SitesBLAST
Comparing WP_013093107.1 NCBI__GCF_000092885.1:WP_013093107.1 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)
P33160 Formate dehydrogenase; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Pseudomonas sp. (strain 101) (Achromobacter parvulus T1) (see 3 papers)
73% identity, 100% coverage: 1:386/386 of query aligns to 1:385/401 of P33160
- M1 (= M1) modified: Initiator methionine, Removed
- I123 (= I124) binding substrate
- N147 (= N148) binding substrate
- S148 (= S149) binding NAD(+)
- RI 202:203 (= RI 203:204) binding NAD(+)
- D222 (= D223) binding NAD(+)
- C256 (≠ S257) mutation C->S,M: High resistance to inactivation by Hg(2+), Increased stability at 25 degree Celsius and decreased thermostability at 45 degree Celsius.
- PLHPE 257:261 (≠ PLYPS 258:262) binding NAD(+)
- T283 (≠ C284) binding NAD(+)
- D309 (= D310) binding NAD(+)
- HISG 333:336 (= HISG 334:337) binding NAD(+)
- S381 (= S382) binding NAD(+)
2nadA High resolution structures of holo and apo formate dehydrogenase (see paper)
73% identity, 100% coverage: 2:386/386 of query aligns to 1:384/391 of 2nadA
- active site: N146 (= N148), R284 (= R286), D308 (= D310), Q313 (= Q315), H332 (= H334)
- binding azide ion: P97 (= P99), F98 (= F100), I122 (= I124), N146 (= N148), R284 (= R286)
- binding nicotinamide-adenine-dinucleotide: I122 (= I124), N146 (= N148), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), D221 (= D223), P256 (= P258), E260 (≠ S262), T261 (= T263), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337), S380 (= S382)
6jujA Crystal structure of formate dehydrogenase mutant v198i/c256i/p260s/e261p/s381n/s383f from pseudomonas sp. 101in complex with non-natural cofactor nicotinamide cytosine dinucleotide (see paper)
73% identity, 99% coverage: 2:383/386 of query aligns to 1:381/381 of 6jujA
- binding [[(2S,3S,4R,5S)-5-(3-aminocarbonylpyridin-1-ium-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2S,3S,4R,5S)-5-(4-azanyl-2-oxidanylidene-pyrimidin-1-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate: F98 (= F100), N146 (= N148), V150 (= V152), G200 (= G202), I202 (= I204), D221 (= D223), R222 (≠ P224), I255 (≠ S257), P256 (= P258), H258 (≠ Y260), T282 (≠ C284), A283 (= A285), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337)
6t9wB Crystal structure of formate dehydrogenase fdh2 d222a/q223r enzyme from granulicella mallensis mp5actx8 in complex with NADP and azide.
71% identity, 99% coverage: 2:385/386 of query aligns to 1:383/383 of 6t9wB
- binding azide ion: P97 (= P99), F98 (= F100), G121 (= G123), I122 (= I124), H332 (= H334)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I122 (= I124), N146 (= N148), S147 (= S149), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), F220 (≠ Y222), R222 (≠ P224), P256 (= P258), H258 (≠ Y260), T261 (= T263), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337), S380 (= S382)
2gsdA NAD-dependent formate dehydrogenase from bacterium moraxella sp.C2 in complex with NAD and azide (see paper)
71% identity, 100% coverage: 2:386/386 of query aligns to 1:384/399 of 2gsdA
- active site: N146 (= N148), R284 (= R286), D308 (= D310), Q313 (= Q315), H332 (= H334)
- binding azide ion: P97 (= P99), F98 (= F100), I122 (= I124), R284 (= R286), H332 (= H334)
- binding nicotinamide-adenine-dinucleotide: I122 (= I124), N146 (= N148), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), D221 (= D223), R222 (≠ P224), P256 (= P258), H258 (≠ Y260), T261 (= T263), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337), S380 (= S382)
3wr5A Structural basis on the efficient co2 reduction of acidophilic formate dehydrogenase
70% identity, 100% coverage: 1:386/386 of query aligns to 5:389/401 of 3wr5A
- active site: N151 (= N148), R289 (= R286), D313 (= D310), Q318 (= Q315), H337 (= H334)
- binding nicotinamide-adenine-dinucleotide: N151 (= N148), V155 (= V152), A203 (≠ G200), G205 (= G202), R206 (= R203), I207 (= I204), D226 (= D223), R227 (≠ P224), V260 (≠ S257), P261 (= P258), T287 (≠ C284), A288 (= A285), R289 (= R286), D313 (= D310), H337 (= H334), S339 (= S336), G340 (= G337), S385 (= S382)
8bxxAA Formate dehydrogenase
71% identity, 96% coverage: 2:372/386 of query aligns to 1:370/370 of 8bxxAA
- binding azide ion: P97 (= P99), F98 (= F100), I122 (= I124), R284 (= R286), H332 (= H334)
- binding nicotinamide-adenine-dinucleotide: I122 (= I124), N146 (= N148), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), F220 (≠ Y222), D221 (= D223), Q222 (≠ P224), P256 (= P258), H258 (≠ Y260), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337)
8oq2A Binding of NADP to a formate dehydrogenase from starkeya novella.
