SitesBLAST
Comparing WP_004119317.1 NCBI__GCF_000359745.1:WP_004119317.1 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)
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
31% identity, 99% coverage: 2:378/381 of query aligns to 5:392/396 of 5f7qE
- binding zinc ion: H243 (= H240), C253 (= C250), C255 (= C252), C260 (= C257)
- binding : K5 (≠ R2), K8 (≠ P5), K12 (≠ R9), N15 (= N12), T32 (≠ A29), S43 (≠ A40), T44 (≠ A41), T67 (≠ A64), G68 (≠ T65), G68 (≠ T65), G69 (= G66), G69 (= G66), R70 (= R67), R70 (= R67), R71 (= R68), A72 (≠ P69), K73 (≠ V70)
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
31% identity, 78% coverage: 80:376/381 of query aligns to 2:306/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (= K85), E10 (≠ H88), G70 (= G149), N110 (≠ D188), N110 (≠ D188), S134 (≠ A212), V135 (= V213), G138 (= G216), L139 (≠ V217), G140 (= G218), E159 (≠ K237), H162 (= H240), E181 (≠ Q259), E253 (= E327), W293 (= W363)
- binding zinc ion: H162 (= H240), C172 (= C250), C174 (= C252), C179 (= C257)
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
25% identity, 97% coverage: 9:377/381 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)
25% identity, 90% coverage: 3:345/381 of query aligns to 8:361/406 of P50456
- R52 (≠ T47) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ L80) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ L130) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H240) binding Zn(2+)
- C257 (= C250) 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 (= C252) 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 (= C257) binding Zn(2+)
- R306 (≠ T290) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ D294) mutation to G: Forms dimers but not tetramers; when associated with G-306.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
25% identity, 87% coverage: 16:345/381 of query aligns to 10:337/382 of 1z6rA
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
27% identity, 77% coverage: 80:373/381 of query aligns to 2:295/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (≠ R87), T11 (≠ D89), K12 (≠ S90), G130 (= G214), T131 (= T215), G180 (≠ E264), G214 (vs. gap), S218 (vs. gap), G260 (≠ E327), V261 (≠ A328), E264 (≠ F331)
- binding beta-D-glucopyranose: G65 (= G149), P78 (= P162), N103 (≠ D187), D104 (= D188), L133 (≠ V217), G134 (= G218), E153 (≠ K237), H156 (= H240), E175 (≠ Q259)
- binding zinc ion: H156 (= H240), C166 (= C250), C168 (= C252), C173 (= C257)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
27% identity, 77% coverage: 80:373/381 of query aligns to 2:295/312 of 3vgkB
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
29% identity, 56% coverage: 131:344/381 of query aligns to 54:279/309 of 2yhwA
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
29% identity, 56% coverage: 131:344/381 of query aligns to 54:278/308 of 2yi1A
- binding adenosine-5'-diphosphate: T140 (= T215), G189 (≠ E264), L216 (vs. gap), V261 (≠ E327)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (≠ P148), G72 (= G149), R73 (≠ E150), S84 (= S161), T85 (≠ P162), L87 (≠ F164), N112 (≠ D187), D113 (= D188), G139 (= G214), T140 (= T215), G141 (= G216), I142 (≠ V217), E162 (≠ K237), H165 (= H240), E184 (≠ Q259)
- binding calcium ion: N112 (≠ D187), N115 (≠ S190), G144 (≠ S219), A161 (≠ G236)
- binding zinc ion: H165 (= H240), C175 (= C250), C177 (= C252), C182 (= C257)
Sites not aligning to the query:
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
29% identity, 56% coverage: 131:344/381 of query aligns to 54:278/308 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 26 papers)
28% identity, 60% coverage: 115:344/381 of query aligns to 439:687/722 of Q9Y223
- I472 (≠ V145) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity corresponding to less than 10% of wild-type activity
- G475 (≠ P148) to F: in THC12; likely pathogenic; requires 2 nucleotide substitutions
- G476 (= G149) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ E150) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- V485 (≠ C158) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells; requires 2 nucleotide substitutions
- L486 (≠ I159) to P: in THC12; uncertain significance; dbSNP:rs774867424
- T489 (≠ P162) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (≠ D187) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D188) 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 (≠ S190) to S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910
- A524 (= A195) 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 (= F199) to C: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986
- T544 (= T215) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells
- G545 (= G216) binding an N-acyl-D-mannosamine 6-phosphate
- C563 (≠ L234) to Y: in THC12; likely pathogenic; results in severely decreased cell surface sialylation
- E566 (≠ K237) binding an N-acyl-D-mannosamine
- H569 (= H240) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (≠ T243) to L: in NM and THC12; likely pathogenic; mildly decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity corresponding to less than 10% of wild-type activity; does not affect homohexamers formation; dbSNP:rs121908632
