SitesBLAST
Comparing WP_009763228.1 NCBI__GCF_000262405.1:WP_009763228.1 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)
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
28% identity, 75% coverage: 28:341/417 of query aligns to 11:334/396 of 1z05A
5f7qE Rok repressor lmo0178 from listeria monocytogenes bound to operator (see paper)
26% identity, 78% coverage: 16:339/417 of query aligns to 7:336/396 of 5f7qE
- binding zinc ion: H243 (= H253), C253 (= C263), C255 (= C265), C260 (= C270)
- binding : K8 (≠ P17), K12 (≠ R21), N15 (= N24), T32 (≠ M41), S43 (≠ Q52), T44 (≠ A53), T67 (vs. gap), G68 (vs. gap), G68 (vs. gap), G69 (= G76), G69 (= G76), R70 (= R77), R70 (= R77), R71 (≠ G78), A72 (≠ L79), K73 (≠ P80)
Sites not aligning to the query:
P50456 DNA-binding transcriptional repressor Mlc; Making large colonies protein; Membrane linked control from Escherichia coli (strain K12) (see 4 papers)
25% identity, 77% coverage: 18:339/417 of query aligns to 11:342/406 of P50456
- R52 (≠ E59) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ M92) mutation to R: Can be bound and inactivated by MtfA.
- F136 (≠ Q142) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H253) binding Zn(2+)
- C257 (= C263) 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 (= C265) 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 (= C270) binding Zn(2+)
- R306 (≠ E303) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ V307) mutation to G: Forms dimers but not tetramers; when associated with G-306.
5f7rA Rok repressor lmo0178 from listeria monocytogenes bound to inducer (see paper)
27% identity, 60% coverage: 91:339/417 of query aligns to 1:252/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ E97), E10 (≠ A100), G70 (= G161), N110 (≠ D201), N110 (≠ D201), S134 (≠ Y225), V135 (≠ F226), G138 (= G229), L139 (= L230), G140 (= G231), E159 (= E250), H162 (= H253), E181 (= E272)
- binding zinc ion: H162 (= H253), C172 (= C263), C174 (= C265), C179 (= C270)
Sites not aligning to the query:
1z6rA Crystal structure of mlc from escherichia coli (see paper)
24% identity, 76% coverage: 21:339/417 of query aligns to 3:318/382 of 1z6rA
2qm1B Crystal structure of glucokinase from enterococcus faecalis
28% identity, 71% coverage: 95:390/417 of query aligns to 10:320/325 of 2qm1B
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
28% identity, 71% coverage: 91:388/417 of query aligns to 1:308/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G9 (≠ A99), T11 (≠ D101), K12 (≠ H102), G130 (= G227), T131 (≠ Q228), G180 (≠ F277), G214 (≠ Y294), S218 (≠ E298), G260 (= G344), V261 (≠ L345), E264 (≠ D348)
- binding beta-D-glucopyranose: G65 (= G161), P78 (≠ T174), N103 (= N200), D104 (= D201), L133 (= L230), G134 (= G231), E153 (= E250), H156 (= H253), E175 (= E272)
- binding zinc ion: H156 (= H253), C166 (= C263), C168 (= C265), C173 (= C270)
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
28% identity, 71% coverage: 91:388/417 of query aligns to 1:308/312 of 3vgkB
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)
29% identity, 49% coverage: 95:298/417 of query aligns to 411:612/722 of Q9Y223
- D413 (≠ E97) binding Mg(2+); to Y: in THC12; likely pathogenic; dbSNP:rs1280775456
- G416 (≠ A100) binding an N-acyl-D-mannosamine 6-phosphate
- T417 (≠ D101) binding ADP; to M: in THC12; likely pathogenic; dbSNP:rs1554659711
- N418 (≠ H102) binding ADP
- R420 (≠ S104) binding ADP; to Q: in THC12; likely pathogenic; dbSNP:rs780092539
- I472 (≠ V157) 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 (≠ P160) to F: in THC12; likely pathogenic; requires 2 nucleotide substitutions
- G476 (= G161) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ P162) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- V485 (≠ T169) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells; requires 2 nucleotide substitutions
- L486 (≠ S170) to P: in THC12; uncertain significance; dbSNP:rs774867424
- T489 (≠ P173) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N200) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (= D201) 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 (≠ T203) to S: in NM and THC12; likely pathogenic; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs1554658910
- A524 (≠ G208) 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 (≠ H212) to C: in NM; decreased N-acylmannosamine kinase activity; dbSNP:rs986773986
- T544 (≠ Q228) to R: in THC12; uncertain significance; reduced protein abundance in homozygous patient cells
- G545 (= G229) binding an N-acyl-D-mannosamine 6-phosphate
- C563 (≠ N247) to Y: in THC12; likely pathogenic; results in severely decreased cell surface sialylation
- E566 (= E250) binding an N-acyl-D-mannosamine