71% identity, 98% coverage: 2:380/386 of query aligns to 2:379/381 of 8oq2A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I123 (= I124), N147 (= N148), V151 (= V152), G201 (= G202), R202 (= R203), I203 (= I204), Q222 (≠ D223), R223 (≠ P224), H224 (= H225), V256 (≠ S257), P257 (= P258), H259 (≠ Y260), T262 (= T263), T283 (≠ C284), A284 (= A285), R285 (= R286), D309 (= D310), H333 (= H334), S335 (= S336), G336 (= G337)
Sites not aligning to the query:
7ya4A Formate dehydrogenase from novosphingobium sp. Ap12 with NAD and azide
68% identity, 99% coverage: 2:385/386 of query aligns to 1:383/384 of 7ya4A
- binding azide ion: P97 (= P99), F98 (= F100), I122 (= I124), R284 (= R286), H332 (= H334)
- binding nicotinamide-adenine-dinucleotide: I122 (= I124), N146 (= N148), S147 (= S149), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), Y220 (= Y222), R222 (≠ P224), P256 (= P258), H258 (≠ Y260), E260 (≠ S262), T261 (= T263), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337), S380 (= S382)
7ya3B Formate dehydrogenase from novosphingobium sp. Ap12 with NADP and azide
68% identity, 99% coverage: 2:385/386 of query aligns to 1:383/384 of 7ya3B
- binding azide ion: I122 (= I124), R284 (= R286), H332 (= H334)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I122 (= I124), N146 (= N148), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), R222 (≠ P224), H223 (= H225), P256 (= P258), H258 (≠ Y260), E260 (≠ S262), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337), S380 (= S382)
4xyeA Granulicella m. Formate dehydrogenase (fdh) in complex with NAD(+) (see paper)
69% identity, 100% coverage: 2:386/386 of query aligns to 1:384/384 of 4xyeA
- active site: N146 (= N148), R284 (= R286), D308 (= D310), Q313 (= Q315), H332 (= H334)
- binding nicotinamide-adenine-dinucleotide: F98 (= F100), I122 (= I124), N146 (= N148), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), A221 (≠ D223), R222 (≠ P224), A255 (≠ S257), P256 (= P258), Y258 (= Y260), R284 (= R286), H332 (= H334), G335 (= G337), S380 (= S382)
4xybA Granulicella m. Formate dehydrogenase (fdh) in complex with NADP(+) and nan3 (see paper)
69% identity, 100% coverage: 2:386/386 of query aligns to 1:384/384 of 4xybA
- active site: N146 (= N148), R284 (= R286), D308 (= D310), Q313 (= Q315), H332 (= H334)
- binding azide ion: P97 (= P99), F98 (= F100), I122 (= I124), R284 (= R286), H332 (= H334)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I122 (= I124), N146 (= N148), V150 (= V152), A198 (≠ G200), G200 (= G202), R201 (= R203), I202 (= I204), R222 (≠ P224), H223 (= H225), P256 (= P258), Y258 (= Y260), T261 (= T263), T282 (≠ C284), A283 (= A285), R284 (= R286), D308 (= D310), H332 (= H334), S334 (= S336), G335 (= G337), S380 (= S382)
7arzA Ternary complex of NAD-dependent formate dehydrogenase from physcomitrium patens
50% identity, 85% coverage: 50:376/386 of query aligns to 30:357/361 of 7arzA
- binding azide ion: T77 (≠ S97), P79 (= P99), F80 (= F100), L99 (≠ A119), V100 (≠ L120), T101 (= T121), G103 (= G123), V104 (≠ I124), R267 (= R286), H315 (= H334)
- binding nicotinamide-adenine-dinucleotide: V104 (≠ I124), N128 (= N148), V132 (= V152), G182 (= G202), R183 (= R203), I184 (= I204), D204 (= D223), R205 (≠ P224), T238 (≠ S257), P239 (= P258), Q243 (≠ S262), N265 (≠ C284), A266 (= A285), R267 (= R286), D291 (= D310), H315 (= H334), S317 (= S336), G318 (= G337)
Sites not aligning to the query:
6t8zAAA Formate dehydrogenase (see paper)
54% identity, 85% coverage: 48:376/386 of query aligns to 24:360/373 of 6t8zAAA
