SitesBLAST
Comparing 354180 FitnessBrowser__Btheta:354180 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, 99% coverage: 1:313/317 of query aligns to 4:321/325 of 2qm1B
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
34% identity, 96% coverage: 7:310/317 of query aligns to 4:308/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G12), T11 (= T14), K12 (≠ S15), G130 (= G142), T131 (= T143), G180 (≠ T192), G214 (= G217), S218 (≠ V221), G260 (= G263), V261 (≠ L264), E264 (≠ A267)
- binding beta-D-glucopyranose: G65 (= G75), P78 (≠ E89), N103 (= N115), D104 (= D116), L133 (≠ I145), G134 (= G146), E153 (= E165), 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)
34% identity, 96% coverage: 7:310/317 of query aligns to 4:308/312 of 3vgkB
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
27% identity, 85% coverage: 38:308/317 of query aligns to 108:378/396 of 1z05A
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
27% identity, 98% coverage: 5:314/317 of query aligns to 83:388/396 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
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
26% identity, 98% coverage: 5:314/317 of query aligns to 2:304/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ D10), E10 (≠ G13), G70 (= G75), N110 (≠ D116), N110 (≠ D116), S134 (≠ T140), V135 (= V141), G138 (= G144), L139 (≠ I145), G140 (= G146), E159 (= E165), H162 (= H168), E181 (= E187), E253 (≠ G263), W293 (≠ G303)
- binding zinc ion: H162 (= H168), C172 (= C178), C174 (= C180), C179 (= C185)
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
29% identity, 97% coverage: 9:317/317 of query aligns to 6:293/297 of Q93LQ8
- D7 (= D10) mutation to G: Loss of catalytic activity.
- G9 (= G12) mutation to A: Loss of catalytic activity.
- D103 (= D116) mutation to G: Loss of catalytic activity.
- G131 (= G144) mutation to A: Loss of catalytic activity.
- G133 (= G146) mutation to A: Loss of catalytic activity.
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
25% identity, 84% coverage: 44:308/317 of query aligns to 124:388/406 of P50456
- F136 (≠ K56) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H168) binding
- C257 (= C178) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C180) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C185) binding
- R306 (≠ Q226) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ I230) 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.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
25% identity, 84% coverage: 44:308/317 of query aligns to 100:364/382 of 1z6rA
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
28% identity, 97% coverage: 8:313/317 of query aligns to 8:305/306 of 7p7wBBB
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
28% identity, 97% coverage: 8:313/317 of query aligns to 5:302/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P74), G67 (= G75), S79 (≠ E89), N105 (= N115), D106 (= D116), G132 (= G142), T133 (= T143), G134 (= G144), V135 (≠ I145), G136 (= G146), E155 (= E165), H158 (= H168), D188 (≠ E187)
- binding zinc ion: H158 (= H168), C179 (= C178), C181 (= C180), C186 (= C185), E212 (≠ L219), H216 (≠ L223)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
28% identity, 97% coverage: 8:313/317 of query aligns to 6:303/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G13), T12 (= T14), K13 (≠ S15), G133 (= G142), T134 (= T143), G194 (≠ T192), E198 (≠ V196), A211 (≠ G217), G256 (= G262), G257 (= G263), N260 (≠ E266)
- binding zinc ion: H159 (= H168), C180 (= C178), C182 (= C180), C187 (= C185), E213 (≠ L219), H217 (≠ L223)
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)
32% identity, 87% coverage: 1:277/317 of query aligns to 404:681/722 of Q9Y223
- D413 (= D10) binding
- G416 (= G13) binding
- T417 (= T14) binding
- N418 (≠ S15) binding
- R420 (≠ K17) binding
- I472 (= I71) 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 (= G75) binding ; binding
- R477 (≠ I76) binding ; binding
- T489 (≠ A88) binding ; binding
- N516 (= N115) binding ; binding
- D517 (= D116) 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 (= N118) 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 (≠ Y127) 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
- E566 (= E165) binding
- H569 (= H168) binding ; binding ; binding
- V572 (≠ L171) 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
- C581 (= C180) binding
- C586 (= C185) binding
- 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 ; binding
- A630 (≠ L223) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (≠ Y224) 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.
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)
31% identity, 87% coverage: 1:277/317 of query aligns to 404:681/722 of O35826
- D413 (= D10) 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 (≠ K17) 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
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
31% identity, 95% coverage: 7:308/317 of query aligns to 4:288/298 of 3vovB
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
30% identity, 88% coverage: 6:284/317 of query aligns to 5:279/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G12), T13 (= T14), N14 (≠ S15), R16 (≠ K17), T140 (= T143), G189 (≠ T192), L216 (= L219), V261 (≠ G263)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G13), G71 (≠ P74), G72 (= G75), R73 (≠ I76), S84 (≠ G87), T85 (≠ A88), L87 (≠ N90), N112 (= N115), D113 (= D116), G139 (= G142), T140 (= T143), G141 (= G144), I142 (= I145), E162 (= E165), H165 (= H168), E184 (= E187)
- binding calcium ion: N112 (= N115), N115 (= N118), G144 (= G147), A161 (≠ T164)
- 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)
30% identity, 88% coverage: 6:284/317 of query aligns to 5:279/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G12), G12 (= G13), T13 (= T14), N14 (≠ S15), R16 (≠ K17), T140 (= T143), G189 (≠ T192), L216 (= L219), V261 (≠ G263)
- binding calcium ion: N112 (= N115), N115 (= N118), G144 (= G147), A161 (≠ T164)
- binding zinc ion: H165 (= H168), C175 (= C178), C177 (= C180), C182 (= C185)
P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
27% identity, 99% coverage: 1:314/317 of query aligns to 1:299/309 of P32718
- A73 (≠ G75) mutation to G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation.
- F145 (≠ G147) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
31% identity, 88% coverage: 6:284/317 of query aligns to 5:280/309 of 2yhwA
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
30% identity, 97% coverage: 8:315/317 of query aligns to 12:310/311 of 4db3A
Query Sequence
>354180 FitnessBrowser__Btheta:354180
MEKEYAIGIDLGGTSVKYALIDNNGVFHFQGKLPSNADVSAEAVIGQLVKAVNEVKTFAE
AKRYTIAGIGIGTPGIVDCTNRIVLGGAENIQGWENLKLADRMEKETGLPTQLGNDANLM
GLGETMYGAGNGATHVVFLTVGTGIGGAVIIDGKLFNGYANRGTELGHVPLIANGEPCAC
GSIGCLEHYASTAALVRRFSKRIAEAGISYPNEEINGELIVRLYKQGDKIAAESLNEHCD
FLGHGIAGFINIFSPQRVVIGGGLSEAGDFYIQKVSEKALRYAIPDCAVNTEIMAASLGN
KAGSIGAASLFLNRKPN
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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