SitesBLAST
Comparing WP_003463377.1 NCBI__GCF_000359605.1:WP_003463377.1 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)
4cpdA Alcohol dehydrogenase tadh from thermus sp. Atn1
34% identity, 99% coverage: 1:375/377 of query aligns to 1:343/346 of 4cpdA
- active site: C38 (= C38), G39 (= G39), S40 (= S40), H43 (= H43), H59 (= H59), E60 (= E60), C89 (= C89), C92 (= C92), C95 (= C95), C103 (= C103), G107 (= G114), D152 (= D161), T156 (= T165), K340 (= K372)
- binding nicotinamide-adenine-dinucleotide: G39 (= G39), S40 (= S40), T156 (= T165), G178 (= G187), P179 (= P188), V180 (≠ I189), D200 (= D209), R201 (≠ Y210), R205 (= R214), A243 (≠ C253), V244 (= V254), V266 (≠ T296), V268 (= V298), L292 (≠ Q322), A293 (= A323), F333 (= F363)
- binding zinc ion: C38 (= C38), H59 (= H59), C89 (= C89), C92 (= C92), C95 (= C95), C103 (= C103), D152 (= D161)
4jlwA Crystal structure of formaldehyde dehydrogenase from pseudomonas aeruginosa (see paper)
31% identity, 96% coverage: 2:364/377 of query aligns to 3:379/395 of 4jlwA
- binding nicotinamide-adenine-dinucleotide: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), D168 (= D161), T172 (= T165), G194 (= G187), P195 (= P188), V196 (≠ I189), D216 (= D209), R221 (= R214), V261 (= V254), R266 (≠ K259), H268 (≠ S261), V281 (≠ L272), P298 (vs. gap), L300 (vs. gap), Q336 (= Q322), T337 (≠ A323)
- binding zinc ion: C45 (= C38), H66 (= H59), C96 (= C89), C99 (= C92), C102 (= C95), C110 (= C103), D168 (= D161)
P46154 Glutathione-independent formaldehyde dehydrogenase; FALDH; FDH; Formaldehyde dismutase; EC 1.2.1.46; EC 1.2.98.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
30% identity, 96% coverage: 2:364/377 of query aligns to 5:381/399 of P46154
- C47 (= C38) binding Zn(2+)
- G48 (= G39) binding NAD(+)
- S49 (= S40) binding NAD(+)
- H52 (= H43) binding NAD(+)
- H68 (= H59) binding Zn(2+)
- C98 (= C89) binding Zn(2+)
- C101 (= C92) binding Zn(2+)
- C104 (= C95) binding Zn(2+)
- C112 (= C103) binding Zn(2+)
- V198 (≠ I189) binding NAD(+)
- D218 (= D209) binding NAD(+)
- R223 (= R214) binding NAD(+)
- V263 (= V254) binding NAD(+)
- R268 (≠ K259) binding NAD(+)
- H270 (≠ S261) binding NAD(+)
- P300 (vs. gap) binding NAD(+)
- L302 (vs. gap) binding NAD(+)
- G337 (= G321) binding NAD(+)
- T339 (≠ A323) binding NAD(+)
1kolA Crystal structure of formaldehyde dehydrogenase (see paper)
30% identity, 96% coverage: 2:364/377 of query aligns to 3:379/396 of 1kolA
- active site: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), H66 (= H59), E67 (= E60), C96 (= C89), C99 (= C92), C102 (= C95), C110 (= C103), N114 (= N107), D168 (= D161), T172 (= T165)
- binding nicotinamide-adenine-dinucleotide: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), F92 (= F85), D168 (= D161), T172 (= T165), G192 (= G185), G194 (= G187), P195 (= P188), V196 (≠ I189), D216 (= D209), L217 (≠ Y210), R221 (= R214), A260 (≠ C253), V261 (= V254), R266 (≠ K259), H268 (≠ S261), V281 (≠ T276), P298 (vs. gap), L300 (vs. gap), Q336 (= Q322), T337 (≠ A323)
- binding zinc ion: C45 (= C38), H66 (= H59), C96 (= C89), C99 (= C92), C102 (= C95), C110 (= C103), D168 (= D161)
Sites not aligning to the query:
