SitesBLAST
Comparing CA265_RS23280 FitnessBrowser__Pedo557:CA265_RS23280 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)
1z6rA Crystal structure of mlc from escherichia coli (see paper)
29% identity, 63% coverage: 134:397/417 of query aligns to 106:364/382 of 1z6rA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
29% identity, 63% coverage: 134:397/417 of query aligns to 130:388/406 of P50456
- F136 (≠ L140) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H250) binding
- C257 (= C260) binding ; mutation to A: Strongly reduced activity; when associated with A-259.; mutation to S: Strongly reduced activity; when associated with S-259.
- C259 (= C262) binding ; mutation to A: Strongly reduced activity; when associated with A-257.; mutation to S: Strongly reduced activity; when associated with S-257.
- C264 (= C267) binding
- R306 (≠ K315) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ Y319) 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.
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
26% identity, 90% coverage: 23:397/417 of query aligns to 10:378/396 of 1z05A
2qm1B Crystal structure of glucokinase from enterococcus faecalis
28% identity, 61% coverage: 145:398/417 of query aligns to 63:317/325 of 2qm1B
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
27% identity, 74% coverage: 90:397/417 of query aligns to 2:306/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (≠ F97), T11 (= T99), K12 (= K100), G130 (≠ D224), T131 (≠ W225), G180 (= G274), G214 (≠ P306), S218 (≠ I310), G260 (≠ K352), V261 (≠ I353), E264 (≠ A356)
- binding beta-D-glucopyranose: G65 (= G159), P78 (≠ F172), N103 (= N197), D104 (= D198), L133 (≠ V227), G134 (= G228), E153 (= E247), H156 (= H250), E175 (= E269)
- binding zinc ion: H156 (= H250), C166 (= C260), C168 (= C262), C173 (= C267)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
27% identity, 74% coverage: 90:397/417 of query aligns to 2:306/312 of 3vgkB
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
22% identity, 93% coverage: 19:405/417 of query aligns to 14:390/396 of 5f7qE
- binding zinc ion: H243 (= H250), C253 (= C260), C255 (= C262), C260 (= C267)
- binding : N15 (≠ Q20), T32 (≠ S37), S43 (≠ P48), T44 (≠ S49), T67 (≠ I72), G68 (= G73), G68 (= G73), G69 (= G74), G69 (= G74), R70 (= R75), R70 (= R75), R71 (≠ K76), A72 (≠ P77), K73 (≠ D78)
Sites not aligning to the query:
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)
29% identity, 61% coverage: 149:401/417 of query aligns to 466:721/722 of O35826
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
- 413 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.
- 420 R→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.
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)
29% identity, 61% coverage: 149:401/417 of query aligns to 466:721/722 of Q9Y223
- I472 (≠ V155) 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 (= G159) binding ; binding
- R477 (≠ L160) binding ; binding
- T489 (≠ S170) binding ; binding
- N516 (= N197) binding ; binding
- D517 (= D198) 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 (= N200) 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 (= A205) 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 (≠ H209) 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 (= G226) binding
- E566 (= E247) binding
- H569 (= H250) binding ; binding ; binding
- V572 (≠ F253) 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 (= G257) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C260) binding
- C581 (= C262) binding
- C586 (= C267) binding
- I587 (≠ L268) 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 (= E269) binding ; binding
- A630 (= A312) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A313) 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.
