SitesBLAST
Comparing 370304 FitnessBrowser__MR1:370304 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)
P0A7B3 NAD kinase; ATP-dependent NAD kinase; EC 2.7.1.23 from Escherichia coli (strain K12) (see paper)
56% identity, 100% coverage: 1:292/292 of query aligns to 1:292/292 of P0A7B3
- R175 (= R174) 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.
7mh7A Crystal structure of NAD kinase from pseudomonas aeruginosa pao1
52% identity, 98% coverage: 5:291/292 of query aligns to 3:290/290 of 7mh7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: D71 (= D72), G72 (= G73), R93 (= R94), F98 (= F99), N145 (= N146), D146 (≠ E147), T186 (= T187), A187 (= A188), Y188 (= Y189), S191 (= S192), D244 (= D245), K283 (= K284)
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)
33% identity, 78% coverage: 63:290/292 of query aligns to 76:307/307 of P9WHV7
- D85 (= D72) 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 (≠ TAYALS 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
3afoA Crystal structure of yeast nadh kinase complexed with nadh
27% identity, 97% coverage: 5:287/292 of query aligns to 37:342/360 of 3afoA
- binding 1,4-dihydronicotinamide adenine dinucleotide: D120 (= D72), G121 (= G73), L124 (= L76), F148 (= F99), N196 (= N146), D197 (≠ E147), T237 (= T187), A238 (= A188), Y239 (= Y189), S242 (= S192), D300 (= D245), G301 (= G246)
O13863 Uncharacterized kinase C1B1.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
29% identity, 80% coverage: 58:290/292 of query aligns to 270:514/537 of O13863
Sites not aligning to the query:
- 72 modified: Phosphoserine
1y3iA Crystal structure of mycobacterium tuberculosis NAD kinase-NAD complex (see paper)
35% identity, 68% coverage: 70:268/292 of query aligns to 12:209/231 of 1y3iA
- binding nicotinamide-adenine-dinucleotide: D14 (= D72), G15 (= G73), R38 (≠ N96), F41 (= F99), L42 (= L100), N88 (= N146), E89 (= E147), T129 (= T187), A130 (= A188), Y131 (= Y189), S134 (= S192)
Q9P7K3 Uncharacterized kinase C24B10.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 77% coverage: 64:288/292 of query aligns to 176:407/449 of Q9P7K3
Sites not aligning to the query:
- 420 modified: Phosphoserine
1z0zA Crystal structure of a NAD kinase from archaeoglobus fulgidus in complex with NAD (see paper)
32% identity, 64% coverage: 61:247/292 of query aligns to 38:211/249 of 1z0zA
- active site: E96 (= E131), C105 (≠ A140)
- binding nicotinamide-adenine-dinucleotide: N115 (= N146), E116 (= E147), M127 (= M158), R143 (= R174), D145 (= D176), T156 (= T187), Y158 (= Y189), S161 (= S192), F182 (≠ H213), D209 (= D245), G210 (= G246)
1z0sA Crystal structure of an NAD kinase from archaeoglobus fulgidus in complex with atp (see paper)
32% identity, 64% coverage: 61:247/292 of query aligns to 38:211/249 of 1z0sA
- active site: E96 (= E131), C105 (≠ A140)
- binding adenosine-5'-triphosphate: R54 (≠ G77), N115 (= N146), E116 (= E147), A125 (= A156), K126 (≠ H157), M127 (= M158), D145 (= D176), G157 (≠ A188), Y158 (= Y189), S161 (= S192), A180 (≠ F211), F182 (≠ H213), D209 (= D245)
- binding pyrophosphate 2-: G48 (= G71), G50 (= G73), T51 (≠ N74), R54 (≠ G77), R72 (≠ N96)
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)
32% identity, 64% coverage: 61:247/292 of query aligns to 38:211/249 of 1suwA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G48 (= G71), D49 (= D72), G50 (= G73), N115 (= N146), E116 (= E147), A125 (= A156), M127 (= M158), R143 (= R174), D145 (= D176), T156 (= T187), Y158 (= Y189), S161 (= S192), F182 (≠ H213), D209 (= D245), G210 (= G246)
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)
32% identity, 64% coverage: 61:247/292 of query aligns to 38:211/249 of O30297
6rbzA Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an adenine derivative (see paper)
