SitesBLAST
Comparing SMa0478 FitnessBrowser__Smeli:SMa0478 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)
79% identity, 99% coverage: 3:400/401 of query aligns to 1:398/401 of P33160
- M1 (= M3) modified: Initiator methionine, Removed
- I123 (= I125) binding
- N147 (= N149) binding
- S148 (= S150) binding
- RI 202:203 (= RI 204:205) binding
- D222 (= D224) binding
- C256 (≠ A258) 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 (= PLHPE 259:263) binding
- T283 (= T285) binding
- D309 (= D311) binding
- HISG 333:336 (= HISG 335:338) binding
- S381 (= S383) binding
3wr5A Structural basis on the efficient co2 reduction of acidophilic formate dehydrogenase
78% identity, 99% coverage: 3:399/401 of query aligns to 5:401/401 of 3wr5A
- active site: N151 (= N149), R289 (= R287), D313 (= D311), Q318 (= Q316), H337 (= H335)
- binding nicotinamide-adenine-dinucleotide: N151 (= N149), V155 (= V153), A203 (≠ G201), G205 (= G203), R206 (= R204), I207 (= I205), D226 (= D224), R227 (= R225), V260 (≠ A258), P261 (= P259), T287 (= T285), A288 (= A286), R289 (= R287), D313 (= D311), H337 (= H335), S339 (= S337), G340 (= G338), S385 (= S383)
6t9wB Crystal structure of formate dehydrogenase fdh2 d222a/q223r enzyme from granulicella mallensis mp5actx8 in complex with NADP and azide.
82% identity, 95% coverage: 4:385/401 of query aligns to 1:382/383 of 6t9wB
- binding azide ion: P97 (= P100), F98 (= F101), G121 (= G124), I122 (= I125), H332 (= H335)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I122 (= I125), N146 (= N149), S147 (= S150), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), F220 (≠ T223), R222 (= R225), P256 (= P259), H258 (= H261), T261 (= T264), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338), S380 (= S383)
2nadA High resolution structures of holo and apo formate dehydrogenase (see paper)
79% identity, 98% coverage: 4:394/401 of query aligns to 1:391/391 of 2nadA
- active site: N146 (= N149), R284 (= R287), D308 (= D311), Q313 (= Q316), H332 (= H335)
- binding azide ion: P97 (= P100), F98 (= F101), I122 (= I125), N146 (= N149), R284 (= R287)
- binding nicotinamide-adenine-dinucleotide: I122 (= I125), N146 (= N149), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), D221 (= D224), P256 (= P259), E260 (= E263), T261 (= T264), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338), S380 (= S383)
2gsdA NAD-dependent formate dehydrogenase from bacterium moraxella sp.C2 in complex with NAD and azide (see paper)
76% identity, 99% coverage: 4:400/401 of query aligns to 1:397/399 of 2gsdA
- active site: N146 (= N149), R284 (= R287), D308 (= D311), Q313 (= Q316), H332 (= H335)
- binding azide ion: P97 (= P100), F98 (= F101), I122 (= I125), R284 (= R287), H332 (= H335)
- binding nicotinamide-adenine-dinucleotide: I122 (= I125), N146 (= N149), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), D221 (= D224), R222 (= R225), P256 (= P259), H258 (= H261), T261 (= T264), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338), S380 (= S383)
8bxxAA Formate dehydrogenase
82% identity, 92% coverage: 4:373/401 of query aligns to 1:370/370 of 8bxxAA
- binding azide ion: P97 (= P100), F98 (= F101), I122 (= I125), R284 (= R287), H332 (= H335)
- binding nicotinamide-adenine-dinucleotide: I122 (= I125), N146 (= N149), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), F220 (≠ T223), D221 (= D224), Q222 (≠ R225), P256 (= P259), H258 (= H261), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338)
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)
78% identity, 95% coverage: 4:384/401 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 (= F101), N146 (= N149), V150 (= V153), G200 (= G203), I202 (= I205), D221 (= D224), R222 (= R225), I255 (≠ A258), P256 (= P259), H258 (= H261), T282 (= T285), A283 (= A286), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338)