- H569 (= H253) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (= V256) 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 (= G260) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C263) binding Zn(2+)
- C581 (= C265) binding Zn(2+)
- C586 (= C270) binding Zn(2+)
- I587 (≠ L271) to T: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs748949603
- E588 (= E272) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
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
- 420:722 natural variant: Missing (in THC12; likely pathogenic)
- 630 A → T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- 631 A → V: in NM; does not affect homohexamers formation; dbSNP:rs62541771
- 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
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
27% identity, 59% coverage: 96:343/417 of query aligns to 8:264/308 of 2yi1A
- binding adenosine-5'-diphosphate: G11 (≠ A99), T13 (≠ D101), N14 (≠ H102), R16 (≠ S104), T140 (≠ Q228), G189 (≠ F277), L216 (≠ I289), V261 (= V340)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G12 (≠ A100), G71 (≠ P160), G72 (= G161), R73 (≠ P162), S84 (≠ G172), T85 (≠ P173), L87 (≠ T175), N112 (= N200), D113 (= D201), G139 (= G227), T140 (≠ Q228), G141 (= G229), I142 (≠ L230), E162 (= E250), H165 (= H253), E184 (= E272)
- binding calcium ion: N112 (= N200), N115 (≠ T203), G144 (≠ L232), A161 (≠ G249)
- binding zinc ion: H165 (= H253), C175 (= C263), C177 (= C265), C182 (= C270)
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
27% identity, 59% coverage: 96:343/417 of query aligns to 8:264/308 of 2yhyA
- binding adenosine-5'-diphosphate: G11 (≠ A99), G12 (≠ A100), T13 (≠ D101), N14 (≠ H102), R16 (≠ S104), T140 (≠ Q228), G189 (≠ F277), L216 (≠ I289), V261 (= V340)
- binding calcium ion: N112 (= N200), N115 (≠ T203), G144 (≠ L232), A161 (≠ G249)
- binding zinc ion: H165 (= H253), C175 (= C263), C177 (= C265), C182 (= C270)
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
30% identity, 43% coverage: 96:276/417 of query aligns to 8:188/309 of 2yhwA
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
27% identity, 70% coverage: 96:386/417 of query aligns to 6:283/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
27% identity, 70% coverage: 96:386/417 of query aligns to 6:283/293 of 6jdhA
6jdbA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac-6p and adp from haemophilus influenzae
28% identity, 58% coverage: 118:357/417 of query aligns to 2:260/290 of 6jdbA
- binding adenosine-5'-diphosphate: K12 (≠ E128), S129 (≠ G227), T130 (≠ Q228), P195 (≠ Y294), K196 (≠ A295), S241 (≠ V340)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: T62 (≠ P160), G63 (= G161), A72 (≠ S170), L73 (≠ V171), N74 (≠ G172), N77 (≠ T175), N102 (= N200), D103 (= D201), S129 (≠ G227), T130 (≠ Q228), H152 (≠ E250), H155 (= H253), E174 (= E272)
- binding zinc ion: H155 (= H253), C165 (= C263), C167 (= C265), C172 (= C270)
P32718 D-allose kinase; Allokinase; EC 2.7.1.55 from Escherichia coli (strain K12) (see paper)
30% identity, 50% coverage: 182:388/417 of query aligns to 96:295/309 of P32718
- F145 (≠ L232) mutation to L: 10-fold increase in catalytic efficiency for glucose phosphorylation. Slight increase in catalytic efficiency for D-allose phosphorylation.
Sites not aligning to the query:
- 73 A→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.
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, 49% coverage: 95:298/417 of query aligns to 411:612/722 of O35826
- D413 (≠ E97) 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 (≠ S104) 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
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)
29% identity, 49% coverage: 95:298/417 of query aligns to 411:612/722 of Q91WG8
- C563 (≠ N247) 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.
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
35% identity, 48% coverage: 155:354/417 of query aligns to 61:262/298 of 3vovB
6jdcA Crystal structure of n-acetyl mannosmaine kinase in complex with mannac from haemophilus influenzae
28% identity, 50% coverage: 151:357/417 of query aligns to 54:240/269 of 6jdcA
Query Sequence
>WP_009763228.1 NCBI__GCF_000262405.1:WP_009763228.1
MPRKAKPGTPSTIGSNPERNRSHNRRVVLDVVRQLGPVGRMEISRHAHLSTQAVSNIVED
LVADGLLIRTGRLRAGRGLPPIQFDVNPNGGMTAGIEIAADHISTLLVDIGGRVRAQRSI
PLPQNDPETVLPVIKAEIEAAQAQLEPPVPQLLGVGVVMPGPFNVEGMTSVGPTTLSGWF
DFDAVARIGDMLGAPVTLENDATAAAVGERLHGVARNLKNFCLIYFGQGLGLGIMIDGRP
YRGANGNAGEIGHVRVAKGGRLCSCGQHGCLEAYASFHSLAQKLAAAGIHGIDYAELERL
HREKHPVVLAWIEEAAGYLAPQVAMLENLFDPEAIVLGGVLPPGLLEDLVEAMQPLPLSV
ARRRNRSEARLIHGRTGGLTAALGAAALPLLETMTPRLDTAHAAEREHTNEETSLAG
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