28% identity, 66% coverage: 64:256/292 of query aligns to 37:228/262 of 6rbzA
7zzhA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 7zzhA
- binding (1~{R},22~{R},23~{S},24~{R})-14-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-7-azanyl-23,24-bis(oxidanyl)-25-oxa-2,4,6,9,14,17,20-heptazatetracyclo[20.2.1.0^{2,10}.0^{3,8}]pentacosa-3(8),4,6,9-tetraen-11-yne-16,19-dione: D45 (= D72), F74 (= F99), Y75 (≠ L100), N122 (= N146), E123 (= E147), T161 (= T187), A162 (= A188), Y163 (= Y189), S166 (= S192)
7zzfA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 7zzfA
- binding (1~{R},23~{R},24~{S},25~{R})-14-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-7-azanyl-24,25-bis(oxidanyl)-26-oxa-2,4,6,9,14,17,21-heptazatetracyclo[21.2.1.0^{2,10}.0^{3,8}]hexacosa-3(8),4,6,9-tetraen-11-yne-18,20-dione: D45 (= D72), F74 (= F99), Y75 (≠ L100), N122 (= N146), E123 (= E147), T161 (= T187), A162 (= A188), Y163 (= Y189), S166 (= S192)
7zzbA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 7zzbA
- 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-[(2-azanylethylcarbamoylamino)methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl]amino]ethanoic acid: D45 (= D72), G46 (= G73), F74 (= F99), Y75 (≠ L100), N122 (= N146), E123 (= E147), T161 (= T187), A162 (= A188), Y163 (= Y189), S166 (= S192), H223 (= H249)
7zz7A Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 7zz7A
- 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-[(2-azanylethanoylamino)methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl]amino]ethanoic acid: D45 (= D72), G46 (= G73), F74 (= F99), Y75 (≠ L100), N122 (= N146), E123 (= E147), T161 (= T187), A162 (= A188), Y163 (= Y189), S166 (= S192), H223 (= H249)
6rbvA Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an adenine derivative (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 6rbvA
2i2cA Crystal structure of lmnadk1 (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 2i2cA
- binding (2s,3s,4r,5r,2's,3's,4'r,5'r)-2,2'-[dithiobis(methylene)]bis[5-(6-amino-9h-purin-9-yl)tetrahydrofuran-3,4-diol]: D45 (= D72), F74 (= F99), Y75 (≠ L100), N122 (= N146), E123 (= E147), T161 (= T187), A162 (= A188), Y163 (= Y189), S166 (= S192)
2i2aA Crystal structure of lmnadk1 from listeria monocytogenes (see paper)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of 2i2aA
- binding glycerol: H173 (≠ T199)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G44 (= G71), D45 (= D72), G46 (= G73), F74 (= F99), Y75 (≠ L100), N122 (= N146), E123 (= E147), T161 (= T187), A162 (= A188), Y163 (= Y189), S166 (= S192), H223 (= H249)
Sites not aligning to the query:
Q8Y8D7 NAD kinase 1; ATP-dependent NAD kinase; EC 2.7.1.23 from Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) (see 2 papers)
29% identity, 66% coverage: 64:256/292 of query aligns to 37:230/264 of Q8Y8D7
- D45 (= D72) active site, Proton acceptor; mutation to N: Only minor changes in the structure and a 10-fold decrease in the kinase activity.
- DG 45:46 (= DG 72:73) binding
- G46 (= G73) binding
- NE 122:123 (= NE 146:147) binding
- S158 (≠ T184) binding
- TAYNKS 161:166 (≠ TAYALS 187:192) binding
- H223 (= H249) binding ; mutation to E: Twice less active than the wild-type. Its activity toward DTA is increased 2-fold.
Query Sequence
>370304 FitnessBrowser__MR1:370304
MTTKFHTIGLIGKPHHPGTNQTLKRLHHWLTMQGYEVLVEERVATELGPHIVAVDLLEIG
ERCDLAIVVGGDGNMLGAARVLARFEVGVIGVNRGNLGFLTDLPPDAFEEALAKVLDGEF
DTEHRFLLEAEVYRHGQLKASNTAVNEAVLHPGKIAHMIEFEVYIDNQFMYSQRADGMIV
STPTGSTAYALSAGGAILTPNLQALILVPMFPHTLSCRPIVVDACSTIKMVVSPENGENL
EVSCDGHVHLAVLPGDEIIVRRSSEQLRLIHPKGHNYFHVLRSKLGWGSKLF
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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