SitesBLAST
Comparing Echvi_3420 FitnessBrowser__Cola:Echvi_3420 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
28% identity, 97% coverage: 3:273/280 of query aligns to 9:318/325 of 2qm1B
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
28% identity, 87% coverage: 1:243/280 of query aligns to 2:271/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P63), G67 (≠ S64), S79 (≠ T77), N105 (= N103), D106 (= D104), G132 (= G130), T133 (= T131), G134 (= G132), V135 (≠ L133), G136 (= G134), E155 (= E153), H158 (vs. gap), D188 (≠ E165)
- binding zinc ion: H158 (vs. gap), C179 (≠ Y159), C181 (≠ D161), C186 (vs. gap), E212 (≠ Q183), H216 (≠ A187)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
28% identity, 87% coverage: 1:243/280 of query aligns to 3:272/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G9), T12 (= T10), K13 (= K11), G133 (= G130), T134 (= T131), G194 (= G170), E198 (≠ T174), A211 (= A181), G256 (= G226), G257 (≠ S227), N260 (≠ K230)
- binding zinc ion: H159 (vs. gap), C180 (≠ Y159), C182 (≠ D161), C187 (vs. gap), E213 (≠ Q183), H217 (≠ A187)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
28% identity, 87% coverage: 1:243/280 of query aligns to 5:274/306 of 7p7wBBB
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
31% identity, 61% coverage: 57:226/280 of query aligns to 144:336/396 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
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
27% identity, 86% coverage: 30:271/280 of query aligns to 109:378/396 of 1z05A
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
31% identity, 61% coverage: 57:226/280 of query aligns to 63:252/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (≠ S64), N110 (≠ D104), N110 (≠ D104), S134 (≠ C128), V135 (≠ I129), G138 (= G132), L139 (= L133), G140 (= G134), E159 (= E153), H162 (vs. gap), E181 (= E165)
- binding zinc ion: H162 (vs. gap), C172 (vs. gap), C174 (≠ L160), C179 (vs. gap)
Sites not aligning to the query:
2gupA Structural genomics, the crystal structure of a rok family protein from streptococcus pneumoniae tigr4 in complex with sucrose
26% identity, 87% coverage: 5:247/280 of query aligns to 6:252/289 of 2gupA
Sites not aligning to the query:
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
28% identity, 93% coverage: 1:260/280 of query aligns to 9:283/311 of 4db3A
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
26% identity, 88% coverage: 1:246/280 of query aligns to 1:261/297 of Q93LQ8
- D7 (= D6) mutation to G: Loss of catalytic activity.
- G9 (= G8) mutation to A: Loss of catalytic activity.
- D103 (= D104) mutation to G: Loss of catalytic activity.
- G131 (= G132) mutation to A: Loss of catalytic activity.
- G133 (= G134) mutation to A: Loss of catalytic activity.
