SitesBLAST
Comparing 352021 FitnessBrowser__Btheta:352021 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)
2qm1B Crystal structure of glucokinase from enterococcus faecalis
35% identity, 98% coverage: 3:321/326 of query aligns to 1:322/325 of 2qm1B
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
35% identity, 94% coverage: 11:318/326 of query aligns to 4:309/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G16), T11 (= T18), K12 (≠ N19), G130 (= G143), T131 (= T144), G180 (≠ A193), G214 (≠ S223), S218 (≠ Y227), G260 (= G269), V261 (≠ L270), E264 (≠ S273)
- binding beta-D-glucopyranose: G65 (≠ N78), P78 (= P90), N103 (= N116), D104 (= D117), L133 (≠ V146), G134 (= G147), E153 (= E166), H156 (= H169), E175 (= E188)
- binding zinc ion: H156 (= H169), C166 (= C179), C168 (= C181), C173 (= C186)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
35% identity, 94% coverage: 11:318/326 of query aligns to 4:309/312 of 3vgkB
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
31% identity, 79% coverage: 66:323/326 of query aligns to 133:386/396 of 1z05A
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
26% identity, 95% coverage: 9:317/326 of query aligns to 2:300/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ D14), E10 (≠ G17), G70 (= G79), N110 (≠ D117), N110 (≠ D117), S134 (≠ T141), V135 (≠ L142), G138 (= G145), L139 (≠ V146), G140 (= G147), E159 (= E166), H162 (= H169), E181 (= E188), E253 (≠ G269), W293 (≠ A310)
- binding zinc ion: H162 (= H169), C172 (= C179), C174 (= C181), C179 (= C186)
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
26% identity, 96% coverage: 4:317/326 of query aligns to 78:384/396 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
1z6rA Crystal structure of mlc from escherichia coli (see paper)
28% identity, 60% coverage: 98:293/326 of query aligns to 152:343/382 of 1z6rA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
28% identity, 60% coverage: 98:293/326 of query aligns to 176:367/406 of P50456
- H247 (= H169) binding
- C257 (= C179) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C181) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C186) binding
- R306 (≠ Q232) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (= L236) mutation to G: Forms dimers but not tetramers; when associated with G-306.
Sites not aligning to the query:
- 52 R→H: Shows increased expression and forms larger colonies.
- 86 H→R: Can be bound and inactivated by MtfA.
- 136 F→A: Decreases association with PtsG EIIB domain.
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)
28% identity, 86% coverage: 5:285/326 of query aligns to 404:688/722 of Q9Y223
- D413 (= D14) binding
- G416 (= G17) binding
- T417 (= T18) binding
- N418 (= N19) binding
- R420 (≠ V21) binding
- I472 (≠ A76) 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 (vs. gap) binding ; binding
- R477 (vs. gap) binding ; binding
- T489 (≠ P90) binding ; binding
- N516 (= N116) binding ; binding
- D517 (= D117) active site; binding ; binding ; mutation D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure.
- N519 (= N119) 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 (≠ G124) 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 (≠ Y128) 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 (= G145) binding
- E566 (= E166) binding
- H569 (= H169) binding ; binding ; binding
- V572 (≠ A172) 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 (= G176) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C179) binding
- C581 (= C181) binding
- C586 (= C186) binding
- I587 (≠ L187) 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 (= E188) binding ; binding
- A630 (= A229) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A230) 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
- 23 binding
- 113 binding
- 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
- 253 binding
- 259 binding
- 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
- 280 binding
- 281 binding
- 282 binding
- 301 binding
- 302 binding
- 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
- 321 binding
- 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.