4xyeA Granulicella m. Formate dehydrogenase (fdh) in complex with NAD(+) (see paper)
73% identity, 96% coverage: 4:387/401 of query aligns to 1:384/384 of 4xyeA
- active site: N146 (= N149), R284 (= R287), D308 (= D311), Q313 (= Q316), H332 (= H335)
- binding nicotinamide-adenine-dinucleotide: F98 (= F101), I122 (= I125), N146 (= N149), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), A221 (≠ D224), R222 (= R225), A255 (= A258), P256 (= P259), Y258 (≠ H261), R284 (= R287), H332 (= H335), G335 (= G338), S380 (= S383)
4xybA Granulicella m. Formate dehydrogenase (fdh) in complex with NADP(+) and nan3 (see paper)
73% identity, 96% coverage: 4:387/401 of query aligns to 1:384/384 of 4xybA
- active site: N146 (= N149), R284 (= R287), D308 (= D311), Q313 (= Q316), H332 (= H335)
- binding azide ion: P97 (= P100), F98 (= F101), I122 (= I125), R284 (= R287), H332 (= H335)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: I122 (= I125), N146 (= N149), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), R222 (= R225), H223 (= H226), P256 (= P259), Y258 (≠ H261), T261 (= T264), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338), S380 (= S383)
7ya4A Formate dehydrogenase from novosphingobium sp. Ap12 with NAD and azide
73% identity, 95% coverage: 4:385/401 of query aligns to 1:382/384 of 7ya4A
- binding azide ion: P97 (= P100), F98 (= F101), I122 (= I125), R284 (= R287), H332 (= H335)
- binding nicotinamide-adenine-dinucleotide: I122 (= I125), N146 (= N149), S147 (= S150), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), Y220 (≠ T223), R222 (= R225), P256 (= P259), H258 (= H261), E260 (= E263), T261 (= T264), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338), S380 (= S383)
7ya3B Formate dehydrogenase from novosphingobium sp. Ap12 with NADP and azide
73% identity, 95% coverage: 4:385/401 of query aligns to 1:382/384 of 7ya3B
- binding azide ion: I122 (= I125), R284 (= R287), H332 (= H335)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: I122 (= I125), N146 (= N149), V150 (= V153), A198 (≠ G201), G200 (= G203), R201 (= R204), I202 (= I205), R222 (= R225), H223 (= H226), P256 (= P259), H258 (= H261), E260 (= E263), T282 (= T285), A283 (= A286), R284 (= R287), D308 (= D311), H332 (= H335), S334 (= S337), G335 (= G338), S380 (= S383)
Q9S7E4 Formate dehydrogenase, chloroplastic/mitochondrial; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Arabidopsis thaliana (Mouse-ear cress)
56% identity, 81% coverage: 52:377/401 of query aligns to 55:380/384 of Q9S7E4
Sites not aligning to the query:
- 1:29 modified: transit peptide, Chloroplast and mitochondrion
3n7uA NAD-dependent formate dehydrogenase from higher-plant arabidopsis thaliana in complex with NAD and azide
56% identity, 81% coverage: 52:377/401 of query aligns to 22:347/351 of 3n7uA
- active site: N119 (= N149), R257 (= R287), D281 (= D311), Q286 (= Q316), H305 (= H335)
- binding azide ion: P70 (= P100), F71 (= F101), I95 (= I125), R257 (= R287), H305 (= H335)
- binding nicotinamide-adenine-dinucleotide: I95 (= I125), N119 (= N149), V123 (= V153), G173 (= G203), R174 (= R204), I175 (= I205), D194 (= D224), R195 (= R225), M228 (≠ A258), P229 (= P259), N255 (≠ T285), A256 (= A286), R257 (= R287), D281 (= D311), H305 (= H335), S307 (= S337), G308 (= G338)
3jtmA Structure of recombinant formate dehydrogenase from arabidopsis thaliana
56% identity, 81% coverage: 52:377/401 of query aligns to 22:347/351 of 3jtmA
7arzA Ternary complex of NAD-dependent formate dehydrogenase from physcomitrium patens
53% identity, 81% coverage: 52:377/401 of query aligns to 31:357/361 of 7arzA
- binding azide ion: T77 (≠ S98), P79 (= P100), F80 (= F101), L99 (≠ A120), V100 (≠ I121), T101 (= T122), G103 (= G124), V104 (≠ I125), R267 (= R287), H315 (= H335)
