SitesBLAST
Comparing WP_012851426.1 NCBI__GCF_000024385.1:WP_012851426.1 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)
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
37% identity, 94% coverage: 9:306/317 of query aligns to 3:308/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G15), T11 (= T17), K12 (= K18), G130 (≠ S142), T131 (= T143), G180 (= G192), G214 (= G213), S218 (≠ A217), G260 (= G259), V261 (≠ L260), E264 (≠ C263)
- binding beta-D-glucopyranose: G65 (= G76), P78 (≠ N89), N103 (= N115), D104 (= D116), L133 (≠ V145), G134 (= G146), E153 (≠ H165), H156 (= H168), E175 (= E187)
- binding zinc ion: H156 (= H168), C166 (= C178), C168 (= C180), C173 (= C185)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
37% identity, 94% coverage: 9:306/317 of query aligns to 3:308/312 of 3vgkB
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
35% identity, 93% coverage: 10:304/317 of query aligns to 4:283/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
35% identity, 93% coverage: 10:304/317 of query aligns to 4:283/293 of 6jdhA
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
34% identity, 97% coverage: 10:317/317 of query aligns to 4:287/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (= K18), S129 (= S142), T130 (= T143), P195 (≠ G213), K196 (≠ V214), S241 (vs. gap)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ V70), G63 (= G71), A72 (≠ E84), L73 (≠ V85), N74 (≠ S86), N77 (= N89), N102 (= N115), D103 (= D116), S129 (= S142), T130 (= T143), H152 (= H165), H155 (= H168), E174 (= E187)
- binding zinc ion: H155 (= H168), C165 (= C178), C167 (= C180), C172 (= C185)
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
32% identity, 97% coverage: 10:317/317 of query aligns to 4:267/269 of 6jdcA
2qm1B Crystal structure of glucokinase from enterococcus faecalis
30% identity, 96% coverage: 6:308/317 of query aligns to 5:320/325 of 2qm1B
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
34% identity, 62% coverage: 109:306/317 of query aligns to 177:380/396 of 1z05A
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
33% identity, 80% coverage: 10:262/317 of query aligns to 6:264/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G15), T13 (= T17), N14 (≠ K18), R16 (≠ A20), T140 (= T143), G189 (= G192), L216 (≠ V214), V261 (≠ G259)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G16), G71 (= G75), G72 (= G76), R73 (≠ P77), S84 (= S86), T85 (≠ P87), L87 (≠ N89), N112 (= N115), D113 (= D116), G139 (≠ S142), T140 (= T143), G141 (= G144), I142 (≠ V145), E162 (≠ H165), H165 (= H168), E184 (= E187)
- binding calcium ion: N112 (= N115), N115 (≠ I118), G144 (= G147), A161 (≠ G164)
- binding zinc ion: H165 (= H168), C175 (= C178), C177 (= C180), C182 (= C185)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
33% identity, 80% coverage: 10:262/317 of query aligns to 6:264/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G15), G12 (= G16), T13 (= T17), N14 (≠ K18), R16 (≠ A20), T140 (= T143), G189 (= G192), L216 (≠ V214), V261 (≠ G259)
- binding calcium ion: N112 (= N115), N115 (≠ I118), G144 (= G147), A161 (≠ G164)
- binding zinc ion: H165 (= H168), C175 (= C178), C177 (= C180), C182 (= C185)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
30% identity, 94% coverage: 12:308/317 of query aligns to 9:306/306 of 7p7wBBB
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
30% identity, 94% coverage: 12:308/317 of query aligns to 6:303/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (≠ G75), G67 (= G76), S79 (≠ L88), N105 (= N115), D106 (= D116), G132 (≠ S142), T133 (= T143), G134 (= G144), V135 (= V145), G136 (= G146), E155 (≠ H165), H158 (= H168), D188 (≠ E187)
- binding zinc ion: H158 (= H168), C179 (= C178), C181 (= C180), C186 (= C185), E212 (= E215), H216 (≠ D219)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
30% identity, 94% coverage: 12:308/317 of query aligns to 7:304/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G16), T12 (= T17), K13 (= K18), G133 (≠ S142), T134 (= T143), G194 (= G192), E198 (≠ V196), A211 (≠ G213), G256 (= G258), G257 (= G259), N260 (≠ Q262)
- binding zinc ion: H159 (= H168), C180 (= C178), C182 (= C180), C187 (= C185), E213 (= E215), H217 (≠ D219)
O35826 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Rattus norvegicus (Rat) (see paper)
33% identity, 79% coverage: 10:261/317 of query aligns to 410:672/722 of O35826
- D413 (= D13) mutation D->K,N: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
- R420 (≠ A20) mutation to M: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization.
Sites not aligning to the query:
- 1 UDP-N-acetylglucosamine 2-epimerase
- 49 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Does not interfere with enzyme oligomerization.
- 110 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
- 132 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process.
- 155 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
- 157 H→A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process.