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
28% identity, 84% coverage: 11:285/326 of query aligns to 6:279/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G16), T13 (= T18), N14 (= N19), R16 (≠ V21), T140 (= T144), G189 (≠ A193), L216 (≠ K224), V261 (≠ G269)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G17), G71 (= G79), G72 (vs. gap), R73 (vs. gap), S84 (≠ A89), T85 (≠ P90), L87 (= L92), N112 (= N116), D113 (= D117), G139 (= G143), T140 (= T144), G141 (= G145), I142 (≠ V146), E162 (= E166), H165 (= H169), E184 (= E188)
- binding calcium ion: N112 (= N116), N115 (= N119), G144 (≠ S148), A161 (≠ G165)
- binding zinc ion: H165 (= H169), C175 (= C179), C177 (= C181), C182 (= C186)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
28% identity, 84% coverage: 11:285/326 of query aligns to 6:279/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G16), G12 (= G17), T13 (= T18), N14 (= N19), R16 (≠ V21), T140 (= T144), G189 (≠ A193), L216 (≠ K224), V261 (≠ G269)
- binding calcium ion: N112 (= N116), N115 (= N119), G144 (≠ S148), A161 (≠ G165)
- binding zinc ion: H165 (= H169), C175 (= C179), C177 (= C181), C182 (= C186)
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)
28% identity, 86% coverage: 5:285/326 of query aligns to 404:688/722 of O35826
- D413 (= D14) 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 (≠ V21) 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
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
27% identity, 84% coverage: 11:285/326 of query aligns to 6:280/309 of 2yhwA
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 87% coverage: 12:294/326 of query aligns to 8:283/306 of 7p7wBBB
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 87% coverage: 12:294/326 of query aligns to 5:280/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P77), G67 (≠ N78), S79 (≠ P90), N105 (= N116), D106 (= D117), G132 (= G143), T133 (= T144), G134 (= G145), V135 (= V146), G136 (= G147), E155 (= E166), H158 (= H169), D188 (≠ E188)
- binding zinc ion: H158 (= H169), C179 (= C179), C181 (= C181), C186 (= C186), E212 (≠ D225), H216 (≠ A229)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 87% coverage: 12:294/326 of query aligns to 6:281/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G17), T12 (= T18), K13 (≠ N19), G133 (= G143), T134 (= T144), G194 (≠ A193), E198 (≠ A197), A211 (≠ S223), G256 (= G268), G257 (= G269), N260 (≠ K272)
- binding zinc ion: H159 (= H169), C180 (= C179), C182 (= C181), C187 (= C186), E213 (≠ D225), H217 (≠ A229)
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
27% identity, 84% coverage: 11:285/326 of query aligns to 5:259/288 of 3eo3A
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
34% identity, 42% coverage: 98:234/326 of query aligns to 85:221/269 of 6jdcA
P45425 N-acetylmannosamine kinase; ManNAc kinase; N-acetyl-D-mannosamine kinase; EC 2.7.1.60 from Escherichia coli (strain K12) (see paper)
30% identity, 82% coverage: 10:277/326 of query aligns to 3:250/291 of P45425
- L84 (≠ I86) mutation to P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation.
- V138 (= V151) mutation to M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation.
2aa4A Crystal structure of escherichia coli putative n-acetylmannosamine kinase, new york structural genomics consortium
30% identity, 82% coverage: 10:277/326 of query aligns to 3:250/289 of 2aa4A
Query Sequence
>352021 FitnessBrowser__Btheta:352021
MNSNMEKPYVVGIDIGGTNTVFGIVDARGTIIASSSIKTAGYPTAAEYADEVCKNLLPLI
IANGGVDKIRGIGVGAPNGNYYTGTIEFAPNLPWKGILPLAAMFEERLGIPTALTNDANA
AAIGEMTYGAARGMKDFIMITLGTGVGSGIVINGQMVYGHDGFAGELGHVIARRDGRVCG
CGRKGCLETYCSATGVARTAREFLAARTDASLLRNIPAENITSKDVYDAAVQGDKLAQEI
FEFTGNILGEALADAIAFSSPEAIVLFGGLAKSGDYIMKPIQKAIDDNILNIYKGKTKLL
VSELKDSDAAVLGASALAWELKDLKE
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