SitesBLAST
Comparing RR42_RS05915 FitnessBrowser__Cup4G11:RR42_RS05915 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)
41% identity, 92% coverage: 14:295/305 of query aligns to 5:287/292 of P0A7B3
- R175 (= R184) 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
39% identity, 93% coverage: 13:295/305 of query aligns to 2:286/290 of 7mh7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: D71 (= D82), G72 (= G83), R93 (≠ H104), F98 (= F109), N145 (= N156), D146 (= D157), T186 (= T197), A187 (= A198), Y188 (= Y199), S191 (= S202), D244 (= D253), K283 (= K292)
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)
36% identity, 67% coverage: 73:276/305 of query aligns to 76:280/307 of P9WHV7
- D85 (= D82) mutation to A: Abolishes catalytic activity.
- N159 (= N156) mutation to A: Abolishes catalytic activity.
- NE 159:160 (≠ ND 156:157) binding
- E160 (≠ D157) mutation to A: Abolishes catalytic activity.
- G190 (= G187) mutation to A: Abolishes catalytic activity.
- L192 (≠ I189) mutation to A: Abolishes catalytic activity.
- T195 (= T192) mutation to A: It promotes stronger allosteric interactions.
- P196 (= P193) mutation to A: Abolishes catalytic activity.
- T197 (= T194) binding ; mutation to A: Abolishes catalytic activity.
- G198 (= G195) mutation to A: Abolishes catalytic activity.
- S199 (= S196) mutation to A: Lower catalytic efficiency. A perturbation of the allosteric interactions is observed when NAD is used as substrate.
- T200 (= T197) mutation to A: Abolishes catalytic activity.
- TAYAFS 200:205 (≠ TAYALS 197:202) binding
- Y202 (= Y199) mutation to A: Abolishes catalytic activity.
- G207 (= G204) mutation to A: Abolishes catalytic activity.
- G208 (= G205) 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)
36% identity, 65% coverage: 80:276/305 of query aligns to 12:209/231 of 1y3iA
- binding nicotinamide-adenine-dinucleotide: D14 (= D82), G15 (= G83), R38 (= R106), F41 (= F109), L42 (≠ M110), N88 (= N156), E89 (≠ D157), T129 (= T197), A130 (= A198), Y131 (= Y199), S134 (= S202)
3afoA Crystal structure of yeast nadh kinase complexed with nadh
32% identity, 58% coverage: 67:244/305 of query aligns to 105:284/360 of 3afoA
- binding 1,4-dihydronicotinamide adenine dinucleotide: D120 (= D82), G121 (= G83), L124 (= L86), F148 (= F109), N196 (= N156), D197 (= D157), T237 (= T197), A238 (= A198), Y239 (= Y199), S242 (= S202)
Sites not aligning to the query:
1z0zA Crystal structure of a NAD kinase from archaeoglobus fulgidus in complex with NAD (see paper)
34% identity, 62% coverage: 66:253/305 of query aligns to 33:217/249 of 1z0zA
- active site: E96 (= E131), C105 (≠ S140)
- binding nicotinamide-adenine-dinucleotide: N115 (= N156), E116 (≠ D157), M127 (= M168), R143 (= R184), D145 (= D186), T156 (= T197), Y158 (= Y199), S161 (= S202), F182 (≠ H223), D209 (≠ T244), G210 (≠ A245)
1z0sA Crystal structure of an NAD kinase from archaeoglobus fulgidus in complex with atp (see paper)
34% identity, 62% coverage: 66:253/305 of query aligns to 33:217/249 of 1z0sA
- active site: E96 (= E131), C105 (≠ S140)
- binding adenosine-5'-triphosphate: R54 (≠ G87), N115 (= N156), E116 (≠ D157), A125 (≠ S166), K126 (≠ G167), M127 (= M168), D145 (= D186), G157 (≠ A198), Y158 (= Y199), S161 (= S202), A180 (= A221), F182 (≠ H223), D209 (≠ T244)
- binding pyrophosphate 2-: G48 (= G81), G50 (= G83), T51 (= T84), R54 (≠ G87), R72 (= R106)
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)
34% identity, 62% coverage: 66:253/305 of query aligns to 33:217/249 of 1suwA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G48 (= G81), D49 (= D82), G50 (= G83), N115 (= N156), E116 (≠ D157), A125 (≠ S166), M127 (= M168), R143 (= R184), D145 (= D186), T156 (= T197), Y158 (= Y199), S161 (= S202), F182 (≠ H223), D209 (≠ T244), G210 (≠ A245)
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)