- 406:722 N-acetylmannosamine kinase
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
27% identity, 97% coverage: 4:310/317 of query aligns to 5:311/311 of 4db3A
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
25% identity, 95% coverage: 9:308/317 of query aligns to 3:302/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ D13), E10 (≠ G16), G70 (= G76), N110 (≠ D116), N110 (≠ D116), S134 (≠ V140), V135 (= V141), G138 (= G144), L139 (≠ V145), G140 (= G146), E159 (≠ H165), H162 (= H168), E181 (= E187), E253 (≠ G259), W293 (≠ G299)
- binding zinc ion: H162 (= H168), C172 (= C178), C174 (= C180), C179 (= C185)
Q9Y223 Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase; UDP-GlcNAc-2-epimerase/ManAc kinase; EC 3.2.1.183; EC 2.7.1.60 from Homo sapiens (Human) (see 18 papers)
33% identity, 79% coverage: 10:261/317 of query aligns to 410:672/722 of Q9Y223
- D413 (= D13) binding Mg(2+)
- G416 (= G16) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (= T17) binding ADP
- N418 (≠ K18) binding ADP
- R420 (≠ A20) binding ADP
- I472 (≠ V72) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 50% of the wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity
- G476 (= G76) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ P77) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ P87) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N115) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D116) active site; binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
- N519 (≠ I118) to S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910; mutation to S: Decreased N-acylmannosamine kinase activity.
- A524 (≠ G123) to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs764698870
- F528 (≠ R127) to C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986; mutation to C: Decreased N-acylmannosamine kinase activity.
- G545 (= G144) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (≠ H165) binding an N-acyl-D-mannosamine
- H569 (= H168) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (= V171) to L: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70-80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
- G576 (= G175) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C178) binding Zn(2+)
- C581 (= C180) binding Zn(2+)
- C586 (= C185) binding Zn(2+)
- I587 (≠ L186) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603; mutation to T: Decreased N-acylmannosamine kinase activity.
- E588 (= E187) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (≠ D219) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A220) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs121908626; to V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 70% of wild-type activity; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs62541771; mutation A->V,T: Decreased N-acylmannosamine kinase activity.
Sites not aligning to the query:
- 13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; dbSNP:rs1209266607
- 19 binding UDP
- 23 binding UDP
- 113 binding UDP
- 132 H → Q: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 10% of wild-type activity; impaired homohexamers formation
- 176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs139425890
- 177 R → C: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to less than 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs539332585
- 200 I → F: in NM; uncertain significance; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 90% of wild-type activity; decreased N-acylmannosamine kinase activity; retains 75% of wild-type activity; dbSNP:rs369328625
- 206 G → S: in NM; moderate phenotype with unusual involvement of quadriceps; dbSNP:rs766266918
- 220 binding UDP
- 253 binding UDP
- 259 binding CMP-N-acetyl-beta-neuraminate
- 263 R → L: in SIALURIA; strong reduction of feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908623
- 266 R → Q: in SIALURIA; abolishes feedback inhibition by CMP-Neu5Ac; dbSNP:rs121908622; R → W: in sialuria; dbSNP:rs121908621
- 271 binding CMP-N-acetyl-beta-neuraminate
- 280 binding CMP-N-acetyl-beta-neuraminate
- 281 binding CMP-N-acetyl-beta-neuraminate
- 282 binding UDP
- 301 binding UDP
- 302 binding UDP
- 303 C → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; retains 80% of wild-type activity; decreased N-acylmannosamine kinase activity; corresponding to 60% of wild-type activity; requires 2 nucleotide substitutions; dbSNP:rs121908633
- 307 binding UDP
- 321 binding UDP
- 331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 20% of wild-type activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
- 378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; corresponding to 10-30% of wild-type activity; decreased N-acylmannosamine kinase activity; impaired homohexamers formation; dbSNP:rs199877522
- 708 G → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; severely decreased; dbSNP:rs1554657922
- 712 M→T: Decreased N-acylmannosamine kinase activity.
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
25% identity, 95% coverage: 9:308/317 of query aligns to 84:386/396 of 5f7qE
Sites not aligning to the query:
- binding : 5, 8, 12, 15, 32, 43, 44, 67, 68, 68, 69, 69, 70, 70, 71, 72, 73
2aa4A Crystal structure of escherichia coli putative n-acetylmannosamine kinase, new york structural genomics consortium
38% identity, 80% coverage: 9:262/317 of query aligns to 3:247/289 of 2aa4A
P45425 N-acetylmannosamine kinase; ManNAc kinase; N-acetyl-D-mannosamine kinase; EC 2.7.1.60 from Escherichia coli (strain K12) (see paper)
38% identity, 80% coverage: 9:262/317 of query aligns to 3:247/291 of P45425
- L84 (≠ R94) mutation to P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation.
- V138 (= V150) mutation to M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation.
Query Sequence
>WP_012851426.1 NCBI__GCF_000024385.1:WP_012851426.1
MGQEHDAPVLAVDIGGTKLAAALVDPEGRITHYDRIATPADPDPRVLWRTLESLLDKLLA
EAGCPQPAGVGVGCGGPMRWPSGEVSPLNIPAWRDFPLRRRLRARHPDLPVRVHNDAICV
AVGEHWRGAGRGYDNVLGMVVSTGVGGGLVLGGRLIDGASGNAGHIGHVVVDPQGPPCEC
GGRGCLEAVARGPGLVAWAQRQGWRPGQAGVSGVELAEDARLGHPVAGAALQRAGRALGV
AIASAMHLCDLEVVAIGGGLAQCGPLLFDPLQEALREHARMEFARRVQVVPAALGQTAGL
VGAAALILAGDRYWNAD
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