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
29% identity, 82% coverage: 3:232/280 of query aligns to 6:266/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G8), T13 (= T10), N14 (≠ K11), R16 (≠ Q13), T140 (= T131), G189 (= G170), L216 (≠ F185), V261 (≠ S227)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G9), G71 (≠ P63), G72 (≠ S64), R73 (≠ V65), S84 (≠ V76), T85 (= T77), L87 (vs. gap), N112 (= N103), D113 (= D104), G139 (= G130), T140 (= T131), G141 (= G132), I142 (≠ L133), E162 (= E153), H165 (vs. gap), E184 (= E165)
- binding calcium ion: N112 (= N103), N115 (= N106), G144 (≠ A135), A161 (≠ G152)
- binding zinc ion: H165 (vs. gap), C175 (vs. gap), C177 (vs. gap), C182 (≠ N163)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
29% identity, 82% coverage: 3:232/280 of query aligns to 6:266/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G8), G12 (= G9), T13 (= T10), N14 (≠ K11), R16 (≠ Q13), T140 (= T131), G189 (= G170), L216 (≠ F185), V261 (≠ S227)
- binding calcium ion: N112 (= N103), N115 (= N106), G144 (≠ A135), A161 (≠ G152)
- binding zinc ion: H165 (vs. gap), C175 (vs. gap), C177 (vs. gap), C182 (≠ N163)
1xc3A Structure of a putative fructokinase from bacillus subtilis (see paper)
27% identity, 96% coverage: 4:272/280 of query aligns to 5:276/295 of 1xc3A
3lm9A Crystal structure of fructokinase with adp and fructose bound in the active site (see paper)
27% identity, 96% coverage: 4:272/280 of query aligns to 5:276/294 of 3lm9A
- binding adenosine-5'-diphosphate: G130 (= G130), T131 (= T131), G182 (≠ T179), P183 (≠ T180), E186 (≠ Q183), A193 (= A190), G231 (≠ S227)
- binding beta-D-fructofuranose: G60 (≠ V62), D104 (= D104), I133 (≠ L133), E151 (= E153), E177 (≠ T174)
- binding zinc ion: H154 (≠ L156), C169 (vs. gap), H172 (vs. gap), C175 (≠ F172)
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
29% identity, 82% coverage: 3:232/280 of query aligns to 6:267/309 of 2yhwA
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, 82% coverage: 3:232/280 of query aligns to 410:675/722 of Q9Y223
- D413 (= D6) binding
- G416 (= G9) binding
- T417 (= T10) binding
- N418 (≠ K11) binding
- R420 (≠ Q13) binding
- I472 (= I60) 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 (≠ S64) binding ; binding
- R477 (≠ V65) binding ; binding
- T489 (= T77) binding ; binding
- N516 (= N103) binding ; binding
- D517 (= D104) 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 (= N106) 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 (≠ G111) 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 (= F115) 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 (= G132) binding
- E566 (= E153) binding
- H569 (vs. gap) binding ; binding ; binding
- V572 (≠ P158) 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 (vs. gap) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (vs. gap) binding
- C581 (vs. gap) binding
- C586 (≠ N163) binding
- I587 (= I164) 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 (= E165) binding ; binding
- A630 (= A187) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A188) 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.
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
26% identity, 90% coverage: 1:253/280 of query aligns to 2:286/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G8), T11 (= T10), K12 (= K11), G130 (= G130), T131 (= T131), G180 (= G170), G214 (≠ A184), S218 (vs. gap), G260 (≠ S227), V261 (≠ I228), E264 (≠ A231)
- binding beta-D-glucopyranose: G65 (≠ S64), P78 (≠ T77), N103 (= N103), D104 (= D104), L133 (= L133), G134 (= G134), E153 (= E153), H156 (≠ L156), E175 (= E165)
- binding zinc ion: H156 (≠ L156), C166 (vs. gap), C168 (vs. gap), C173 (vs. gap)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
26% identity, 90% coverage: 1:253/280 of query aligns to 2:286/312 of 3vgkB
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, 82% coverage: 3:232/280 of query aligns to 410:675/722 of O35826
- D413 (= D6) 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 (≠ Q13) 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
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
23% identity, 68% coverage: 53:241/280 of query aligns to 144:361/406 of P50456
- H247 (vs. gap) binding
- C257 (vs. gap) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (vs. gap) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (≠ N163) binding
- R306 (≠ A190) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ D194) 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.
Query Sequence
>Echvi_3420 FitnessBrowser__Cola:Echvi_3420
MKIGIDLGGTKVQIGLEKNGTIVRQQKAFLTEKDNLEASLAQLKEFIRPFISEAVSGIGI
GVPSVVDTAQGIVYNVTNIPAWEKVHLKDILEEEFNIPVMVNNDVNCFVLGEHRFGLGKN
FQHIVGLCIGTGLGAGLVLDNQLYMGHNCGAGEIGLVPYLDQNIEYYASGNFFTAIHDTT
ALQAFHAATAGDHDALQQWEEFGLHFGKAMLAAMYTYDPEAIIIGGSISKAYPFFSQALQ
KTLAEFIYPESFKRLKILISENEHIPMLGAAALTHLNLHP
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