- G576 (= G247) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C250) binding Zn(2+)
- C581 (= C252) binding Zn(2+)
- C586 (= C257) binding Zn(2+)
- I587 (≠ L258) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603
- E588 (≠ Q259) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (vs. gap) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (vs. gap) to V: in NM; does not affect homohexamers formation; dbSNP:rs62541771
Sites not aligning to the query:
- 13 C → S: in NM; decreased UDP-N-acetylglucosamine 2-epimerase 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; impaired homohexamers formation
- 157 H → Y: in THC12; likely pathogenic
- 176 D → V: in NM; decreased UDP-N-acetylglucosamine 2-epimerase 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; impaired homohexamers formation; dbSNP:rs539332585
- 200 I → F: in NM; uncertain significance; 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; requires 2 nucleotide substitutions; dbSNP:rs121908633
- 307 binding UDP
- 321 binding UDP
- 331 V → A: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; no effect on N-acylmannosamine kinase activity; impaired homohexamers formation
- 378 D → Y: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; impaired homohexamers formation; dbSNP:rs199877522
- 413 binding Mg(2+); D → Y: in THC12; likely pathogenic; dbSNP:rs1280775456
- 416 binding an N-acyl-D-mannosamine 6-phosphate
- 417 binding ADP; T → M: in THC12; likely pathogenic; dbSNP:rs1554659711
- 418 binding ADP
- 420 binding ADP; R → Q: in THC12; likely pathogenic; dbSNP:rs780092539
- 420:722 natural variant: Missing (in THC12; likely pathogenic)
- 704 P → R: in THC12; likely pathogenic; the orthologous mutation in mouse embryos results in cerebrospinal hemorrhages and defective angiogenesis; results in loss of cell surface sialylation
- 708 G → S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; severely decreased N-acylmannosamine kinase activity; dbSNP:rs1554657922
- 712 M → T: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs28937594
Q91WG8 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 Mus musculus (Mouse) (see paper)
27% identity, 60% coverage: 115:344/381 of query aligns to 439:687/722 of Q91WG8
- C563 (≠ L234) mutation to Y: Loss-of-function mutant resulting in impaired sialic acid biosynthesis.
Sites not aligning to the query:
- 704 P→R: Homozygous embryos exhibit cerebrospinal hemorrhages and defective angiogenesis in the diencephalon at 11 dpc, and become non-viable between 11.5 and 12.5 dpc. Loss-of-function mutant resulting in impaired sialic acid biosynthesis.
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)
28% identity, 56% coverage: 115:326/381 of query aligns to 439:669/722 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.
2qm1B Crystal structure of glucokinase from enterococcus faecalis
27% identity, 61% coverage: 141:373/381 of query aligns to 69:321/325 of 2qm1B
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
29% identity, 45% coverage: 175:344/381 of query aligns to 75:258/288 of 3eo3A
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
31% identity, 46% coverage: 143:319/381 of query aligns to 61:236/298 of 3vovB
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
27% identity, 63% coverage: 93:333/381 of query aligns to 3:254/269 of 6jdcA
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
27% identity, 61% coverage: 93:326/381 of query aligns to 3:240/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (≠ P102), S129 (≠ G214), T130 (= T215), P195 (≠ A277), K196 (= K278)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ V143), G63 (= G144), A72 (= A153), L73 (≠ V154), N74 (≠ S161), N77 (≠ F164), N102 (≠ D187), D103 (= D188), S129 (≠ G214), T130 (= T215), H152 (≠ K237), H155 (= H240), E174 (≠ Q259)
- binding zinc ion: H155 (= H240), C165 (= C250), C167 (= C252), C172 (= C257)
Sites not aligning to the query:
7p7wBBB Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
24% identity, 67% coverage: 76:331/381 of query aligns to 1:263/306 of 7p7wBBB
7p9pAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
24% identity, 67% coverage: 78:331/381 of query aligns to 1:261/304 of 7p9pAAA
- binding phosphoaminophosphonic acid-adenylate ester: G11 (≠ H88), T12 (≠ D89), K13 (≠ S90), G133 (= G214), T134 (= T215), G194 (≠ E264), E198 (≠ I268), A211 (≠ R281), G256 (= G326), G257 (≠ E327), N260 (≠ Q330)
- binding zinc ion: H159 (= H240), C180 (= C250), C182 (= C252), C187 (= C257), E213 (= E283), H217 (≠ A287)
Query Sequence
>WP_004119317.1 NCBI__GCF_000359745.1:WP_004119317.1
MRGNPSTSRALNRRLILNLLRNRGPMPRAEIATVTGLSPAAVTFVVTELIEEGLVVEGKA
QPGATGRRPVPVDINYGGHLAVGFKLRHDSIDCVLTDLATTPIASFDMPVPDTRPETMVE
AIATAIPKLLADAGRTGSPVMGVGVSIPGEVDAVKGICIQSPRFGWRNLAFPELLREQVH
IPVWIDDDISAFTVAQRLFGAGRNYSNFATIAVGTGVGSSLVMDGEIYHGSHGLAGKLGH
IITVPGGRLCECGRRGCLQAHTAEAAMIDEWGLRRGAKATRDEYAAAVETGDADALEIMA
QAGELIGRHLADLVNLFDPEVLIAGGEAMQFGDAILEPIRRSMAKYVFLNTPELLPDWVP
GSWARGAAALATQHFFDLDVE
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