5ylnA Zinc dependent alcohol dehydrogenase 2 from streptococcus pneumonia - apo form
30% identity, 100% coverage: 1:376/377 of query aligns to 5:342/348 of 5ylnA
Q52078 Formaldehyde dismutase; EC 1.2.98.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see paper)
39% identity, 57% coverage: 2:216/377 of query aligns to 5:225/399 of Q52078
- C46 (= C38) binding Zn(2+)
- GSDQH 47:51 (≠ GSDLH 39:43) binding NAD(+)
- H67 (= H59) binding Zn(2+)
- C97 (= C89) binding Zn(2+)
- C100 (= C92) binding Zn(2+)
- C103 (= C95) binding Zn(2+)
- C111 (= C103) binding Zn(2+)
- D170 (= D161) binding Zn(2+)
- T174 (= T165) binding NAD(+)
- PV 197:198 (≠ PI 188:189) binding NAD(+)
- DQ 218:219 (≠ DY 209:210) binding NAD(+)
- R223 (= R214) binding NAD(+)
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2:399 modified: mature protein, Formaldehyde dismutase
- 263 binding NAD(+)
- 268 binding NAD(+)
- 299 binding NAD(+)
- 299:301 binding NAD(+)
- 336:338 binding NAD(+)
2dphA Crystal structure of formaldehyde dismutase
39% identity, 57% coverage: 2:216/377 of query aligns to 4:224/398 of 2dphA
- active site: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), H66 (= H59), E67 (= E60), C96 (= C89), C99 (= C92), C102 (= C95), C110 (= C103), L114 (vs. gap), S168 (= S160), D169 (= D161), P172 (= P164)
- binding nicotinamide-adenine-dinucleotide: C45 (= C38), G46 (= G39), S47 (= S40), H50 (= H43), F92 (= F85), D169 (= D161), T173 (= T165), A192 (≠ L184), G193 (= G185), G195 (= G187), P196 (= P188), V197 (≠ I189), G216 (≠ V208), D217 (= D209), Q218 (≠ Y210), R222 (= R214)
- binding zinc ion: C45 (= C38), H66 (= H59), C96 (= C89), C99 (= C92), C102 (= C95), C110 (= C103), D169 (= D161)
Sites not aligning to the query:
3m6iA L-arabinitol 4-dehydrogenase (see paper)
27% identity, 93% coverage: 27:376/377 of query aligns to 38:356/358 of 3m6iA
- active site: C49 (= C38), G50 (= G39), S51 (= S40), H54 (= H43), H74 (= H59), E75 (= E60), C104 (= C89), C107 (= C92), C110 (= C95), C118 (= C103), D122 (≠ N107), P160 (≠ V162), A164 (= A166), K352 (= K372)
- binding nicotinamide-adenine-dinucleotide: C49 (= C38), V163 (≠ T165), G185 (= G187), P186 (= P188), I187 (= I189), D207 (= D209), R212 (= R214), C255 (= C253), T256 (≠ V254), I278 (≠ T296), G279 (= G297), V280 (= V298), R304 (≠ A323)
- binding zinc ion: C49 (= C38), H74 (= H59), C104 (= C89), C107 (= C92), C110 (= C95), C118 (= C103)
Q7SI09 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (see 2 papers)
27% identity, 93% coverage: 27:376/377 of query aligns to 42:360/363 of Q7SI09
- C53 (= C38) binding Zn(2+)
- F59 (≠ L44) mutation F->A,S,Y: No effect.
- H78 (= H59) binding Zn(2+)
- E79 (= E60) binding Zn(2+)
- C108 (= C89) binding Zn(2+)
- C111 (= C92) binding Zn(2+)
- C114 (= C95) binding Zn(2+)
- C122 (= C103) binding Zn(2+)
- E163 (≠ D161) binding Zn(2+)
- PI 190:191 (= PI 188:189) binding NAD(+)
- D211 (= D209) binding NAD(+)
- DI 211:212 (≠ DY 209:210) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-348.
- R216 (= R214) binding NAD(+)
- I282 (≠ T296) binding NAD(+)
- QYR 306:308 (≠ GQA 321:323) binding NAD(+)
- S348 (≠ N364) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 211-SR-212.