34% identity, 62% coverage: 66:253/305 of query aligns to 33:217/249 of O30297
O13863 Uncharacterized kinase C1B1.02c; EC 2.7.1.- from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 73% coverage: 74:297/305 of query aligns to 280:513/537 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)
25% identity, 73% coverage: 74:296/305 of query aligns to 176:407/449 of Q9P7K3
Sites not aligning to the query:
- 420 modified: Phosphoserine
6z65A Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a di-adenosine derivative (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:223/261 of 6z65A
- binding ~{N}-[[(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]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-4-azanyl-butanamide: D45 (= D82), L49 (= L86), F74 (= F109), Y75 (≠ M110), N119 (= N156), E120 (≠ D157), T158 (= T197), A159 (= A198), Y160 (= Y199), S163 (= S202)
3v8nA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with 8-bromo-5'-amino-5'-deoxyadenosine, reacted with a citrate molecule in n site (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:219/257 of 3v8nA
3v8pA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a new di-adenosine inhibitor formed in situ (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:222/260 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 (= D82), G46 (= G83), L49 (= L86), F74 (= F109), Y75 (≠ M110), N118 (= N156), E119 (≠ D157), T157 (= T197), A158 (= A198), Y159 (= Y199), S162 (= S202), D218 (= D253)
3v7wA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with 5'-azido-5'-deoxyadenosine (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:222/260 of 3v7wA
- binding 5'-azido-5'-deoxyadenosine: D45 (= D82), G46 (= G83), L72 (= L107), F74 (= F109), Y75 (≠ M110), N118 (= N156), N118 (= N156), E119 (≠ D157), T157 (= T197), A158 (= A198), Y159 (= Y199), S162 (= S202)
5ejiA Crystal structure of NAD kinase w78f mutant from listeria monocytogenes in complex with NADP/mn++/ppi
30% identity, 60% coverage: 74:257/305 of query aligns to 37:222/260 of 5ejiA
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G44 (= G81), D45 (= D82), L72 (= L107), G73 (= G108), F74 (= F109), Y75 (≠ M110), N118 (= N156), E119 (≠ D157), T157 (= T197), A158 (= A198), Y159 (= Y199), S162 (= S202)
- binding pyrophosphate 2-: G44 (= G81), D45 (= D82), G46 (= G83), T47 (= T84)
6rc0A Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an adenine derivative (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:223/261 of 6rc0A
6rc1A Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an adenine derivative (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:222/259 of 6rc1A
6rbpA Crystal structure of NAD kinase 1 from listeria monocytogenes in complexe with an adenine derivative (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:222/260 of 6rbpA
8a9vA Crystal structure of NAD kinase 1 from listeria monocytogenes in complex with a linear di-adenosine derivative (see paper)
30% identity, 60% coverage: 74:257/305 of query aligns to 37:223/261 of 8a9vA
- binding ~{N}-[[(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]methoxy]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-2-azanyl-ethanesulfonamide: D45 (= D82), L49 (= L86), L72 (= L107), F74 (= F109), Y75 (≠ M110), N119 (= N156), E120 (≠ D157), T158 (= T197), A159 (= A198), Y160 (= Y199), S163 (= S202), H220 (≠ M254)
Query Sequence
>RR42_RS05915 FitnessBrowser__Cup4G11:RR42_RS05915
MSSLPKPGAARAPFRTVALIGRYATAGIEGPLEELAACILRNGQDVVFERDTALATGLTD
YPALAPDEIGKHADVAVVLGGDGTLLGLARQLAGYPVPLIGVNHGRLGFMTDIPLQDVHS
VLPDMLAGRYESETRMLLESKVVRDDGVIFSALAFNDVVVNRSGISGMVELAVSVDGHFM
YNQRSDGLIVSTPTGSTAYALSAGGPILHPTLSGLVLVPIAPHALSNRPIVLPHDAEVSI
EVATARDASVNFDMQSLTSLLPGDRIVVRRSAKTVNLLHPIGYNYYATLRKKLHWHEYPS
EDNRL
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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