SitesBLAST
Comparing Synpcc7942_2304 FitnessBrowser__SynE:Synpcc7942_2304 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)
33% identity, 94% coverage: 4:291/305 of query aligns to 8:287/292 of P0A7B3
- R175 (≠ A180) 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
35% identity, 72% coverage: 73:292/305 of query aligns to 66:287/290 of 7mh7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: D71 (= D78), G72 (= G79), R93 (≠ T100), F98 (= F105), N145 (= N152), D146 (≠ E153), T186 (= T193), A187 (= A194), Y188 (= Y195), S191 (= S198), D244 (= D249), K283 (= K288)
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, 72% coverage: 73:291/305 of query aligns to 80:304/307 of P9WHV7
- D85 (= D78) mutation to A: Abolishes catalytic activity.
- N159 (= N152) mutation to A: Abolishes catalytic activity.
- NE 159:160 (= NE 152:153) binding
- E160 (= E153) mutation to A: Abolishes catalytic activity.
- G190 (= G183) mutation to A: Abolishes catalytic activity.
- L192 (≠ I185) mutation to A: Abolishes catalytic activity.
- T195 (= T188) mutation to A: It promotes stronger allosteric interactions.
- P196 (= P189) mutation to A: Abolishes catalytic activity.
- T197 (= T190) binding ; mutation to A: Abolishes catalytic activity.
- G198 (= G191) mutation to A: Abolishes catalytic activity.
- S199 (= S192) mutation to A: Lower catalytic efficiency. A perturbation of the allosteric interactions is observed when NAD is used as substrate.
- T200 (= T193) mutation to A: Abolishes catalytic activity.
- TAYAFS 200:205 (≠ TAYSLS 193:198) binding
- Y202 (= Y195) mutation to A: Abolishes catalytic activity.
- G207 (= G200) mutation to A: Abolishes catalytic activity.
- G208 (= G201) 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)
33% identity, 70% coverage: 76:289/305 of query aligns to 12:226/231 of 1y3iA
- binding nicotinamide-adenine-dinucleotide: D14 (= D78), G15 (= G79), R38 (≠ H102), F41 (= F105), L42 (= L106), N88 (= N152), E89 (= E153), T129 (= T193), A130 (= A194), Y131 (= Y195), S134 (= S198)
3afoA Crystal structure of yeast nadh kinase complexed with nadh
32% identity, 54% coverage: 73:236/305 of query aligns to 115:280/360 of 3afoA
- binding 1,4-dihydronicotinamide adenine dinucleotide: D120 (= D78), G121 (= G79), L124 (= L82), F148 (= F105), N196 (= N152), D197 (≠ E153), T237 (= T193), A238 (= A194), Y239 (= Y195), S242 (= S198)
Sites not aligning to the query:
O13863 Uncharacterized kinase C1B1.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 76% coverage: 62:292/305 of query aligns to 276:512/537 of O13863
Sites not aligning to the query:
- 72 modified: Phosphoserine
1z0zA Crystal structure of a NAD kinase from archaeoglobus fulgidus in complex with NAD (see paper)
29% identity, 68% coverage: 68:275/305 of query aligns to 39:233/249 of 1z0zA
- active site: E96 (≠ S127), C105 (≠ V136)
- binding nicotinamide-adenine-dinucleotide: N115 (= N152), E116 (= E153), M127 (≠ S163), R143 (≠ A180), D145 (= D182), T156 (= T193), Y158 (= Y195), S161 (= S198), F182 (≠ H219), D209 (= D249), G210 (= G250)
1z0sA Crystal structure of an NAD kinase from archaeoglobus fulgidus in complex with atp (see paper)
29% identity, 68% coverage: 68:275/305 of query aligns to 39:233/249 of 1z0sA
- active site: E96 (≠ S127), C105 (≠ V136)
- binding adenosine-5'-triphosphate: R54 (≠ A83), N115 (= N152), E116 (= E153), A125 (≠ L161), K126 (≠ T162), M127 (≠ S163), D145 (= D182), G157 (≠ A194), Y158 (= Y195), S161 (= S198), A180 (≠ C217), F182 (≠ H219), D209 (= D249)
- binding pyrophosphate 2-: G48 (= G77), G50 (= G79), T51 (= T80), R54 (≠ A83), R72 (≠ H102)
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)
29% identity, 68% coverage: 68:275/305 of query aligns to 39:233/249 of 1suwA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G48 (= G77), D49 (= D78), G50 (= G79), N115 (= N152), E116 (= E153), A125 (≠ L161), M127 (≠ S163), R143 (≠ A180), D145 (= D182), T156 (= T193), Y158 (= Y195), S161 (= S198), F182 (≠ H219), D209 (= D249), G210 (= G250)
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)
29% identity, 68% coverage: 68:275/305 of query aligns to 39:233/249 of O30297
