SitesBLAST
Comparing WP_004110897.1 NCBI__GCF_000359745.1:WP_004110897.1 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)
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
27% identity, 79% coverage: 10:333/408 of query aligns to 1:332/396 of 1z05A
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
26% identity, 72% coverage: 8:301/408 of query aligns to 9:307/406 of P50456
- R52 (≠ E51) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ Y84) mutation to R: Can be bound and inactivated by MtfA.
- F136 (= F137) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H247) binding Zn(2+)
- C257 (= C257) 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 (= C259) 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 (= C264) binding Zn(2+)
- R306 (= R300) mutation to G: Forms dimers but not tetramers; when associated with G-310.
Sites not aligning to the query:
- 310 L→G: Forms dimers but not tetramers; when associated with G-306.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
26% identity, 71% coverage: 11:301/408 of query aligns to 1:283/382 of 1z6rA
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
25% identity, 64% coverage: 8:270/408 of query aligns to 7:266/396 of 5f7qE
- binding zinc ion: H243 (= H247), C253 (= C257), C255 (= C259), C260 (= C264)
- binding : K8 (≠ L9), K12 (= K13), N15 (= N16), T32 (≠ A33), S43 (≠ Q44), T44 (= T45), T67 (≠ A68), G68 (≠ R69), G68 (≠ R69), G69 (= G70), G69 (= G70), R70 (≠ Q71), R70 (≠ Q71), R71 (≠ P72), A72 (≠ I73), K73 (≠ I74)
Sites not aligning to the query:
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
27% identity, 57% coverage: 113:345/408 of query aligns to 29:246/290 of 6jdbA
- binding adenosine-5'-diphosphate: S129 (≠ A219), T130 (≠ G220), P195 (= P288), K196 (≠ D289), S241 (= S334)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ P152), G63 (= G153), A72 (≠ S162), L73 (= L163), N74 (≠ S164), N77 (= N167), N102 (= N192), D103 (= D193), S129 (≠ A219), T130 (≠ G220), H152 (≠ E244), H155 (= H247), E174 (≠ D266)
- binding zinc ion: H155 (= H247), C165 (= C257), C167 (= C259), C172 (= C264)
Sites not aligning to the query:
2qm1B Crystal structure of glucokinase from enterococcus faecalis
24% identity, 74% coverage: 86:387/408 of query aligns to 9:324/325 of 2qm1B
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
26% identity, 64% coverage: 86:345/408 of query aligns to 4:226/269 of 6jdcA
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
28% identity, 57% coverage: 147:380/408 of query aligns to 58:283/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
28% identity, 57% coverage: 147:380/408 of query aligns to 58:283/293 of 6jdhA
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
26% identity, 66% coverage: 117:384/408 of query aligns to 38:309/311 of 4db3A
2aa4A Crystal structure of escherichia coli putative n-acetylmannosamine kinase, new york structural genomics consortium
31% identity, 49% coverage: 147:345/408 of query aligns to 59:247/289 of 2aa4A
P45425 N-acetylmannosamine kinase; ManNAc kinase; N-acetyl-D-mannosamine kinase; EC 2.7.1.60 from Escherichia coli (strain K12) (see paper)
31% identity, 49% coverage: 147:345/408 of query aligns to 59:247/291 of P45425
- L84 (≠ Q172) mutation to P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation.
- V138 (vs. gap) mutation to M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation.
