SitesBLAST
Comparing SMa2303 FitnessBrowser__Smeli:SMa2303 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)
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
29% identity, 93% coverage: 19:399/408 of query aligns to 1:390/396 of 5f7qE
- binding zinc ion: H243 (= H261), C253 (= C271), C255 (= C273), C260 (= C278)
- binding : K5 (= K23), K8 (≠ Q26), K12 (≠ R30), N15 (= N33), T32 (≠ A50), S43 (≠ A61), T44 (≠ A62), T67 (≠ A85), G68 (≠ Q86), G68 (≠ Q86), G69 (= G87), G69 (= G87), R70 (= R88), R70 (= R88), R71 (= R89), A72 (≠ P90), K73 (≠ I91)
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
29% identity, 74% coverage: 100:399/408 of query aligns to 1:306/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (= K106), E10 (≠ A109), G70 (= G170), N110 (≠ D209), N110 (≠ D209), S134 (≠ A233), V135 (≠ I234), G138 (= G237), L139 (≠ V238), G140 (≠ A239), E159 (≠ K258), H162 (= H261), E181 (≠ M280), E253 (= E350), W293 (= W386)
- binding zinc ion: H162 (= H261), C172 (= C271), C174 (= C273), C179 (= C278)
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
26% identity, 91% coverage: 30:400/408 of query aligns to 4:386/396 of 1z05A
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
24% identity, 85% coverage: 24:371/408 of query aligns to 8:364/406 of P50456
- R52 (≠ S68) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ V101) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ V151) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H261) binding Zn(2+)
- C257 (= C271) 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 (= C273) 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 (= C278) binding Zn(2+)
- R306 (≠ A313) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ A317) mutation to G: Forms dimers but not tetramers; when associated with G-306.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
23% identity, 82% coverage: 37:371/408 of query aligns to 10:340/382 of 1z6rA
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
28% identity, 66% coverage: 100:369/408 of query aligns to 1:279/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (≠ M108), T11 (≠ G110), K12 (≠ S111), G130 (= G235), T131 (≠ V236), G180 (≠ E285), G214 (vs. gap), S218 (vs. gap), G260 (≠ E350), V261 (≠ A351), E264 (≠ Y354)
- binding beta-D-glucopyranose: G65 (= G170), P78 (≠ N183), N103 (≠ D208), D104 (= D209), L133 (≠ V238), G134 (≠ A239), E153 (≠ K258), H156 (= H261), E175 (≠ M280)
- binding zinc ion: H156 (= H261), C166 (= C271), C168 (= C273), C173 (= C278)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
28% identity, 66% coverage: 100:369/408 of query aligns to 1:279/312 of 3vgkB
2qm1B Crystal structure of glucokinase from enterococcus faecalis
27% identity, 59% coverage: 134:373/408 of query aligns to 41:294/325 of 2qm1B
4db3A 1.95 angstrom resolution crystal structure of n-acetyl-d-glucosamine kinase from vibrio vulnificus.
27% identity, 60% coverage: 104:349/408 of query aligns to 12:261/311 of 4db3A
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)
25% identity, 53% coverage: 135:349/408 of query aligns to 438:669/722 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.
