 (= G199), G171 (= G200), E172 (= E201), T236 (= T269), W238 (= W271), D301 (= D333), R326 (= R362), D388 (≠ N428), W467 (= W514), G531 (= G577), W532 (= W578)
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
51% identity, 96% coverage: 27:618/619 of query aligns to 1:576/577 of 4maeA
- active site: E172 (= E201), N256 (= N289), D299 (= D331)
- binding cerium (iii) ion: E172 (= E201), N256 (= N289), D299 (= D331), D301 (= D333)
- binding pyrroloquinoline quinone: E55 (= E81), C104 (= C133), C105 (= C134), R110 (= R139), T154 (= T183), S169 (= S198), G170 (= G199), G171 (= G200), E172 (= E201), T236 (= T269), W238 (= W271), D301 (= D333), R326 (= R362), D388 (≠ N428), W467 (= W514), G531 (= G577), W532 (= W578)
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)
49% identity, 96% coverage: 24:618/619 of query aligns to 25:607/626 of P16027
- C130 (= C133) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (= C134) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D331) mutation to E: Lower affinity for methanol.
- C413 (= C420) modified: Disulfide link with 442
- C442 (= C449) modified: Disulfide link with 413
Sites not aligning to the query:
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
49% identity, 96% coverage: 27:618/619 of query aligns to 1:580/596 of 1w6sC
- active site: E177 (= E201), N261 (= N289), D303 (= D331)
- binding calcium ion: E177 (= E201), N261 (= N289)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), C104 (= C134), R109 (= R139), T159 (= T183), S174 (= S198), A176 (≠ G200), E177 (= E201), T241 (= T269), W243 (= W271), R331 (= R362), N394 (= N428), W476 (= W514), W540 (= W578)
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
46% identity, 98% coverage: 10:618/619 of query aligns to 18:611/631 of P12293
- C135 (= C133) modified: Disulfide link with 136
- C136 (= C134) modified: Disulfide link with 135
- C418 (= C420) modified: Disulfide link with 447
- C447 (= C449) modified: Disulfide link with 418
Sites not aligning to the query:
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
46% identity, 96% coverage: 27:618/619 of query aligns to 1:580/600 of 1lrwA
- active site: E177 (= E201), N261 (= N289), D303 (= D331)
- binding calcium ion: E177 (= E201), N261 (= N289), D303 (= D331)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), C104 (= C134), R109 (= R139), T159 (= T183), S174 (= S198), G175 (= G199), A176 (≠ G200), E177 (= E201), T241 (= T269), W243 (= W271), R331 (= R362), W476 (= W514), W540 (= W578)
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
49% identity, 93% coverage: 45:618/619 of query aligns to 19:571/571 of 4aahA
- active site: E171 (= E201), N255 (= N289), D297 (= D331)
- binding calcium ion: E171 (= E201), N255 (= N289)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), C104 (= C134), R109 (= R139), S168 (= S198), A170 (≠ G200), E171 (= E201), W237 (= W271), R324 (= R362), N387 (= N428), W467 (= W514), W531 (= W578)
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
48% identity, 96% coverage: 27:618/619 of query aligns to 1:580/596 of 5xm3A
- active site: E177 (= E201), N261 (= N289), D303 (= D331)
- binding magnesium ion: E177 (= E201), N261 (= N289)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C133), R109 (= R139), T159 (= T183), S174 (= S198), G175 (= G199), A176 (≠ G200), E177 (= E201), T241 (= T269), W243 (= W271), R331 (= R362), N394 (= N428), W476 (= W514), G539 (= G577), W540 (= W578)
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
48% identity, 96% coverage: 27:618/619 of query aligns to 1:580/597 of 2d0vA
- active site: E177 (= E201), N261 (= N289), D303 (= D331)
- binding calcium ion: E177 (= E201), N261 (= N289), D303 (= D331)
- binding pyrroloquinoline quinone: E55 (= E81), R109 (= R139), T159 (= T183), S174 (= S198), G175 (= G199), A176 (≠ G200), E177 (= E201), T241 (= T269), W243 (= W271), R331 (= R362), N394 (= N428), W476 (= W514), G539 (= G577), W540 (= W578)
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
45% identity, 96% coverage: 27:618/619 of query aligns to 1:588/588 of 7o6zB
- binding methanol: E173 (= E201), W263 (= W293), D314 (= D331)
- binding Neodymium Ion: E173 (= E201), N259 (= N289), D314 (= D331), D316 (= D333)
- binding pyrroloquinoline quinone: E55 (= E81), C105 (= C133), C106 (= C134), R111 (= R139), T155 (= T183), G170 (≠ S198), G171 (= G199), D172 (≠ G200), E173 (= E201), W241 (= W271), D316 (= D333), R341 (= R362), D403 (≠ N428), W481 (= W514), G544 (= G577), W545 (= W578)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
45% identity, 96% coverage: 27:618/619 of query aligns to 1:588/588 of 7o6zA
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)
39% identity, 92% coverage: 8:577/619 of query aligns to 7:553/587 of C5AXV8
- D319 (= D333) mutation to S: Loss of efficient ethanol oxidation with La(3+).
