SitesBLAST
Comparing WP_011321017.1 NCBI__GCF_000204075.1:WP_011321017.1 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)
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
37% identity, 89% coverage: 3:284/316 of query aligns to 2:277/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G10), T11 (= T12), K12 (= K13), G130 (≠ S135), T131 (= T136), G180 (= G185), G214 (= G221), S218 (= S225), G260 (≠ S267), V261 (= V268), E264 (≠ A271)
- binding beta-D-glucopyranose: G65 (= G69), P78 (≠ H82), N103 (= N108), D104 (= D109), L133 (≠ V138), G134 (= G139), E153 (= E158), H156 (= H161), E175 (= E180)
- binding zinc ion: H156 (= H161), C166 (= C171), C168 (= C173), C173 (= C178)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
37% identity, 89% coverage: 3:284/316 of query aligns to 2:277/312 of 3vgkB
2qm1B Crystal structure of glucokinase from enterococcus faecalis
32% identity, 99% coverage: 2:313/316 of query aligns to 6:319/325 of 2qm1B
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
30% identity, 79% coverage: 63:312/316 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)
30% identity, 79% coverage: 63:312/316 of query aligns to 64:300/306 of 5f7rA
- binding alpha-D-glucopyranose: G70 (= G69), N110 (≠ D109), N110 (≠ D109), S134 (≠ T133), V135 (≠ I134), G138 (= G137), L139 (≠ V138), G140 (= G139), E159 (= E158), H162 (= H161), E181 (= E180), E253 (≠ S267), W293 (≠ P305)
- binding zinc ion: H162 (= H161), C172 (= C171), C174 (= C173), C179 (= C178)
Sites not aligning to the query:
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
31% identity, 83% coverage: 56:316/316 of query aligns to 132:384/396 of 1z05A
1z6rA Crystal structure of mlc from escherichia coli (see paper)
31% identity, 73% coverage: 58:289/316 of query aligns to 120:341/382 of 1z6rA
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
31% identity, 73% coverage: 58:289/316 of query aligns to 144:365/406 of P50456
- H247 (= H161) binding Zn(2+)
- C257 (= C171) 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 (= C173) 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 (= C178) binding Zn(2+)
- R306 (≠ K230) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (= L234) 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.
- 136 F→A: Decreases association with PtsG EIIB domain.
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
32% identity, 89% coverage: 4:284/316 of query aligns to 3:262/298 of 3vovB
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
30% identity, 90% coverage: 5:288/316 of query aligns to 6:280/309 of 2yhwA
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
30% identity, 90% coverage: 5:288/316 of query aligns to 6:279/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G10), T13 (= T12), N14 (≠ K13), R16 (≠ A15), T140 (= T136), G189 (= G185), L216 (= L216), V261 (≠ S267)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G11), G71 (= G68), G72 (= G69), R73 (≠ P70), S84 (= S81), T85 (≠ H82), L87 (vs. gap), N112 (= N108), D113 (= D109), G139 (≠ S135), T140 (= T136), G141 (= G137), I142 (≠ V138), E162 (= E158), H165 (= H161), E184 (= E180)
- binding calcium ion: N112 (= N108), N115 (= N111), G144 (= G140), A161 (≠ G157)
- binding zinc ion: H165 (= H161), C175 (= C171), C177 (= C173), C182 (= C178)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
30% identity, 90% coverage: 5:288/316 of query aligns to 6:279/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G10), G12 (= G11), T13 (= T12), N14 (≠ K13), R16 (≠ A15), T140 (= T136), G189 (= G185), L216 (= L216), V261 (≠ S267)
- binding calcium ion: N112 (= N108), N115 (= N111), G144 (= G140), A161 (≠ G157)
- binding zinc ion: H165 (= H161), C175 (= C171), C177 (= C173), C182 (= C178)
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, 90% coverage: 5:288/316 of query aligns to 410:688/722 of Q9Y223
- D413 (= D8) binding Mg(2+)
- G416 (= G11) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (= T12) binding ADP
- N418 (≠ K13) binding ADP
- R420 (≠ A15) binding ADP
- I472 (≠ V65) 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 (= G69) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ P70) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ H82) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N108) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D109) 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 (= N111) 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 (≠ G116) 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 (= F120) 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 (= G137) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (= E158) binding an N-acyl-D-mannosamine
- H569 (= H161) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (= V164) 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 (= G168) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C171) binding Zn(2+)
- C581 (= C173) binding Zn(2+)
- C586 (= C178) binding Zn(2+)
- I587 (≠ V179) 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 (= E180) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (= A227) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A228) 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.
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, 90% coverage: 5:288/316 of query aligns to 410:688/722 of O35826
- D413 (= D8) 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.
- R420 (≠ A15) mutation to 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.
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
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
31% identity, 97% coverage: 4:309/316 of query aligns to 3:281/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (= K13), S129 (= S135), T130 (= T136), P195 (≠ G221), K196 (≠ Q222), S241 (= S267)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (= T75), G63 (= G76), A72 (≠ H82), L73 (≠ H83), N74 (≠ V84), N77 (vs. gap), N102 (= N108), D103 (= D109), S129 (= S135), T130 (= T136), H152 (≠ E158), H155 (= H161), E174 (= E180)
- binding zinc ion: H155 (= H161), C165 (= C171), C167 (= C173), C172 (= C178)
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
29% identity, 84% coverage: 4:268/316 of query aligns to 3:243/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
29% identity, 84% coverage: 4:268/316 of query aligns to 3:243/293 of 6jdhA
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
28% identity, 90% coverage: 5:288/316 of query aligns to 5:259/288 of 3eo3A
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
36% identity, 58% coverage: 4:185/316 of query aligns to 3:180/269 of 6jdcA
2aa4A Crystal structure of escherichia coli putative n-acetylmannosamine kinase, new york structural genomics consortium
35% identity, 84% coverage: 4:268/316 of query aligns to 3:243/289 of 2aa4A
Query Sequence
>WP_011321017.1 NCBI__GCF_000204075.1:WP_011321017.1
MKLTLALDFGGTKLAAGLVNADSRKWLRYERRFSPINGDANTDLEIMRSLIHSLLQGETP
TAIGVSFGGPVDATTGTVRLSHHVPGWENIPLKSLLEKEFGVPTSVDNDANVAALGEQHF
GAGQGYDSLFYITISTGVGGGWILNGKPWRGAVGMAGEIGHIVVEPAGPICLCGKRGCVE
RLASGPYMAQNAKDILENQPEREDGQILRNLVGNNLNLLTGQLISEAATKGDNLAQAVLQ
KSAWALGVGIGNVANLINPQRFILGGSVTKAGEIWWTVLQETARFTALPEVPLEIVPAVL
ADDAPLWGAVALAQNL
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