4ej6A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021
32% identity, 73% coverage: 1:277/377 of query aligns to 4:260/343 of 4ej6A
- active site: C40 (= C38), G41 (= G39), T42 (≠ S40), H45 (= H43), H61 (= H59), E62 (= E60), C91 (= C89), C94 (= C92), C97 (= C95), C105 (= C103), R109 (≠ N107), P147 (≠ V162), C151 (≠ A166)
- binding zinc ion: C91 (= C89), C94 (= C92), C97 (= C95), C105 (= C103)
Sites not aligning to the query:
4ejmA Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021 bound to NADP
32% identity, 73% coverage: 1:277/377 of query aligns to 4:260/342 of 4ejmA
- active site: C40 (= C38), G41 (= G39), T42 (≠ S40), H45 (= H43), H61 (= H59), E62 (= E60), C91 (= C89), C94 (= C92), C97 (= C95), C105 (= C103), R109 (≠ N107), P147 (≠ V162), C151 (≠ A166)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G170 (= G185), G172 (= G187), V173 (≠ P188), I174 (= I189), T194 (≠ L215), R195 (≠ E216), Q196 (≠ H217), K199 (= K220), C240 (= C253), E245 (= E264), T246 (≠ F265)
- binding zinc ion: C91 (= C89), C94 (= C92), C97 (= C95), C105 (= C103)
Sites not aligning to the query:
1rjwA Crystal structure of NAD(+)-dependent alcohol dehydrogenase from bacillus stearothermophilus strain lld-r (see paper)
33% identity, 67% coverage: 3:254/377 of query aligns to 4:239/339 of 1rjwA
- active site: C38 (= C38), H39 (≠ G39), T40 (≠ S40), H43 (= H43), H61 (= H59), E62 (= E60), C92 (= C89), C95 (= C92), C98 (= C95), C106 (= C103), K110 (≠ D111), C148 (≠ L159), T152 (= T165)
- binding trifluoroethanol: T40 (≠ S40), C148 (≠ L159)
- binding zinc ion: C38 (= C38), H61 (= H59), C92 (= C89), C95 (= C92), C98 (= C95), C106 (= C103)
Sites not aligning to the query:
3piiA Crystal structure of mutant of ht- alcohol dehydrogenase with substrate analogue butyramide
33% identity, 67% coverage: 3:254/377 of query aligns to 4:239/337 of 3piiA
- active site: C38 (= C38), H39 (≠ G39), T40 (≠ S40), H43 (= H43), H61 (= H59), E62 (= E60), C92 (= C89), C95 (= C92), C98 (= C95), C106 (= C103), K110 (≠ D111), C148 (≠ L159), T152 (= T165)
- binding butyramide: T40 (≠ S40), H61 (= H59), W87 (≠ F85), C148 (≠ L159)
- binding zinc ion: C38 (= C38), H61 (= H59), E62 (= E60), C92 (= C89), C95 (= C92), C98 (= C95), C106 (= C103), C148 (≠ L159)
Sites not aligning to the query:
P12311 Alcohol dehydrogenase; ADH-T; EC 1.1.1.1 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
33% identity, 67% coverage: 3:254/377 of query aligns to 4:239/337 of P12311
- C38 (= C38) mutation to S: No activity.
- T40 (≠ S40) mutation to A: No activity.; mutation to S: Little decrease in activity.
- H43 (= H43) mutation to A: No activity.; mutation to R: Higher level of activity at pH 9.
P07913 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 from Escherichia coli (strain K12) (see paper)
27% identity, 100% coverage: 1:376/377 of query aligns to 1:339/341 of P07913
- C38 (= C38) mutation to D: Shows only 1% of wild-type catalytic activity. This mutant can be stimulated to the wild-type activity level after incubation with Zn(+).; mutation to S: Loss of catalytic activity. This mutant cannot be stimulated to the wild-type activity level after incubation with Zn(+).
Q96V44 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Hypocrea jecorina (Trichoderma reesei) (see paper)
27% identity, 93% coverage: 27:376/377 of query aligns to 55:374/377 of Q96V44
- DI 224:225 (≠ DY 209:210) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-362.
- A362 (≠ N364) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 224-SR-225.
7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis (see paper)
28% identity, 92% coverage: 20:367/377 of query aligns to 22:347/357 of 7y9pA
B6HI95 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 from Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum) (see paper)
26% identity, 92% coverage: 27:373/377 of query aligns to 43:367/385 of B6HI95
- DI 212:213 (≠ DY 209:210) mutation to SR: Alters cofactor specificity from NAD to NADP; when associated with T-358.
- S358 (≠ N364) mutation to T: Alters cofactor specificity from NAD to NADP; when associated with 212-SR-213.
P06757 Alcohol dehydrogenase 1; Alcohol dehydrogenase A subunit; EC 1.1.1.1 from Rattus norvegicus (Rat) (see paper)
27% identity, 93% coverage: 18:368/377 of query aligns to 21:369/376 of P06757
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
6dkhC The crystal structure of l-idonate 5-dehydrogenase from escherichia coli str. K-12 substr. Mg1655
27% identity, 99% coverage: 2:375/377 of query aligns to 9:344/346 of 6dkhC
Query Sequence
>WP_003463377.1 NCBI__GCF_000359605.1:WP_003463377.1
MKSVTYQGKYEVAVTQVPFPTIEDDEDVIVKITSTAICGSDLHLYQGNFPLPIGYQIGHE
PMGIVEEVGPKVTKVKKGDRVVIPFTIACGQCPYCKTHHESQCDQANPHYDSGGYLGYSE
KFGNYPGGQAEYLRVPFGNYTPFLIPEDCELDDASLLFLSDVLPTALWSVEHAGVKAGDT
VIVLGCGPIGLMVQKFAWQKRANRVIAVDYIPYRLEHARKENRVEVFNFTQYDDMGETLK
EITNGGADVVIDCVGMDGKKSPLEFVEQKTKLQGGTIGPIQIATKAVKKCGVVQMTGVYG
GNYNLFPLGAFFSRNVQLKMGQAHARSYMASIYRQIVNGDIDPTTIITHQLPLEDASHGY
DIFNGKKENCMKVVLQP
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