SitesBLAST
Comparing WP_012755543.1 NCBI__GCF_000023185.1:WP_012755543.1 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, 95% coverage: 4:309/321 of query aligns to 2:309/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (= G11), T11 (= T13), K12 (≠ Q14), G130 (≠ S138), T131 (= T139), G180 (= G188), G214 (≠ S216), S218 (≠ F220), G260 (= G262), V261 (≠ L263), E264 (= E266)
- binding beta-D-glucopyranose: G65 (= G72), P78 (= P85), N103 (= N111), D104 (= D112), L133 (≠ I141), G134 (= G142), E153 (≠ H161), H156 (= H164), E175 (= E183)
- binding zinc ion: H156 (= H164), C166 (= C174), C168 (= C176), C173 (= C181)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
37% identity, 95% coverage: 4:309/321 of query aligns to 2:309/312 of 3vgkB
2qm1B Crystal structure of glucokinase from enterococcus faecalis
31% identity, 98% coverage: 1:314/321 of query aligns to 4:324/325 of 2qm1B
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
31% identity, 94% coverage: 5:306/321 of query aligns to 3:282/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (≠ Q14), S129 (= S138), T130 (= T139), P195 (≠ S216), K196 (≠ R217), S241 (vs. gap)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ P71), G63 (= G72), A72 (= A81), L73 (≠ S82), N74 (= N83), N77 (≠ T86), N102 (= N111), D103 (= D112), S129 (= S138), T130 (= T139), H152 (= H161), H155 (= H164), E174 (= E183)
- binding zinc ion: H155 (= H164), C165 (= C174), C167 (= C176), C172 (= C181)
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
35% identity, 96% coverage: 6:314/321 of query aligns to 4:296/298 of 3vovB
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
30% identity, 77% coverage: 63:308/321 of query aligns to 136:380/396 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, 91% coverage: 17:308/321 of query aligns to 106:389/406 of P50456
- F136 (≠ T51) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H164) binding Zn(2+)
- C257 (= C174) 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 (= C176) 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 (= C181) binding Zn(2+)
- R306 (≠ N225) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (= L229) 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)
29% identity, 77% coverage: 63:308/321 of query aligns to 122:365/382 of 1z6rA
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
30% identity, 94% coverage: 5:306/321 of query aligns to 3:283/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
30% identity, 94% coverage: 5:306/321 of query aligns to 3:283/293 of 6jdhA
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
32% identity, 94% coverage: 5:306/321 of query aligns to 3:262/269 of 6jdcA
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
29% identity, 87% coverage: 5:283/321 of query aligns to 5:280/309 of 2yhwA
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
27% identity, 81% coverage: 6:265/321 of query aligns to 85:341/396 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
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
28% identity, 87% coverage: 5:283/321 of query aligns to 5:279/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (= G11), T13 (= T13), N14 (≠ Q14), R16 (= R16), T140 (= T139), G189 (= G188), L216 (≠ R217), V261 (≠ G262)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (= G12), G71 (≠ P71), G72 (= G72), R73 (≠ P73), S84 (≠ N83), T85 (≠ I84), L87 (≠ T86), N112 (= N111), D113 (= D112), G139 (≠ S138), T140 (= T139), G141 (= G140), I142 (= I141), E162 (≠ H161), H165 (= H164), E184 (= E183)
- binding calcium ion: N112 (= N111), N115 (≠ I114), G144 (= G143), A161 (= A160)
- binding zinc ion: H165 (= H164), C175 (= C174), C177 (= C176), C182 (= C181)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
28% identity, 87% coverage: 5:283/321 of query aligns to 5:279/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (= G11), G12 (= G12), T13 (= T13), N14 (≠ Q14), R16 (= R16), T140 (= T139), G189 (= G188), L216 (≠ R217), V261 (≠ G262)
- binding calcium ion: N112 (= N111), N115 (≠ I114), G144 (= G143), A161 (= A160)
- binding zinc ion: H165 (= H164), C175 (= C174), C177 (= C176), C182 (= C181)
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
26% identity, 81% coverage: 6:265/321 of query aligns to 4:257/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ D9), E10 (≠ G12), G70 (= G72), N110 (≠ D112), N110 (≠ D112), S134 (≠ T136), V135 (= V137), G138 (= G140), L139 (≠ I141), G140 (= G142), E159 (≠ H161), H162 (= H164), E181 (= E183), E253 (≠ G261)
- binding zinc ion: H162 (= H164), C172 (= C174), C174 (= C176), C179 (= C181)
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)
28% identity, 87% coverage: 5:283/321 of query aligns to 409:688/722 of Q9Y223
- D413 (= D9) binding Mg(2+)
- G416 (= G12) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (= T13) binding ADP
- N418 (≠ Q14) binding ADP
- R420 (= R16) binding ADP
- I472 (≠ V68) 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 (= G72) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ P73) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ I84) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N111) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D112) 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 (≠ I114) 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 (≠ G119) 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 (= F123) 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 (= G140) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (≠ H161) binding an N-acyl-D-mannosamine
- H569 (= H164) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (= V167) 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 (= G171) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C174) binding Zn(2+)
- C581 (= C176) binding Zn(2+)
- C586 (= C181) binding Zn(2+)
- I587 (≠ F182) 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 (= E183) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (= A222) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A223) 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.
2aa4A Crystal structure of escherichia coli putative n-acetylmannosamine kinase, new york structural genomics consortium
34% identity, 86% coverage: 6:280/321 of query aligns to 4:259/289 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)
34% identity, 86% coverage: 6:280/321 of query aligns to 4:259/291 of P45425
- L84 (≠ V91) mutation to P: 12-fold increase in catalytic efficiency for glucose phosphorylation. 2-fold decrease in catalytic efficiency for N-acetylmannosamine phosphorylation.
- V138 (= V146) mutation to M: 6-fold increase in catalytic efficiency for glucose phosphorylation. No change in catalytic efficiency for N-acetylmannosamine phosphorylation.
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, 82% coverage: 5:267/321 of query aligns to 409:675/722 of O35826
- D413 (= D9) 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 (= R16) 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
Query Sequence
>WP_012755543.1 NCBI__GCF_000023185.1:WP_012755543.1
MQQVAIGIDLGGTQVRAALVDEQGRILARAAEPTDALAGPDRVLAQICGLTDGLLAASNP
ASVVGVGVSAPGPLDTVAGVASNIPTLSGFVDFPLKAELQKRFPFPVDLENDAIAAAIGE
WQFGAGTGLDNLVYVTVSTGIGGGVVSDGRVVRGRKGMAAHVGHMSVVPNGELCPCGNRG
CFEAYGSGTAFARRAQIRAVESSATTIGSDGGAIDSRSVFAAARNGDRLANQLIDEEAEI
LGRGFTSLIHIFSPDIIVMGGGLSHEFDRLQPGIQGYITQWAMPAFKDVRVMLAALDQNS
GLVGAAALAFLTGKVPAVDQI
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