- binding nicotinamide-adenine-dinucleotide: I99 (= I124), N125 (= N148), V129 (= V152), G177 (= G200), G179 (= G202), R180 (= R203), I181 (= I204), Y200 (= Y222), D201 (= D223), Y202 (≠ P224), Q203 (≠ H225), C235 (≠ S257), P236 (= P258), H238 (≠ Y260), T262 (≠ C284), A263 (= A285), R264 (= R286), D288 (= D310), H317 (= H334), S319 (= S336), G320 (= G337)
Sites not aligning to the query:
6t8yBBB Formate dehydrogenase (see paper)
54% identity, 85% coverage: 48:376/386 of query aligns to 25:361/375 of 6t8yBBB
- binding 1,4-dihydronicotinamide adenine dinucleotide: I100 (= I124), N126 (= N148), V130 (= V152), G178 (= G200), G180 (= G202), R181 (= R203), I182 (= I204), Y201 (= Y222), D202 (= D223), Y203 (≠ P224), Q204 (≠ H225), C236 (≠ S257), P237 (= P258), H239 (≠ Y260), T263 (≠ C284), A264 (= A285), R265 (= R286), D289 (= D310), H318 (= H334), S320 (= S336), G321 (= G337)
Sites not aligning to the query:
3n7uA NAD-dependent formate dehydrogenase from higher-plant arabidopsis thaliana in complex with NAD and azide
52% identity, 84% coverage: 51:376/386 of query aligns to 22:347/351 of 3n7uA
- active site: N119 (= N148), R257 (= R286), D281 (= D310), Q286 (= Q315), H305 (= H334)
- binding azide ion: P70 (= P99), F71 (= F100), I95 (= I124), R257 (= R286), H305 (= H334)
- binding nicotinamide-adenine-dinucleotide: I95 (= I124), N119 (= N148), V123 (= V152), G173 (= G202), R174 (= R203), I175 (= I204), D194 (= D223), R195 (≠ P224), M228 (≠ S257), P229 (= P258), N255 (≠ C284), A256 (= A285), R257 (= R286), D281 (= D310), H305 (= H334), S307 (= S336), G308 (= G337)
3jtmA Structure of recombinant formate dehydrogenase from arabidopsis thaliana
52% identity, 84% coverage: 51:376/386 of query aligns to 22:347/351 of 3jtmA
Q9S7E4 Formate dehydrogenase, chloroplastic/mitochondrial; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Arabidopsis thaliana (Mouse-ear cress)
52% identity, 84% coverage: 51:376/386 of query aligns to 55:380/384 of Q9S7E4
Sites not aligning to the query:
- 1:29 modified: transit peptide, Chloroplast and mitochondrion
6d4bA Crystal structure of candida boidinii formate dehydrogenase v123a mutant complexed with NAD+ and azide
50% identity, 81% coverage: 50:361/386 of query aligns to 19:338/361 of 6d4bA
- binding azide ion: P68 (= P99), F69 (= F100), V93 (≠ I124), R258 (= R286), H311 (= H334)
- binding nicotinamide-adenine-dinucleotide: V93 (≠ I124), N119 (= N148), G173 (= G202), R174 (= R203), I175 (= I204), Y194 (= Y222), D195 (= D223), Y196 (≠ P224), A229 (≠ S257), P230 (= P258), H232 (≠ Y260), T235 (= T263), T256 (≠ C284), A257 (= A285), R258 (= R286), D282 (= D310), H311 (= H334), S313 (= S336), G314 (= G337)
Sites not aligning to the query:
O13437 Formate dehydrogenase; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Candida boidinii (Yeast) (see 4 papers)
50% identity, 81% coverage: 50:361/386 of query aligns to 19:338/364 of O13437
- C23 (≠ S54) mutation to S: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, significantly more stable in the presence of CuCl(2); when associated with A-262. Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type, significantly more stable in the presence of CuCl(2); when associated with V-262. No significant change in affinity for formate or NAD, 5 degrees Celsius decrease in thermal stability compared to the wild-type, significantly higher stability compared to wild-type under biotransformation conditions, and significantly more stable in the presence of CuCl(2).
