SitesBLAST
Comparing Echvi_0656 FitnessBrowser__Cola:Echvi_0656 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)
7mh7A Crystal structure of NAD kinase from pseudomonas aeruginosa pao1
33% identity, 88% coverage: 32:286/291 of query aligns to 35:287/290 of 7mh7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: D71 (= D73), G72 (= G74), R93 (≠ T95), F98 (= F100), N145 (= N146), D146 (≠ E147), T186 (= T187), A187 (≠ G188), Y188 (= Y189), S191 (= S192), D244 (= D244), K283 (= K282)
P0A7B3 NAD kinase; ATP-dependent NAD kinase; EC 2.7.1.23 from Escherichia coli (strain K12) (see paper)
29% identity, 92% coverage: 19:285/291 of query aligns to 24:287/292 of P0A7B3
- R175 (≠ W174) mutation to E: Does not exhibit NADH kinase activity in addition to NAD kinase activity.; mutation to G: Exhibits NADH kinase activity in addition to NAD kinase activity. Reduces the Vmax of the NAD kinase activity.; mutation to H: Exhibits NADH kinase activity in addition to NAD kinase activity.; mutation to I: Does not exhibit NADH kinase activity in addition to NAD kinase activity.; mutation to K: Does not exhibit NADH kinase activity in addition to NAD kinase activity.; mutation to Q: Exhibits NADH kinase activity in addition to NAD kinase activity.; mutation to T: Exhibits NADH kinase activity in addition to NAD kinase activity.
P9WHV7 NAD kinase; ATP-dependent NAD kinase; Poly(P)-dependent NAD kinase; PPNK; EC 2.7.1.23 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 3 papers)
31% identity, 76% coverage: 63:282/291 of query aligns to 75:296/307 of P9WHV7
- D85 (= D73) mutation to A: Abolishes catalytic activity.
- N159 (= N146) mutation to A: Abolishes catalytic activity.
- NE 159:160 (= NE 146:147) binding
- E160 (= E147) mutation to A: Abolishes catalytic activity.
- G190 (= G177) mutation to A: Abolishes catalytic activity.
- L192 (≠ I179) mutation to A: Abolishes catalytic activity.
- T195 (= T182) mutation to A: It promotes stronger allosteric interactions.
- P196 (= P183) mutation to A: Abolishes catalytic activity.
- T197 (= T184) binding ; mutation to A: Abolishes catalytic activity.
- G198 (= G185) mutation to A: Abolishes catalytic activity.
- S199 (= S186) mutation to A: Lower catalytic efficiency. A perturbation of the allosteric interactions is observed when NAD is used as substrate.
- T200 (= T187) mutation to A: Abolishes catalytic activity.
- TAYAFS 200:205 (≠ TGYSLS 187:192) binding
- Y202 (= Y189) mutation to A: Abolishes catalytic activity.
- G207 (= G194) mutation to A: Abolishes catalytic activity.
- G208 (= G195) mutation to A: Possesses 30% of the activity compared to the wild-type enzyme. While mutant affects the catalytic efficiency, it does not alter the binding affinity for ATP and poly(P). It causes a decrease in the affinity for NAD and alters the allosteric interactions mediated by the dinucleotide, both in the presence of poly(P) and ATP.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1y3iA Crystal structure of mycobacterium tuberculosis NAD kinase-NAD complex (see paper)
31% identity, 73% coverage: 71:282/291 of query aligns to 12:225/231 of 1y3iA
- binding nicotinamide-adenine-dinucleotide: D14 (= D73), G15 (= G74), R38 (= R97), F41 (= F100), L42 (= L101), N88 (= N146), E89 (= E147), T129 (= T187), A130 (≠ G188), Y131 (= Y189), S134 (= S192)
3afoA Crystal structure of yeast nadh kinase complexed with nadh
33% identity, 58% coverage: 65:232/291 of query aligns to 112:282/360 of 3afoA
- binding 1,4-dihydronicotinamide adenine dinucleotide: D120 (= D73), G121 (= G74), L124 (= L77), F148 (= F100), N196 (= N146), D197 (≠ E147), T237 (= T187), A238 (≠ G188), Y239 (= Y189), S242 (= S192)
Sites not aligning to the query:
1z0zA Crystal structure of a NAD kinase from archaeoglobus fulgidus in complex with NAD (see paper)
33% identity, 73% coverage: 59:269/291 of query aligns to 35:233/249 of 1z0zA
- active site: E96 (≠ T122), C105 (≠ L131)
- binding nicotinamide-adenine-dinucleotide: N115 (= N146), E116 (= E147), M127 (= M158), R143 (≠ W174), D145 (= D176), T156 (= T187), Y158 (= Y189), S161 (= S192), F182 (≠ H213), D209 (= D244), G210 (≠ S245)
1z0sA Crystal structure of an NAD kinase from archaeoglobus fulgidus in complex with atp (see paper)
33% identity, 73% coverage: 59:269/291 of query aligns to 35:233/249 of 1z0sA
- active site: E96 (≠ T122), C105 (≠ L131)
- binding adenosine-5'-triphosphate: R54 (≠ D78), N115 (= N146), E116 (= E147), A125 (≠ S156), K126 (≠ S157), M127 (= M158), D145 (= D176), G157 (= G188), Y158 (= Y189), S161 (= S192), A180 (≠ S211), F182 (≠ H213), D209 (= D244)