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)
37% identity, 93% coverage: 2:577/619 of query aligns to 3:556/595 of Q88JH0
- Q87 (≠ E81) binding pyrroloquinoline quinone
- C131 (= C133) modified: Disulfide link with 132
- C132 (= C134) modified: Disulfide link with 131
- R137 (= R139) binding pyrroloquinoline quinone
- S181 (≠ T183) binding pyrroloquinoline quinone
- G197 (= G199) binding pyrroloquinoline quinone
- G198 (= G200) binding pyrroloquinoline quinone
- E199 (= E201) binding Pr(3+)
- W263 (= W271) binding pyrroloquinoline quinone
- N281 (= N289) binding Pr(3+)
- D323 (= D331) binding Pr(3+)
- D325 (= D333) binding Pr(3+)
- R350 (= R362) binding pyrroloquinoline quinone
- F412 (≠ A423) mutation to 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.; mutation to 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.
- N417 (= N428) binding pyrroloquinoline quinone
- W493 (= W514) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 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
37% identity, 89% coverage: 24:577/619 of query aligns to 1:529/562 of 6zcvA
- active site: E172 (= E201), N254 (= N289), D296 (= D331)
- binding calcium ion: N161 (≠ K190), K163 (= K192), P278 (≠ V313), D279 (= D314)
- binding pyrroloquinoline quinone: Q60 (≠ E81), C104 (= C133), C105 (= C134), I108 (≠ V137), R110 (= R139), S154 (≠ T183), G170 (= G199), G171 (= G200), E172 (= E201), W236 (= W271), D298 (= D333), R323 (= R362), N390 (= N428), W466 (= W514), G529 (= G577)
Sites not aligning to the query:
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)
38% identity, 92% coverage: 51:619/619 of query aligns to 63:614/623 of Q9Z4J7
- E95 (= E81) binding pyrroloquinoline quinone
- C139 (= C133) modified: Disulfide link with 140
- CC 139:140 (= CC 133:134) 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 (= C134) modified: Disulfide link with 139
- R145 (= R139) binding pyrroloquinoline quinone
- T189 (= T183) binding pyrroloquinoline quinone
- HGS 207:209 (≠ -GI 196:197) binding pyrroloquinoline quinone
- E213 (= E201) binding Ca(2+)
- N300 (= N289) binding Ca(2+)
- D350 (= D331) binding Ca(2+)
- R378 (= R362) binding pyrroloquinoline quinone
- W523 (= W514) binding pyrroloquinoline quinone
- A587 (= A584) 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+)
Query Sequence
>WP_010959663.1 NCBI__GCF_000008325.1:WP_010959663.1
MKKPVKSWLIASSIASLLAVPGVSFANAEVEALTKDPKNFATWGGNYAGTRYSTLDQINF
KNAKHLQPVWTFSTGMLRGHEGGPLVVNDVIYIHTGYPHKVYALDQATQSVIWEYVYAPD
KGTDQSQVISVMCCDVVNRGLAYGDGKIFLAQGDATLVALDAKTGKIVWKVKNGDPKTGM
TATNAPLVVKDKVLTGISGGEFGVRGFLAAYNIKDGSLVWKKYSMGPDDEVGLDPEHTMT
WTDGKMAPVGKDSSLKTWQGDQWKIGGGTTWGWYSYDPDLNLVYYGSGNPSTWNPVQRPG
DNKWSMTIWARDVDTGEAKWVYQMTPHDEWDYDGINEMMLIDQEMTAKDGSKHSKLLTHF
DRNGFGYTLDRVTGELLVAEKFDKAVNWATHVDMKTGRPQVNPKYSTQHGGQDVDTKGIC
PSAMGAKNEPPVTYSPRTKLIYIPGNHTCMNYEPFEVEYTAGQPYVGATLNIFPARANVK
TGEKESSNHMGSFTAWDPTTGTIAWQFDEPFSLWSGMVSTAGDIVIYGTLEGYLKVRDAK
TGEELYRFKTPSGIIGNVSTWTYNGKQYIGVLSGIGGWAGVGMAAGLEGDTEGLGAVGAY
KGLSSHTKLGGVFTVFALP
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