- G708 (= G388) to S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; severely decreased; dbSNP:rs1554657922
- M712 (≠ R392) mutation to 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
- 413 binding
- 416 binding
- 417 binding
- 418 binding
- 420 binding
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
30% identity, 59% coverage: 149:396/417 of query aligns to 62:308/309 of 2yhwA
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
25% identity, 62% coverage: 149:405/417 of query aligns to 60:306/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (= G159), N110 (≠ D198), N110 (≠ D198), S134 (≠ L222), V135 (≠ M223), G138 (= G226), L139 (≠ V227), G140 (= G228), E159 (= E247), H162 (= H250), E181 (= E269), E253 (≠ K352), W293 (≠ R392)
- binding zinc ion: H162 (= H250), C172 (= C260), C174 (= C262), C179 (= C267)
Sites not aligning to the query:
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
30% identity, 59% coverage: 149:396/417 of query aligns to 62:307/308 of 2yi1A
- binding adenosine-5'-diphosphate: T140 (≠ W225), G189 (= G274), L216 (= L308), V261 (≠ K352)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (≠ P158), G72 (= G159), R73 (≠ L160), S84 (≠ Y169), T85 (≠ S170), L87 (≠ F172), N112 (= N197), D113 (= D198), G139 (≠ D224), T140 (≠ W225), G141 (= G226), I142 (≠ V227), E162 (= E247), H165 (= H250), E184 (= E269)
- binding calcium ion: N112 (= N197), N115 (= N200), G144 (≠ L229), A161 (≠ G246)
- binding zinc ion: H165 (= H250), C175 (= C260), C177 (= C262), C182 (= C267)
Sites not aligning to the query:
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
30% identity, 59% coverage: 149:396/417 of query aligns to 62:307/308 of 2yhyA
Sites not aligning to the query:
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
32% identity, 54% coverage: 172:396/417 of query aligns to 62:287/288 of 3eo3A
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
26% identity, 52% coverage: 180:397/417 of query aligns to 85:282/290 of 6jdbA
- binding adenosine-5'-diphosphate: S129 (≠ D224), T130 (≠ W225), P195 (= P306), K196 (≠ A307), S241 (≠ K352)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: N102 (= N197), D103 (= D198), S129 (≠ D224), T130 (≠ W225), H152 (≠ E247), H155 (= H250), E174 (= E269)
- binding zinc ion: H155 (= H250), C165 (= C260), C167 (= C262), C172 (= C267)
Sites not aligning to the query:
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
26% identity, 66% coverage: 121:397/417 of query aligns to 29:283/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
26% identity, 66% coverage: 121:397/417 of query aligns to 29:283/293 of 6jdhA
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
30% identity, 61% coverage: 147:399/417 of query aligns to 57:290/298 of 3vovB
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
26% identity, 48% coverage: 155:354/417 of query aligns to 63:258/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P158), G67 (= G159), S79 (≠ Y171), N105 (= N197), D106 (= D198), G132 (≠ D224), T133 (≠ W225), G134 (= G226), V135 (= V227), G136 (= G228), E155 (= E247), H158 (= H250), D188 (≠ E269)
- binding zinc ion: H158 (= H250), C179 (= C260), C181 (= C262), C186 (= C267), E212 (= E300), H216 (≠ A312)
P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
30% identity, 48% coverage: 152:353/417 of query aligns to 66:248/309 of P32718
- A73 (≠ G159) mutation to G: 60-fold increase in catalytic efficiency for glucose phosphorylation. 45-fold increase in D-glucose affinity. No change in catalytic efficiency for D-allose phosphorylation.
- F145 (≠ L229) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.
Query Sequence
>CA265_RS23280 FitnessBrowser__Pedo557:CA265_RS23280
MNLNLLNNLTSNTSDKQFIQKHKLIKYLFNLGASSVSTLCEIMEMSTPSILKLLIGLIDE
GWVEKKGYGLSIGGRKPDLYRLKDKKILILCIDIELFHTKIAIIDNNYNFVLDVKTVLVP
ISKSRTDFFNILHSHLQDILKSAGIQREQFIGCSVGMPGLIDAEKGENYSYFLSDGENIP
LTAAFEKMLNMPVVIQNDVNGSSMAEFTHGMAKGKKNVLVLLMDWGVGLGIIMDGKLRQG
TCGFSGELGHMPFVENGALCYCGKHGCLETIASGNALSEMAKEGILSGKNSMLNKLSNEE
LERIEPALIIKAANKGDQYAIQLLSNVGTHMGKGIAVLIQLFNPELIILSGKIAGAKQYI
TLPMQQAINTYCMTQIREKTTIVSSELGENSRLLGYAATGIDQFLGAYIKKAKKLRK
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