- binding nicotinamide-adenine-dinucleotide: V104 (≠ I125), N128 (= N149), V132 (= V153), G182 (= G203), R183 (= R204), I184 (= I205), D204 (= D224), R205 (= R225), T238 (≠ A258), P239 (= P259), Q243 (≠ E263), N265 (≠ T285), A266 (= A286), R267 (= R287), D291 (= D311), H315 (= H335), S317 (= S337), G318 (= G338)
Sites not aligning to the query:
6t8zAAA Formate dehydrogenase (see paper)
57% identity, 82% coverage: 49:377/401 of query aligns to 24:360/373 of 6t8zAAA
- binding nicotinamide-adenine-dinucleotide: I99 (= I125), N125 (= N149), V129 (= V153), G177 (= G201), G179 (= G203), R180 (= R204), I181 (= I205), Y200 (≠ T223), D201 (= D224), Y202 (≠ R225), Q203 (≠ H226), C235 (≠ A258), P236 (= P259), H238 (= H261), T262 (= T285), A263 (= A286), R264 (= R287), D288 (= D311), H317 (= H335), S319 (= S337), G320 (= G338)
Sites not aligning to the query:
6t8yBBB Formate dehydrogenase (see paper)
57% identity, 82% coverage: 49:377/401 of query aligns to 25:361/375 of 6t8yBBB
- binding 1,4-dihydronicotinamide adenine dinucleotide: I100 (= I125), N126 (= N149), V130 (= V153), G178 (= G201), G180 (= G203), R181 (= R204), I182 (= I205), Y201 (≠ T223), D202 (= D224), Y203 (≠ R225), Q204 (≠ H226), C236 (≠ A258), P237 (= P259), H239 (= H261), T263 (= T285), A264 (= A286), R265 (= R287), D289 (= D311), H318 (= H335), S320 (= S337), G321 (= G338)
Sites not aligning to the query:
6d4bA Crystal structure of candida boidinii formate dehydrogenase v123a mutant complexed with NAD+ and azide
51% identity, 78% coverage: 52:362/401 of query aligns to 20:338/361 of 6d4bA
- binding azide ion: P68 (= P100), F69 (= F101), V93 (≠ I125), R258 (= R287), H311 (= H335)
- binding nicotinamide-adenine-dinucleotide: V93 (≠ I125), N119 (= N149), G173 (= G203), R174 (= R204), I175 (= I205), Y194 (≠ T223), D195 (= D224), Y196 (≠ R225), A229 (= A258), P230 (= P259), H232 (= H261), T235 (= T264), T256 (= T285), A257 (= A286), R258 (= R287), D282 (= D311), H311 (= H335), S313 (= S337), G314 (= G338)
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)
51% identity, 78% coverage: 52:362/401 of query aligns to 20:338/364 of O13437
- C23 (≠ S55) 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 (= K79) 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 (= F101) 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 (= N149) 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 (= I205) 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 (≠ H226) 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 (= R287) mutation to A: No catalytic activity.
- C262 (= C291) 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 (= Q316) 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 (= P317) 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 (= H335) 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 (≠ R352) 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.
Q08911 Formate dehydrogenase 1; FDH; NAD-dependent formate dehydrogenase; EC 1.17.1.9 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
50% identity, 82% coverage: 48:377/401 of query aligns to 19:368/376 of Q08911
- DY 197:198 (≠ DR 224:225) mutation to AR: Shifts the coenzyme preference of the enzyme from NAD(+) to NADP(+).
Query Sequence
>SMa0478 FitnessBrowser__Smeli:SMa0478
MEMAKVACVLYDDPVDGYPTAYARDGLPTLERYPGGQTLPTPKAIDFEPGALLGSVSGEL
GLRKFLEGQGHTLVVTSDKDGPDSVFERELVDAEIVISQPFWPAYLTAERIVKAARLKLA
ITAGIGSDHVDLQAAIDRGITVAEVTYCNSISVSEHVVMMILSLARNYIPSYQWVVKGGW
NVADCVARSYDIEGMDIGTVGAGRIGTAVLRRLKPFDVKLHYTDRHRLPDEVAKELGVTF
HQTAAEMVPVCDVVTINAPLHPETENLFNEAMIGKMKRGAYLVNTARGKICNRDAVARAL
ESGQLAGYAGDVWFPQPAPKDHPWRSMPHHGMTPHISGSSLSAQARYAAGTREILECWFE
GRPIREEYLIVSGGKLAGAGAHSYSAGDATRGSEEAAHFKT
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