SitesBLAST
Comparing WP_015945030.1 NCBI__GCF_000021925.1:WP_015945030.1 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)
26% identity, 93% coverage: 22:400/406 of query aligns to 19:389/396 of 5f7qE
- binding zinc ion: H243 (= H248), C253 (= C258), C255 (= C260), C260 (= C265)
- binding : T32 (≠ S35), S43 (≠ T46), T44 (= T47), T67 (= T70), G68 (= G71), G68 (= G71), G69 (= G72), G69 (= G72), R70 (= R73), R70 (= R73), R71 (≠ K74), A72 (≠ P75), K73 (≠ V76)
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)
23% identity, 85% coverage: 19:365/406 of query aligns to 18:362/406 of P50456
- R52 (≠ L53) mutation to H: Shows increased expression and forms larger colonies.
- H86 (≠ Y86) mutation to R: Can be bound and inactivated by MtfA.
- F136 (vs. gap) mutation to A: Decreases association with PtsG EIIB domain.
- H247 (= H248) binding Zn(2+)
- C257 (= C258) 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 (= C260) 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 (= C265) binding Zn(2+)
- R306 (≠ E309) mutation to G: Forms dimers but not tetramers; when associated with G-310.
- L310 (≠ I313) 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)
24% identity, 78% coverage: 86:400/406 of query aligns to 2:305/306 of 5f7rA
- binding alpha-D-glucopyranose: K7 (≠ D91), E10 (≠ R94), G70 (= G154), N110 (≠ G196), N110 (≠ G196), S134 (≠ N220), V135 (≠ C221), G138 (= G224), L139 (≠ I225), G140 (≠ R226), E159 (≠ T245), H162 (= H248), E181 (= E267), E253 (≠ P346), W293 (≠ S388)
- binding zinc ion: H162 (= H248), C172 (= C258), C174 (= C260), C179 (= C265)
2yhwA High-resolution crystal structures of n-acetylmannosamine kinase: insights about substrate specificity, activity and inhibitor modelling. (see paper)
32% identity, 51% coverage: 145:350/406 of query aligns to 63:266/309 of 2yhwA
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)
32% identity, 51% coverage: 145:350/406 of query aligns to 467:674/722 of Q9Y223
- I472 (= I150) 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 (= G154) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- R477 (≠ P155) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- T489 (≠ E167) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- N516 (= N195) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- D517 (≠ G196) 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 (= N198) 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 (= A203) 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 (≠ Y207) 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 (= G224) binding an N-acyl-D-mannosamine 6-phosphate
- E566 (≠ T245) binding an N-acyl-D-mannosamine
- H569 (= H248) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate; binding Zn(2+)
- V572 (≠ I251) 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 (= G255) to E: in NM; decreased UDP-N-acetylglucosamine 2-epimerase activity; decreased N-acylmannosamine kinase activity; dbSNP:rs121908625
- C579 (= C258) binding Zn(2+)
- C581 (= C260) binding Zn(2+)
- C586 (= C265) binding Zn(2+)
- I587 (≠ V266) 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 (= E267) binding an N-acyl-D-mannosamine; binding an N-acyl-D-mannosamine 6-phosphate
- A630 (≠ E306) to T: in NM; decreased N-acylmannosamine kinase activity; does not affect homohexamers formation; dbSNP:rs1382191649
- A631 (= A307) 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.
2yi1A Crystal structure of n-acetylmannosamine kinase in complex with n- acetyl mannosamine 6-phosphate and adp. (see paper)
31% identity, 51% coverage: 145:350/406 of query aligns to 63:265/308 of 2yi1A
- binding adenosine-5'-diphosphate: T140 (≠ V223), G189 (≠ I272), L216 (= L301), V261 (≠ P346)
- binding 2-acetamido-2-deoxy-6-O-phosphono-alpha-D-mannopyranose: G71 (≠ V153), G72 (= G154), R73 (≠ P155), S84 (≠ P166), T85 (≠ E167), L87 (≠ F169), N112 (= N195), D113 (≠ G196), G139 (= G222), T140 (≠ V223), G141 (= G224), I142 (= I225), E162 (≠ T245), H165 (= H248), E184 (= E267)
- binding calcium ion: N112 (= N195), N115 (= N198), G144 (≠ T227), A161 (≠ D244)
- binding zinc ion: H165 (= H248), C175 (= C258), C177 (= C260), C182 (= C265)
Sites not aligning to the query:
2yhyA Structure of n-acetylmannosamine kinase in complex with n- acetylmannosamine and adp (see paper)
31% identity, 51% coverage: 145:350/406 of query aligns to 63:265/308 of 2yhyA
Sites not aligning to the query:
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)
32% identity, 51% coverage: 145:350/406 of query aligns to 467:674/722 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.
1z6rA Crystal structure of mlc from escherichia coli (see paper)
23% identity, 85% coverage: 19:365/406 of query aligns to 7:338/382 of 1z6rA
1z05A Crystal structure of the rok family transcriptional regulator, homolog of e.Coli mlc protein.
