SitesBLAST
Comparing WP_039969159.1 NCBI__GCF_000195635.1:WP_039969159.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2qm1B Crystal structure of glucokinase from enterococcus faecalis
26% identity, 99% coverage: 3:272/274 of query aligns to 9:318/325 of 2qm1B
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
24% identity, 92% coverage: 23:273/274 of query aligns to 25:301/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (≠ S64), N110 (≠ D104), N110 (≠ D104), S134 (≠ T128), V135 (≠ I129), G138 (= G132), L139 (≠ I133), G140 (= G134), E159 (= E153), H162 (≠ S156), E181 (vs. gap), E253 (≠ G225), W293 (≠ S265)
- binding zinc ion: H162 (≠ S156), C172 (≠ R166), C174 (= C168), C179 (vs. gap)
Sites not aligning to the query:
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
24% identity, 92% coverage: 23:273/274 of query aligns to 106:385/396 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
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
25% identity, 98% coverage: 1:269/274 of query aligns to 1:281/297 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.
3lm9A Crystal structure of fructokinase with adp and fructose bound in the active site (see paper)
27% identity, 88% coverage: 5:246/274 of query aligns to 6:247/294 of 3lm9A
- binding adenosine-5'-diphosphate: G130 (= G130), T131 (= T131), G182 (≠ A182), P183 (≠ A183), E186 (≠ N186), A193 (= A193), G231 (= G226)
- binding beta-D-fructofuranose: G60 (≠ S64), D104 (= D104), I133 (= I133), E151 (≠ G150), E177 (≠ D177)
- binding zinc ion: H154 (≠ E153), C169 (= C168), H172 (≠ F172), C175 (≠ R175)
1xc3A Structure of a putative fructokinase from bacillus subtilis (see paper)
27% identity, 88% coverage: 5:246/274 of query aligns to 6:247/295 of 1xc3A
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
24% identity, 86% coverage: 40:274/274 of query aligns to 122:381/396 of 1z05A
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 84% coverage: 17:246/274 of query aligns to 86:341/382 of 1z6rA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
26% identity, 84% coverage: 17:246/274 of query aligns to 110:365/406 of P50456
- F136 (= F44) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (vs. gap) binding Zn(2+)
- C257 (≠ L143) binding Zn(2+); mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (≠ G145) binding Zn(2+); mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (≠ E153) binding Zn(2+)
- R306 (≠ Q189) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ A193) 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.
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
27% identity, 89% coverage: 1:245/274 of query aligns to 2:279/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G8), T11 (= T10), K12 (≠ N11), G130 (= G130), T131 (= T131), G180 (≠ S170), G214 (vs. gap), S218 (≠ A184), G260 (= G226), V261 (≠ I227), E264 (≠ A230)
- binding beta-D-glucopyranose: G65 (≠ S64), P78 (≠ A77), N103 (= N103), D104 (= D104), L133 (≠ I133), G134 (= G134), E153 (= E153), H156 (≠ S156), E175 (= E165)
- binding zinc ion: H156 (≠ S156), C166 (vs. gap), C168 (vs. gap), C173 (≠ D163)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
27% identity, 89% coverage: 1:245/274 of query aligns to 2:279/312 of 3vgkB
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
29% identity, 84% coverage: 3:231/274 of query aligns to 6:266/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G8), T13 (= T10), N14 (= N11), R16 (= R13), T140 (= T131), G189 (≠ S170), L216 (vs. gap), V261 (≠ G226)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G9), G71 (≠ P63), G72 (≠ S64), R73 (≠ I65), S84 (≠ N75), T85 (≠ V76), L87 (≠ N78), N112 (= N103), D113 (= D104), G139 (= G130), T140 (= T131), G141 (= G132), I142 (= I133), E162 (= E153), H165 (≠ S156), E184 (= E165)
- binding calcium ion: N112 (= N103), N115 (= N106), G144 (≠ A135), A161 (≠ G152)
- binding zinc ion: H165 (≠ S156), C175 (vs. gap), C177 (vs. gap), C182 (vs. gap)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
29% identity, 84% coverage: 3:231/274 of query aligns to 6:266/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G8), G12 (= G9), T13 (= T10), N14 (= N11), R16 (= R13), T140 (= T131), G189 (≠ S170), L216 (vs. gap), V261 (≠ G226)
- binding calcium ion: N112 (= N103), N115 (= N106), G144 (≠ A135), A161 (≠ G152)
- binding zinc ion: H165 (≠ S156), C175 (vs. gap), C177 (vs. gap), C182 (vs. gap)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
26% identity, 91% coverage: 1:249/274 of query aligns to 5:274/306 of 7p7wBBB
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
26% identity, 91% coverage: 1:249/274 of query aligns to 3:272/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G9), T12 (= T10), K13 (≠ N11), G133 (= G130), T134 (= T131), G194 (≠ A162), E198 (= E165), A211 (≠ G180), G256 (= G225), G257 (= G226), N260 (≠ A237)
- binding zinc ion: H159 (≠ S156), C180 (vs. gap), C182 (vs. gap), C187 (vs. gap), E213 (≠ A182), H217 (≠ N186)