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
25% identity, 47% coverage: 159:349/408 of query aligns to 61:261/309 of 2yhwA
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
24% identity, 47% coverage: 159:349/408 of query aligns to 61:260/308 of 2yi1A
- binding adenosine-5'-diphosphate: T140 (≠ V236), G189 (≠ E285), L216 (≠ A305)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (≠ P169), G72 (= G170), R73 (≠ V171), S84 (= S182), T85 (≠ N183), L87 (≠ Y185), N112 (≠ D208), D113 (= D209), G139 (= G235), T140 (≠ V236), G141 (= G237), I142 (≠ V238), E162 (≠ K258), H165 (= H261), E184 (≠ M280)
- binding calcium ion: N112 (≠ D208), N115 (= N211), G144 (≠ C240), A161 (≠ G257)
- binding zinc ion: H165 (= H261), C175 (= C271), C177 (= C273), C182 (= C278)
Sites not aligning to the query:
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
24% identity, 47% coverage: 159:349/408 of query aligns to 61:260/308 of 2yhyA
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 18 papers)
24% identity, 47% coverage: 159:349/408 of query aligns to 465:669/722 of Q9Y223
- I472 (= I166) 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 (= G170) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ V171) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ N183) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (≠ D208) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D209) 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 (= N211) 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 (= A216) 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 (= F220) 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 (= G237) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (≠ K258) binding an N-acyl-D-mannosamine
- H569 (= H261) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (≠ H264) 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 (= G268) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C271) binding Zn(2+)
- C581 (= C273) binding Zn(2+)
- C586 (= C278) binding Zn(2+)
- I587 (≠ L279) 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 (≠ M280) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (= A310) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (≠ I311) 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
- 413 binding Mg(2+)
- 416 binding an N-acyl-D-mannosamine 6-phosphate
- 417 binding ADP
- 418 binding ADP
- 420 binding ADP
- 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.
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
33% identity, 44% coverage: 164:342/408 of query aligns to 61:236/298 of 3vovB
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
26% identity, 62% coverage: 97:349/408 of query aligns to 1:258/306 of 7p7wBBB
Sites not aligning to the query:
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 62% coverage: 99:349/408 of query aligns to 1:256/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (≠ A109), T12 (≠ G110), K13 (≠ S111), G133 (= G235), T134 (≠ V236), G194 (≠ E285), E198 (≠ L289), A211 (≠ R304), G256 (= G349)
- binding zinc ion: H159 (= H261), C180 (= C271), C182 (= C273), C187 (= C278), E213 (= E306), H217 (≠ A310)
Sites not aligning to the query:
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
27% identity, 60% coverage: 104:349/408 of query aligns to 5:255/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (= P169), G67 (= G170), S79 (= S182), N105 (≠ D208), D106 (= D209), G132 (= G235), T133 (≠ V236), G134 (= G237), V135 (= V238), G136 (≠ A239), E155 (≠ K258), H158 (= H261), D188 (≠ M280)
- binding zinc ion: H158 (= H261), C179 (= C271), C181 (= C273), C186 (= C278), E212 (= E306), H216 (≠ A310)
Q93LQ8 Beta-glucoside kinase; EC 2.7.1.85 from Klebsiella pneumoniae (see paper)
28% identity, 56% coverage: 124:352/408 of query aligns to 25:245/297 of Q93LQ8
- D103 (= D209) mutation to G: Loss of catalytic activity.
- G131 (= G237) mutation to A: Loss of catalytic activity.
- G133 (≠ A239) mutation to A: Loss of catalytic activity.
Sites not aligning to the query:
- 7 D→G: Loss of catalytic activity.
- 9 G→A: Loss of catalytic activity.
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
26% identity, 39% coverage: 191:349/408 of query aligns to 74:240/288 of 3eo3A
Query Sequence
>SMa2303 FitnessBrowser__Smeli:SMa2303
MHSRENEAIFNLQNKIMSDVRTKGDQSTTRAMNRRLILNLLRREGAKSRAEIAAATGLSP
AAVTFVVSDLIEEGLLIEGQSVAGAQGRRPIPVAIDYAGGVALGFKLMAGSVECVVTDLE
TTPLASLRLPLPAHDPDTIAEALAAAAPKLVALANRPAARLAGIGIAMPGVIDNQRAVCI
RSNRYGWDNVPLGDLVASRIGVPVWLEDDTNAYAIAQQLFGLGRHYKTMGVLAIGVGVAC
SLVLDGKLYRGAHGAAGKFGHFPHMEGGRPCECGKRGCLMSYFSEPAMLQTWHERSGRPE
TDGRAEMVAAIAAGDKAAHSVMREAGETLGRHLAGLMNVIDPEVIVVGGEAVAYGDALFG
PLRATLERFAFRQAPPVLLDWEDDSWARGAAALVTQKLFDFETTAGNA
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