- K47 (= K78) mutation to E: Slight increase in substrate affinity for formate and also affinity for NAD increases by half after 2 weeks. Also after 4 months affinity for formate increases by more than half and affinity for NAD increases by more than half. Retains 84% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius.
- F69 (= F100) mutation to A: 2-fold decrease in substrate affinity for formate, but no significant change in affinity for NAD. A significant reduction in catalytic activity compared to the wild-type.
- N119 (= N148) mutation to A: 94-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type; when associated with A-311.; mutation to H: 80-fold decrease in substrate affinity for formate and a 1250-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type.
- I175 (= I204) mutation to A: 2-fold decrease in substrate affinity for formate and a 12-fold decrease in substrate affinity for NAD. A significant reduction in catalytic activity compared to the wild-type.
- Q197 (≠ H225) mutation to L: 4-fold decrease in substrate affinity for formate but no significant change in affinity for NAD compared to the wild-type.
- R258 (= R286) mutation to A: No catalytic activity.
- C262 (= C290) mutation to A: Slight increase in substrate affinity for formate but no change in affinity for NAD, 9 degrees Celsius decrease in thermal stability compared to the wild-type, greater stability at a higher pH compared to the wild-type; when associated with S-23.; mutation to V: Large increase in substrate affinity for formate but no significant change in affinity for NAD, 13 degrees Celsius decrease in thermal stability compared to the wild-type; when associated with S-23. Great increase in substrate affinity for formate and NAD and 8 degrees Celsius decrease in thermal stability compared to the wild-type.
- Q287 (= Q315) mutation to A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-311.; mutation to E: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with T-288. No significant decrease in substrate affinity for formate but a 4-fold decrease in substrate affinity for NAD and a significant reduction in catalytic activity compared to the wild-type, a more acidic pH is seen than in the wild-type, preventing formate binding by a single ionization of a group compared to that of the wild-type.
- P288 (= P316) mutation to T: 380-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with E-287.
- H311 (= H334) mutation to A: 2-fold decrease in substrate affinity for formate and 3-fold decrease in substrate affinity for NAD compared to the wild-type; when associated with A-287. 93-fold decrease in substrate affinity for formate and 2700-fold decrease in substrate affinity for NAD, and a significant reduction in catalytic activity compared to the wild-type; when associated with A-119.; mutation to Q: 10-fold decrease in substrate affinity for formate and significant reduction in the catalytic activity compared to the wild-type.
- K328 (≠ R351) mutation to V: A 75% increase in substrate affinity for formate after 2 weeks and a 50% increase in affinity for NAD. However, after 4 months the affinity for formate increases 7-fold and affinity for NAD increases by 2 thirds. Retains 70% of residual activity after incubation for 20 minutes at a thermal inactivation temperature of 55 degrees Celsius in samples stored for 2 weeks compared to wild-type which loses 50% of its activity at 55 degrees Celsius.
Sites not aligning to the query:
- 360 K→A: Exhibits no change in substrate affinity for formate, but shows a 4-fold decrease in substrate affinity for NAD implying that L-360 side chain forms strong interactions with the cofactor. A higher reaction rate is observed at an acidic and basic pH values.
Query Sequence
>WP_013093107.1 NCBI__GCF_000092885.1:WP_013093107.1
MAKILCALFPDPVTGYPPSYARTDVPSIASYPGGQRPPSPKGPLGFKPGELVGSVSGELG
LRHYLESQGHELIVTSDKDGPDSIFERHLCDADIVISQPFWPAYLTRERIAKAKKLKLAL
TAGIGSDHVDLQAAAERDITVAEVTFSNSISVAEHVVMTVLALVRNYLPSHQYAVNGGWN
IADCVARSYDLEGMHFGTIGAGRIGLAVLRRLKPFDVHLHYYDPHRLSPELERELNVTFH
SSAESLVRVCDVINLQSPLYPSTEHMFNDAMLAQIKPGAYLINCARGKLCDADAVARALQ
SGRLAGYGGDVWFPQPAPAEHPWRSMPNEGMTPHISGASLSAQARYAAGTREILECFLEG
RAIRAEYLIVNGGKLAGTGAASYKLG
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