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
26% identity, 91% coverage: 1:249/274 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 (≠ A77), N105 (= N103), D106 (= D104), G132 (= G130), T133 (= T131), G134 (= G132), V135 (≠ I133), G136 (= G134), E155 (= E153), H158 (≠ S156), D188 (vs. gap)
- binding zinc ion: H158 (≠ S156), C179 (vs. gap), C181 (vs. gap), C186 (vs. gap), E212 (≠ A182), H216 (≠ N186)
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
33% identity, 60% coverage: 1:165/274 of query aligns to 9:175/311 of 4db3A
Sites not aligning to the query:
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
29% identity, 86% coverage: 3:239/274 of query aligns to 6:276/309 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 26 papers)
28% identity, 84% coverage: 3:231/274 of query aligns to 410:675/722 of Q9Y223
- D413 (= D6) binding Mg(2+); to Y: in THC12; likely pathogenic; dbSNP:rs1280775456
- G416 (= G9) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (= T10) binding ADP; to M: in THC12; likely pathogenic; dbSNP:rs1554659711
- N418 (= N11) binding ADP
- R420 (= R13) binding ADP; to Q: in THC12; likely pathogenic; dbSNP:rs780092539
- I472 (= I60) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity corresponding to less than 10% of wild-type activity
- G475 (≠ P63) to F: in THC12; likely pathogenic; requires 2 nucleotide substitutions
- G476 (≠ S64) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ I65) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- V485 (= V73) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells; requires 2 nucleotide substitutions
- L486 (vs. gap) to P: in THC12; uncertain significance; dbSNP:rs774867424
- T489 (≠ V76) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N103) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D104) 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 (= N106) to S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910
- 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 (≠ Y115) to C: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986
- T544 (= T131) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells
- G545 (= G132) binding an N-acyl-D-mannosamine 6-phosphate
- C563 (≠ G150) to Y: in THC12; likely pathogenic; results in severely decreased cell surface sialylation
- E566 (= E153) binding an N-acyl-D-mannosamine
- H569 (≠ S156) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (≠ Y159) to L: in NM and THC12; likely pathogenic; mildly decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
- G576 (≠ A162) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (vs. gap) binding Zn(2+)
- C581 (vs. gap) binding Zn(2+)
- C586 (vs. gap) binding Zn(2+)
- I587 (≠ F164) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603
- E588 (= E165) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (vs. gap) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A187) to V: in NM; does not affect homohexamers formation; dbSNP:rs62541771
Sites not aligning to the query:
- 13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase 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; impaired homohexamers formation
- 157 H → Y: in THC12; likely pathogenic
- 176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase 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; impaired homohexamers formation; dbSNP:rs539332585
- 200 I → F: in NM; uncertain significance; 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; requires 2 nucleotide substitutions; dbSNP:rs121908633
- 307 binding UDP
- 321 binding UDP
- 331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
- 378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; impaired homohexamers formation; dbSNP:rs199877522
- 420:722 natural variant: Missing (in THC12; likely pathogenic)
- 704 P → R: in THC12; likely pathogenic; the orthologous mutation in mouse embryos results in cerebrospinal hemorrhages and defective angiogenesis; results in loss of cell surface sialylation
- 708 G → S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; severely decreased N-acylmannosamine kinase activity; dbSNP:rs1554657922
- 712 M → T: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs28937594
2gupA Structural genomics, the crystal structure of a rok family protein from streptococcus pneumoniae tigr4 in complex with sucrose
31% identity, 57% coverage: 4:160/274 of query aligns to 5:154/289 of 2gupA
Sites not aligning to the query:
Query Sequence
>WP_039969159.1 NCBI__GCF_000195635.1:WP_039969159.1
MKLSIDLGGTNIRVAQVEEGRCLSKVSVPCLAQQDAPIVLDQLFQLVRSMMNEQVDGIGI
GVPSIVDSEKGIVYNVANISSWKEIRLKEILENEFNVAVAINNDSNCFALGESLYGEGKP
YDNMVGVTIGTGIGAGVIIGRRLYGGQFMGAGEIGSFPYLDADFERYCSSFFFKRHDTTG
AAAAENARQGEQAALDIWKEFGMHLGNLVKVILFAYAPQAIVLGGGIVAAYPFFKDAMEY
TMQSFPYRVMLDNVRVIASHQNDSSLLGASALLE
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