Q9P7K3 Uncharacterized kinase C24B10.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 76% coverage: 72:303/305 of query aligns to 178:423/449 of Q9P7K3
- S420 (= S300) modified: Phosphoserine
2i2bA Crystal structure of lmnadk1 from listeria monocytogenes (see paper)
28% identity, 58% coverage: 73:249/305 of query aligns to 40:217/258 of 2i2bA
Sites not aligning to the query:
3v8pA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a new di-adenosine inhibitor formed in situ (see paper)
28% identity, 58% coverage: 73:249/305 of query aligns to 40:218/260 of 3v8pA
- binding 2-[6-azanyl-9-[(2R,3R,4S,5R)-5-[[(azanylidene-$l^{4}-azanylidene)amino]methyl]-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]sulfanyl-N-[[(2R,3S,4R,5R)-5-(6-azanyl-8-bromanyl-purin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl]ethanamide: D45 (= D78), G46 (= G79), L49 (= L82), F74 (= F105), Y75 (≠ L106), N118 (= N152), E119 (= E153), T157 (= T193), A158 (= A194), Y159 (= Y195), S162 (= S198), D218 (= D249)
3v7wA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with 5'-azido-5'-deoxyadenosine (see paper)
28% identity, 58% coverage: 73:249/305 of query aligns to 40:218/260 of 3v7wA
- binding 5'-azido-5'-deoxyadenosine: D45 (= D78), G46 (= G79), L72 (= L103), F74 (= F105), Y75 (≠ L106), N118 (= N152), N118 (= N152), E119 (= E153), T157 (= T193), A158 (= A194), Y159 (= Y195), S162 (= S198)
4dy6A Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with 2'-phosphate bis(adenosine)-5'-diphosphate (see paper)
28% identity, 58% coverage: 73:249/305 of query aligns to 40:217/258 of 4dy6A
- binding [(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl[(2r,3r,4r,5r)-5-(6-amino-9h-purin-9-yl)-3-hydroxy-4-(phosphonooxy)tetrahydrofuran-2-yl]methyl dihydrogen diphosphate: D45 (= D78), G46 (= G79), H71 (= H102), F74 (= F105), N117 (= N152), E118 (= E153), T156 (= T193), A157 (= A194), Y158 (= Y195), S161 (= S198)
6rgeA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with an inhibitor
28% identity, 58% coverage: 73:249/305 of query aligns to 40:217/259 of 6rgeA
- binding [(2~{R},3~{R},4~{R},5~{R})-2-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-5-(hydroxymethyl)-4-oxidanyl-oxolan-3-yl] dihydrogen phosphate: G44 (= G77), D45 (= D78), G46 (= G79), L49 (= L82), H71 (= H102), F74 (= F105), N117 (= N152), E118 (= E153), T156 (= T193), A157 (= A194), Y158 (= Y195), S161 (= S198)
6rgcA Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an inhibitor (see paper)
28% identity, 58% coverage: 73:249/305 of query aligns to 40:217/259 of 6rgcA
- 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-methyl-amino]methyl]oxolane-3,4-diol: D45 (= D78), G46 (= G79), L72 (= L103), F74 (= F105), N117 (= N152), E118 (= E153), T156 (= T193), A157 (= A194), Y158 (= Y195), S161 (= S198)
6rgaA Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an inhibitor (see paper)
28% identity, 58% coverage: 73:249/305 of query aligns to 40:217/259 of 6rgaA
- binding (2~{R},3~{S},4~{R},5~{R})-2-(aminomethyl)-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]oxolane-3,4-diol: D45 (= D78), L49 (= L82), F74 (= F105), N117 (= N152), E118 (= E153), T156 (= T193), A157 (= A194), Y158 (= Y195), S161 (= S198)
5dhuA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a novel inhibitor (see paper)
29% identity, 58% coverage: 73:249/305 of query aligns to 40:221/263 of 5dhuA
Sites not aligning to the query:
5dhtA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a novel inhibitor (see paper)
29% identity, 58% coverage: 73:249/305 of query aligns to 40:221/263 of 5dhtA
Query Sequence
>Synpcc7942_2304 FitnessBrowser__SynE:Synpcc7942_2304
VPDVGIIYNDSKPRACTIAEELQQQLQDRGWGVRLATSQSGLLGYSNPDTVICHTPVESL
VPRGFDASLRWAIVLGGDGTVLAAARQLAPIGVPMLTVNTGHLGFLAEAYLDSLPAAIEQ
LCKGEYSIEERTMMEVKVLRRELIRWEALSLNEMALHREPLTSMCHFEVAIGKHVPVDIA
ADGVIVSTPTGSTAYSLSSGGPVVTPDVPVFQLVPICPHSLASRALVFANREPMTIFPAT
PERLMMVVDGNAGCYVWPEERVLIQRSRYPAQFIRLQPNEFFRVLREKLGWGLPHVAKPS
APDQS
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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