SitesBLAST
Comparing WP_013403895.1 NCBI__GCF_000166355.1:WP_013403895.1 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)
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
31% identity, 99% coverage: 2:398/399 of query aligns to 6:395/396 of 5f7qE
- binding zinc ion: H243 (= H240), C253 (= C250), C255 (= C252), C260 (= C257)
- binding : K8 (≠ H4), K12 (= K8), N15 (= N11), T32 (≠ A28), S43 (≠ A39), T44 (= T40), T67 (≠ K63), G68 (= G64), G68 (= G64), G69 (= G65), G69 (= G65), R70 (= R66), R70 (= R66), R71 (= R67), A72 (≠ P68), K73 (≠ V69)
Sites not aligning to the query:
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
31% identity, 95% coverage: 7:384/399 of query aligns to 3:377/396 of 1z05A
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
33% identity, 64% coverage: 140:393/399 of query aligns to 61:306/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (= G149), N110 (≠ E188), N110 (≠ E188), S134 (= S212), V135 (= V213), G138 (= G216), L139 (= L217), G140 (= G218), E159 (= E237), H162 (= H240), E181 (= E259), E253 (≠ K340), W293 (≠ V380)
- binding zinc ion: H162 (= H240), C172 (= C250), C174 (= C252), C179 (= C257)
Sites not aligning to the query:
2qm1B Crystal structure of glucokinase from enterococcus faecalis
31% identity, 78% coverage: 80:389/399 of query aligns to 8:320/325 of 2qm1B
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
25% identity, 95% coverage: 7:384/399 of query aligns to 13:387/406 of P50456
- R52 (≠ D46) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ S79) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ I130) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H240) binding Zn(2+)
- C257 (= C250) 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 (= C252) 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 (= C257) binding Zn(2+)
- R306 (≠ D303) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ V307) mutation to G: Forms dimers but not tetramers; when associated with G-306.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
25% identity, 95% coverage: 7:384/399 of query aligns to 2:363/382 of 1z6rA
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
39% identity, 53% coverage: 143:354/399 of query aligns to 59:274/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G130 (= G214), T131 (≠ I215), G180 (≠ E264), G214 (≠ P294), S218 (≠ I298), G260 (≠ K340), V261 (= V341), E264 (≠ F344)
- binding beta-D-glucopyranose: G65 (= G149), P78 (= P162), N103 (= N187), D104 (≠ E188), L133 (= L217), G134 (= G218), E153 (= E237), H156 (= H240), E175 (= E259)
- binding zinc ion: H156 (= H240), C166 (= C250), C168 (= C252), C173 (= C257)
Sites not aligning to the query:
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
39% identity, 53% coverage: 143:354/399 of query aligns to 59:274/312 of 3vgkB
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
28% identity, 71% coverage: 79:361/399 of query aligns to 4:279/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G86), T13 (≠ D88), N14 (≠ Y89), R16 (≠ H91), T140 (≠ I215), G189 (≠ E264), L216 (≠ S295), V261 (≠ F343)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (≠ V87), G71 (≠ P148), G72 (= G149), R73 (≠ I150), S84 (≠ A161), T85 (≠ P162), L87 (= L164), N112 (= N187), D113 (≠ E188), G139 (= G214), T140 (≠ I215), G141 (= G216), I142 (≠ L217), E162 (= E237), H165 (= H240), E184 (= E259)
- binding calcium ion: N112 (= N187), N115 (= N190), G144 (≠ A219), A161 (≠ G236)
- binding zinc ion: H165 (= H240), C175 (= C250), C177 (= C252), C182 (= C257)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
28% identity, 71% coverage: 79:361/399 of query aligns to 4:279/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G86), G12 (≠ V87), T13 (≠ D88), N14 (≠ Y89), R16 (≠ H91), T140 (≠ I215), G189 (≠ E264), L216 (≠ S295), V261 (≠ F343)
- binding calcium ion: N112 (= N187), N115 (= N190), G144 (≠ A219), A161 (≠ G236)
- binding zinc ion: H165 (= H240), C175 (= C250), C177 (= C252), C182 (= C257)
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, 74% coverage: 68:361/399 of query aligns to 391:688/722 of Q9Y223
- D413 (= D84) binding Mg(2+); to Y: in THC12; likely pathogenic; dbSNP:rs1280775456
- G416 (≠ V87) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (≠ D88) binding ADP; to M: in THC12; likely pathogenic; dbSNP:rs1554659711
- N418 (≠ Y89) binding ADP
- R420 (≠ H91) binding ADP; to Q: in THC12; likely pathogenic; dbSNP:rs780092539
- I472 (= I145) 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 (≠ P148) to F: in THC12; likely pathogenic; requires 2 nucleotide substitutions
- G476 (= G149) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ I150) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- V485 (= V158) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells; requires 2 nucleotide substitutions
- L486 (= L159) to P: in THC12; uncertain significance; dbSNP:rs774867424
- T489 (≠ P162) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N187) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (≠ E188) 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 (= N190) to S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910
- A524 (≠ G195) 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 (= F199) to C: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986
- T544 (≠ I215) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells
- G545 (= G216) binding an N-acyl-D-mannosamine 6-phosphate
- C563 (≠ F234) to Y: in THC12; likely pathogenic; results in severely decreased cell surface sialylation
- E566 (= E237) binding an N-acyl-D-mannosamine
- H569 (= H240) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (≠ I243) 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 (≠ D247) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C250) binding Zn(2+)
- C581 (= C252) binding Zn(2+)
- C586 (= C257) binding Zn(2+)
- I587 (≠ L258) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603
- E588 (= E259) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (= A300) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A301) 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
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
28% identity, 71% coverage: 79:361/399 of query aligns to 4:280/309 of 2yhwA
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)
27% identity, 74% coverage: 68:361/399 of query aligns to 391:688/722 of O35826