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 58% coverage: 147:384/408 of query aligns to 64:306/306 of 7p7wBBB
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 58% coverage: 147:384/408 of query aligns to 61:303/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P152), G67 (= G153), S79 (≠ L166), N105 (= N192), D106 (= D193), G132 (≠ A219), T133 (≠ G222), G134 (= G223), V135 (≠ I224), G136 (= G225), E155 (= E244), H158 (= H247), D188 (= D266)
- binding zinc ion: H158 (= H247), C179 (= C257), C181 (= C259), C186 (= C264), E212 (≠ D290), H216 (≠ M294)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
26% identity, 65% coverage: 119:384/408 of query aligns to 34:304/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G133 (≠ A219), T134 (≠ G222), G194 (≠ P271), E198 (≠ Y275), A211 (≠ P288), G256 (= G333), G257 (≠ S334), N260 (≠ P337)
- binding zinc ion: H159 (= H247), C180 (= C257), C182 (= C259), C187 (= C264), E213 (≠ D290), H217 (≠ M294)
Sites not aligning to the query:
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
34% identity, 39% coverage: 167:326/408 of query aligns to 79:236/298 of 3vovB
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
26% identity, 46% coverage: 84:270/408 of query aligns to 2:185/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ E89), E10 (≠ R92), G70 (= G153), N110 (≠ D193), N110 (≠ D193), S134 (≠ F217), V135 (≠ L218), G138 (= G223), L139 (≠ I224), G140 (= G225), E159 (= E244), H162 (= H247), E181 (≠ D266)
- binding zinc ion: H162 (= H247), C172 (= C257), C174 (= C259), C179 (= C264)
Sites not aligning to the query:
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)
35% identity, 31% coverage: 143:270/408 of query aligns to 466:592/722 of Q9Y223
- I472 (= I149) 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 (≠ P152) to F: in THC12; likely pathogenic; requires 2 nucleotide substitutions
- G476 (= G153) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (= R154) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- V485 (≠ T161) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells; requires 2 nucleotide substitutions
- L486 (≠ S162) to P: in THC12; uncertain significance; dbSNP:rs774867424
- T489 (≠ P165) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N192) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D193) 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 (≠ T195) to S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910
- A524 (≠ G200) 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 (≠ Y204) to C: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986
- T544 (≠ G220) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells
- G545 (≠ D221) binding an N-acyl-D-mannosamine 6-phosphate
- C563 (≠ N241) to Y: in THC12; likely pathogenic; results in severely decreased cell surface sialylation
- E566 (= E244) binding an N-acyl-D-mannosamine
- H569 (= H247) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (= V250) 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 (= G254) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C257) binding Zn(2+)
- C581 (= C259) binding Zn(2+)
- C586 (= C264) binding Zn(2+)
- I587 (≠ L265) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603
- E588 (≠ D266) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
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
- 413 binding Mg(2+); D → Y: in THC12; likely pathogenic; dbSNP:rs1280775456
- 416 binding an N-acyl-D-mannosamine 6-phosphate
- 417 binding ADP; T → M: in THC12; likely pathogenic; dbSNP:rs1554659711
- 418 binding ADP
- 420 binding ADP; R → Q: in THC12; likely pathogenic; dbSNP:rs780092539
- 420:722 natural variant: Missing (in THC12; likely pathogenic)
- 630 A → T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- 631 A → V: in NM; does not affect homohexamers formation; dbSNP:rs62541771
- 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)
33% identity, 37% coverage: 143:291/408 of query aligns to 62:204/309 of 2yhwA
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
38% identity, 30% coverage: 147:270/408 of query aligns to 59:179/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G130 (≠ A219), T131 (≠ G220)
- binding beta-D-glucopyranose: G65 (= G153), P78 (≠ L166), N103 (= N192), D104 (= D193), L133 (≠ I224), G134 (= G225), E153 (= E244), H156 (= H247), E175 (≠ D266)
- binding zinc ion: H156 (= H247), C166 (= C257), C168 (= C259), C173 (= C264)
Sites not aligning to the query:
Query Sequence
>WP_004110897.1 NCBI__GCF_000359745.1:WP_004110897.1
MKTISGTNLEQAKSHNRRVVIEAIRTNGPLSRAAIARLTALTTQTVSNIVEELARSHLLI
PMEAQKIARGQPIIPYTINPSGAYSIGLELGRQRAAGVLTDLSGTVCARIDRHVDRPGPT
EAMPVFAAIVRDLQEAFSFDRDRLLGVGIALPGRYADGGVTSLSPLNLPGWQNFPVAREL
ERLIGLPVLVENDATAGAIGERLYGVARGLGSFVYLFLAGDGGIGAGMFLDGHLYKGSRA
NAGEIGHIIVEPHGRLCTCGKRGCLDRYVSPSVAYECLGIEDAQELDPDDLDAMIAANSR
GLQTWLEQAVQPLRQTIDFLELAFDPQTIVLGGSAPPSLMTGLAERVEPLHIPVNPMEER
KIPRLMVGATGKDTAILGAAALPIFSETNPQFDVLQKPIIHRAAEQAG
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