24% identity, 84% coverage: 19:359/406 of query aligns to 8:349/396 of 1z05A
3vovB Crystal structure of rok hexokinase from thermus thermophilus (see paper)
33% identity, 53% coverage: 148:364/406 of query aligns to 61:263/298 of 3vovB
3vglA Crystal structure of a rok family glucokinase from streptomyces griseus in complex with glucose and amppnp (see paper)
30% identity, 57% coverage: 125:356/406 of query aligns to 35:270/312 of 3vglA
- binding phosphoaminophosphonic acid-adenylate ester: G130 (= G222), T131 (≠ V223), G180 (≠ I272), G214 (vs. gap), S218 (≠ C304), G260 (≠ P346), V261 (≠ L347), E264 (≠ H350)
- binding beta-D-glucopyranose: G65 (= G154), P78 (≠ E167), N103 (= N195), D104 (≠ G196), L133 (≠ I225), G134 (≠ R226), E153 (≠ T245), H156 (= H248), E175 (= E267)
- binding zinc ion: H156 (= H248), C166 (= C258), C168 (= C260), C173 (= C265)
Sites not aligning to the query:
3vgkB Crystal structure of a rok family glucokinase from streptomyces griseus (see paper)
30% identity, 57% coverage: 125:356/406 of query aligns to 35:270/312 of 3vgkB
2qm1B Crystal structure of glucokinase from enterococcus faecalis
30% identity, 49% coverage: 146:345/406 of query aligns to 69:270/325 of 2qm1B
3eo3A Crystal structure of the n-acetylmannosamine kinase domain of human gne protein (see paper)
32% identity, 42% coverage: 179:350/406 of query aligns to 71:245/288 of 3eo3A
3lm9A Crystal structure of fructokinase with adp and fructose bound in the active site (see paper)
22% identity, 57% coverage: 122:354/406 of query aligns to 35:239/294 of 3lm9A
- binding adenosine-5'-diphosphate: G130 (= G222), T131 (≠ V223), G182 (≠ R296), P183 (= P297), E186 (≠ Y300), A193 (= A307), G231 (≠ P346)
- binding beta-D-fructofuranose: G60 (= G154), D104 (≠ G196), I133 (= I225), E151 (≠ D243), E177 (≠ N291)
- binding zinc ion: H154 (= H248), C169 (≠ M283), H172 (≠ G286), C175 (≠ R289)
1xc3A Structure of a putative fructokinase from bacillus subtilis (see paper)
22% identity, 57% coverage: 122:354/406 of query aligns to 35:239/295 of 1xc3A
6jdoA Crystal structure of n-acetyl mannosmaine kinase with amp-pnp from pasteurella multocida
24% identity, 57% coverage: 120:349/406 of query aligns to 30:245/293 of 6jdoA
6jdhA Crystal structure of n-acetyl mannosmaine kinase from pasteurella multocida
24% identity, 57% coverage: 120:349/406 of query aligns to 30:245/293 of 6jdhA
7p9lAAA Ubiquitin-like protein SMT3,N-acetyl-D-glucosamine kinase
25% identity, 67% coverage: 109:382/406 of query aligns to 13:300/303 of 7p9lAAA
- binding 2-acetamido-2-deoxy-6-O-phosphono-beta-D-glucopyranose: P66 (≠ V153), G67 (= G154), S79 (≠ P166), N105 (= N195), D106 (≠ G196), G132 (= G222), T133 (≠ V223), G134 (= G224), V135 (≠ I225), G136 (≠ R226), E155 (≠ T245), H158 (= H248), D188 (≠ E267)
- binding zinc ion: H158 (= H248), C179 (= C258), C181 (= C260), C186 (= C265), E212 (= E302), H216 (≠ E306)
Query Sequence
>WP_015945030.1 NCBI__GCF_000021925.1:WP_015945030.1
MRTGVLIYKDVLSSLSPEAKKILGLILHKGGMTKSQLAKVAGLKLTTLNRMMLPLEKADL
ILPTETGESTGGRKPVIYDVNPRRYYVIGIDISRLYSQVVLTNLKMELIEKDRFDMDRNS
SPQATLNRILDWIGRVMEKRGHGYVIGVGIGTVGPLDRQSGIILNPENFEAQGWENIPLK
AIVEERTGLPVIIDNGANGAVLAETRYGSGKGMKSVIYLNCGVGIRTGVISSGTLVRTIN
DADDTFAHMVIDVNGKPCHCGNQGCVERYSSIYAIMEALAEEMPQGKDRRNHKADRPVSY
LELCREAEENDTIARQVLQNAAVRMGTGLANFIQLLNPGLVVLSGPLILHSQLFYEVCVE
AAKRRRPWDKGGHLVFSRGGAFEENAISIGAAALVVEHYLEPETLG
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