SitesBLAST
Comparing WP_092057054.1 NCBI__GCF_900111775.1:WP_092057054.1 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)
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
37% identity, 96% coverage: 6:311/318 of query aligns to 4:308/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G11), T11 (= T13), K12 (≠ N14), G130 (= G139), T131 (= T140), G180 (≠ A189), G214 (≠ S218), S218 (≠ G222), G260 (= G264), V261 (≠ A265), E264 (≠ S268)
- binding beta-D-glucopyranose: G65 (= G74), P78 (= P89), N103 (= N112), D104 (= D113), L133 (≠ V142), G134 (= G143), E153 (= E162), H156 (= H165), E175 (= E184)
- binding zinc ion: H156 (= H165), C166 (= C175), C168 (= C177), C173 (= C182)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
37% identity, 96% coverage: 6:311/318 of query aligns to 4:308/312 of 3vgkB
2qm1B Crystal structure of glucokinase from enterococcus faecalis
33% identity, 98% coverage: 1:311/318 of query aligns to 4:318/325 of 2qm1B
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
34% identity, 82% coverage: 51:311/318 of query aligns to 122:380/396 of 1z05A
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
28% identity, 84% coverage: 44:309/318 of query aligns to 125:388/406 of P50456
- F136 (≠ L55) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H165) binding Zn(2+)
- C257 (= C175) 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 (= C177) 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 (= C182) binding Zn(2+)
- R306 (≠ Q227) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (= L231) 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)
28% identity, 84% coverage: 44:309/318 of query aligns to 101:364/382 of 1z6rA
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
29% identity, 97% coverage: 6:312/318 of query aligns to 11:308/311 of 4db3A
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
31% identity, 96% coverage: 7:312/318 of query aligns to 5:302/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P73), G67 (= G74), S79 (≠ P86), N105 (= N112), D106 (= D113), G132 (= G139), T133 (= T140), G134 (= G141), V135 (= V142), G136 (= G143), E155 (= E162), H158 (= H165), D188 (≠ E184)
- binding zinc ion: H158 (= H165), C179 (= C175), C181 (= C177), C186 (= C182), E212 (= E215), H216 (≠ R219)
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
31% identity, 96% coverage: 7:312/318 of query aligns to 6:303/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (= G12), T12 (= T13), K13 (≠ N14), G133 (= G139), T134 (= T140), G194 (≠ A189), E198 (≠ A193), A211 (= A213), G256 (= G264), G257 (≠ A265), N260 (≠ S268)
- binding zinc ion: H159 (= H165), C180 (= C175), C182 (= C177), C187 (= C182), E213 (= E215), H217 (≠ R219)
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
31% identity, 96% coverage: 7:312/318 of query aligns to 8:305/306 of 7p7wBBB
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
31% identity, 77% coverage: 68:311/318 of query aligns to 145:384/396 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)
32% identity, 77% coverage: 68:311/318 of query aligns to 64:300/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (= G74), N110 (≠ D113), N110 (≠ D113), S134 (≠ T137), V135 (≠ L138), G138 (= G141), L139 (≠ V142), G140 (= G143), E159 (= E162), H162 (= H165), E181 (= E184), E253 (≠ G264), W293 (≠ G304)
- binding zinc ion: H162 (= H165), C172 (= C175), C174 (= C177), C179 (= C182)
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, 81% coverage: 5:263/318 of query aligns to 3:240/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (≠ N14), S129 (≠ G139), T130 (= T140), P195 (= P205), K196 (≠ R219)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ V68), G63 (= G69), A72 (≠ V82), L73 (≠ T83), N74 (≠ T84), N77 (= N87), N102 (= N112), D103 (= D113), S129 (≠ G139), T130 (= T140), H152 (≠ E162), H155 (= H165), E174 (= E184)
- binding zinc ion: H155 (= H165), C165 (= C175), C167 (= C177), C172 (= C182)
Sites not aligning to the query:
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
34% identity, 58% coverage: 8:192/318 of query aligns to 6:183/269 of 6jdcA
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
30% identity, 87% coverage: 2:279/318 of query aligns to 2:276/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G11), T13 (= T13), N14 (= N14), R16 (= R16), T140 (= T140), G189 (≠ A189), L216 (≠ R219), V261 (≠ G264)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G12), G71 (≠ P73), G72 (= G74), R73 (≠ L75), S84 (= S85), T85 (≠ P86), L87 (= L88), N112 (= N112), D113 (= D113), G139 (= G139), T140 (= T140), G141 (= G141), I142 (≠ V142), E162 (= E162), H165 (= H165), E184 (= E184)
- binding calcium ion: N112 (= N112), N115 (= N115), G144 (= G144), A161 (≠ G161)
- binding zinc ion: H165 (= H165), C175 (= C175), C177 (= C177), C182 (= C182)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
30% identity, 87% coverage: 2:279/318 of query aligns to 2:276/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G11), G12 (= G12), T13 (= T13), N14 (= N14), R16 (= R16), T140 (= T140), G189 (≠ A189), L216 (≠ R219), V261 (≠ G264)
- binding calcium ion: N112 (= N112), N115 (= N115), G144 (= G144), A161 (≠ G161)
- binding zinc ion: H165 (= H165), C175 (= C175), C177 (= C177), C182 (= C182)
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
31% identity, 87% coverage: 2:279/318 of query aligns to 2:277/309 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)
33% identity, 82% coverage: 2:263/318 of query aligns to 406:669/722 of Q9Y223
- D413 (= D9) binding Mg(2+)
- G416 (= G12) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (= T13) binding ADP
- N418 (= N14) binding ADP
- R420 (= R16) binding ADP
- I472 (≠ M70) 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 (= G74) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ L75) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ P86) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N112) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D113) 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 (= N115) 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 (≠ G120) 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 (= F124) 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 (= G141) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (= E162) binding an N-acyl-D-mannosamine
- H569 (= H165) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (= V168) 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 (= G172) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C175) binding Zn(2+)
- C581 (= C177) binding Zn(2+)
- C586 (= C182) binding Zn(2+)
- I587 (≠ L183) 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 (= E184) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (= A224) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A225) 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 UDP
- 23 binding UDP
- 113 binding UDP
- 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 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; 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 UDP
- 321 binding UDP
- 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.
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
27% identity, 96% coverage: 5:309/318 of query aligns to 3:283/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
27% identity, 96% coverage: 5:309/318 of query aligns to 3:283/293 of 6jdhA
Query Sequence
>WP_092057054.1 NCBI__GCF_900111775.1:WP_092057054.1
MTPAAVGIDLGGTNCRAALVGPQGRIGELLRRPTRMGADYAAWLEDFAGGIDELLRQGQA
LGLKVTAVGMGAPGLIALDGTVTTSPNLPALDGRPLAADLAERLQLPVVVANDANAIAWG
EALFGAGRDFSSFIGLTLGTGVGGGLVLDRRLWLGADGAAGEVGHWTVVPDGRPCGCGNR
GCLEQYASARALAVLARERIAAGEPSALAQIAAGELTSRQVGDAARQGDALALAVLEEAG
GYLGQVLGGIANLLNLDGAVIAGGAVDSFDLMHPAILRELRRHVFAVPGRRLVVVPGQLA
DEAGILGAAALTGFSEQL
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