- binding pyrophosphate 2-: G48 (= G72), G50 (= G74), T51 (= T75), R54 (≠ D78), R72 (= R97)
Sites not aligning to the query:
1suwA Crystal structure of a NAD kinase from archaeoglobus fulgidus in complex with its substrate and product: insights into the catalysis of NAD kinase (see paper)
33% identity, 73% coverage: 59:269/291 of query aligns to 35:233/249 of 1suwA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G48 (= G72), D49 (= D73), G50 (= G74), N115 (= N146), E116 (= E147), A125 (≠ S156), M127 (= M158), R143 (≠ W174), D145 (= D176), T156 (= T187), Y158 (= Y189), S161 (= S192), F182 (≠ H213), D209 (= D244), G210 (≠ S245)
O30297 NAD kinase; ATP-dependent NAD kinase; EC 2.7.1.23 from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) (see paper)
33% identity, 73% coverage: 59:269/291 of query aligns to 35:233/249 of O30297
O13863 Uncharacterized kinase C1B1.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 76% coverage: 65:286/291 of query aligns to 280:512/537 of O13863
Sites not aligning to the query:
- 72 modified: Phosphoserine
Q9P7K3 Uncharacterized kinase C24B10.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 78% coverage: 65:290/291 of query aligns to 176:411/449 of Q9P7K3
Sites not aligning to the query:
- 420 modified: Phosphoserine
7zzdA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:223/262 of 7zzdA
- binding 2-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-[(3-azanylpropanoylamino)methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl]amino]ethanoic acid: D45 (= D73), G46 (= G74), F74 (= F100), Y75 (≠ L101), N120 (= N146), E121 (= E147), T159 (= T187), A160 (≠ G188), Y161 (= Y189), S164 (= S192), H221 (≠ S245)
7zz9A Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:223/262 of 7zz9A
- binding 3-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-(2-azanylethyl)amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methylamino]-3-oxidanylidene-propanoic acid: D45 (= D73), G46 (= G74), L49 (= L77), F74 (= F100), Y75 (≠ L101), N120 (= N146), E121 (= E147), T159 (= T187), A160 (≠ G188), Y161 (= Y189), S164 (= S192)
6z64A Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a di-adenosine derivative (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:223/262 of 6z64A
- binding (2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-(3-azanylpropyl)amino]methyl]oxolane-3,4-diol: D45 (= D73), L49 (= L77), F74 (= F100), Y75 (≠ L101), N120 (= N146), E121 (= E147), T159 (= T187), A160 (≠ G188), Y161 (= Y189), S164 (= S192)
5ejiA Crystal structure of NAD kinase w78f mutant from listeria monocytogenes in complex with NADP/mn++/ppi
29% identity, 63% coverage: 65:247/291 of query aligns to 37:221/260 of 5ejiA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G44 (= G72), D45 (= D73), L72 (≠ M98), G73 (= G99), F74 (= F100), Y75 (≠ L101), N118 (= N146), E119 (= E147), T157 (= T187), A158 (≠ G188), Y159 (= Y189), S162 (= S192)
- binding pyrophosphate 2-: G44 (= G72), D45 (= D73), G46 (= G74), T47 (= T75)
6rbzA Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an adenine derivative (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:223/262 of 6rbzA
5dhuA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a novel inhibitor (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:224/263 of 5dhuA
5dhtA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a novel inhibitor (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:224/263 of 5dhtA
5dhsA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a novel inhibitor (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:224/263 of 5dhsA
- binding 5'-azido-5'-deoxy-8-[(2-{[2-(3-ethynylphenyl)ethyl]amino}-2-oxoethyl)sulfanyl]adenosine: N121 (= N146), E122 (= E147), G130 (≠ S157), P131 (≠ M158), R147 (≠ W174), G148 (≠ A175), D149 (= D176), Y162 (= Y189), S165 (= S192), A184 (≠ S211), H222 (≠ S245)
5dhrA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a novel inhibitor (see paper)
28% identity, 63% coverage: 65:247/291 of query aligns to 37:224/263 of 5dhrA
Query Sequence
>Echvi_0656 FitnessBrowser__Cola:Echvi_0656
MKITIHGISFQKEFVPYIEKLIAVLHGHGTDLFLTETFSKYLKKSGAKATGFTVLGERKE
LAGMDFVISVGGDGTLLDTVSLVGEYEVPIVGINTGRMGFLATIAKEDVEKAVQVLFDGD
FTIQDRILINLEADQKLFNGVPYGLNEFTIHKRDTSSMIIVHTYIDGEYLNSYWADGLIV
ATPTGSTGYSLSCGGPLISPSAKNFVITPVSPHNLNVRPMIVSDESEITFSIEGRSKKFL
ISLDSRSTAVDASVKLKVKREKFVARLVKFHDYSFFDTLRKKLNWGFDMRN
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