SitesBLAST
Comparing PP_3394 FitnessBrowser__Putida:PP_3394 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)
Q8TB92 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; HMGCL-like 1; Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase; er-cHL; EC 4.1.3.4 from Homo sapiens (Human) (see 2 papers)
38% identity, 91% coverage: 4:284/309 of query aligns to 78:355/370 of Q8TB92
- R86 (= R12) mutation to Q: Abolishes catalytic activity.
- L237 (≠ V166) mutation to S: Abolishes catalytic activity.
- H278 (= H207) mutation to R: Abolishes catalytic activity.
Sites not aligning to the query:
- 2 modified: N-myristoyl glycine; G→A: Abolishes myristoylation and induces a subcellular location change.
3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
38% identity, 91% coverage: 4:284/309 of query aligns to 6:283/296 of 3mp3B
- binding (3R,5S,9R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8-dimethyl-10,14,19-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: R14 (= R12), D15 (= D13), Q18 (= Q16), F49 (= F47), V50 (= V48), S51 (≠ P49), W54 (≠ L52), P81 (= P79), N82 (= N80), K84 (≠ R82), G85 (= G83), N111 (≠ R112), R122 (= R123), Y140 (≠ G141), S142 (= S143), T178 (= T179), H206 (= H207)
- binding magnesium ion: D15 (= D13), H206 (= H207), H208 (= H209)
2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
38% identity, 91% coverage: 4:284/309 of query aligns to 6:283/296 of 2cw6A
P35914 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Homo sapiens (Human) (see 11 papers)
38% identity, 91% coverage: 4:284/309 of query aligns to 33:310/325 of P35914
- E37 (= E8) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
- R41 (= R12) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
- D42 (= D13) to E: in HMGCLD; reduced activity; to G: in HMGCLD; loss of activity; dbSNP:rs1467902610; to H: in HMGCLD; loss of activity; mutation D->A,N: Loss of activity, and reduced proton exchange rate.
- K48 (≠ Q19) to N: in HMGCLD; abolishes almost all enzymatic activity
- E72 (= E43) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
- S142 (≠ E116) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- C174 (= C148) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
- F192 (≠ V166) to S: in HMGCLD; activity lower than 5% respect to the wild-type
- I200 (≠ V174) to F: in HMGCLD; activity lower than 5% respect to the wild-type
- G203 (= G177) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
- D204 (= D178) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
- H233 (= H207) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
- E279 (= E253) mutation to A: Reduced thermal stability, but normal activity.
- D280 (= D254) mutation to A: Normal activity.
Sites not aligning to the query:
- 323 modified: Interchain; C→S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.
3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
37% identity, 91% coverage: 4:284/309 of query aligns to 6:283/296 of 3mp5B
- binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D13), Q18 (= Q16), S51 (≠ P49), W54 (≠ L52), F100 (≠ V101), N111 (≠ R112), N113 (≠ P114), Y140 (≠ G141), S142 (= S143), T178 (= T179), C239 (= C240)
- binding magnesium ion: D15 (= D13), H206 (= H207), H208 (= H209)
6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
37% identity, 95% coverage: 4:297/309 of query aligns to 8:296/305 of 6ndsA
- binding coenzyme a: V52 (= V48), S53 (≠ P49), I57 (≠ L53), N84 (= N80), G87 (= G83), R90 (≠ D86), N113 (= N109), M114 (≠ V110), R115 (= R111)
- binding zinc ion: D17 (= D13), H207 (= H207), H209 (= H209)
1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
39% identity, 87% coverage: 4:273/309 of query aligns to 4:270/283 of 1ydnA
P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii (see paper)
36% identity, 89% coverage: 1:275/309 of query aligns to 1:272/301 of P13703
- C237 (= C240) active site
Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
27% identity, 70% coverage: 94:308/309 of query aligns to 184:387/506 of Q9FG67
- A290 (= A205) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.
Sites not aligning to the query:
- 102 S→F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
27% identity, 93% coverage: 4:289/309 of query aligns to 4:280/308 of 3rmjB
Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain MC58) (see 2 papers)
27% identity, 93% coverage: 4:289/309 of query aligns to 7:283/517 of Q9JZG1
- D16 (= D13) binding
- H204 (= H207) binding
- H206 (= H209) binding
- N240 (= N249) binding
Sites not aligning to the query:
- 366:517 Required for the condensation reaction. Not required to bind substrate
3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
25% identity, 77% coverage: 1:238/309 of query aligns to 9:221/370 of 3mi3A
6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
24% identity, 73% coverage: 82:308/309 of query aligns to 101:320/409 of 6e1jA
Sites not aligning to the query:
- binding coenzyme a: 30, 60, 63, 95, 97, 322, 323, 324, 327, 331, 359, 362, 363
- binding manganese (ii) ion: 27, 82, 84
3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
26% identity, 77% coverage: 1:238/309 of query aligns to 27:250/400 of 3ivtB
Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
26% identity, 77% coverage: 1:238/309 of query aligns to 32:255/418 of Q9Y823
- R43 (= R12) binding ; mutation R->A,K,Q: Abolishes the catalytic activity.
- E44 (≠ D13) binding ; binding ; binding
- Q47 (= Q16) mutation to A: Abolishes the catalytic activity.
- E74 (= E43) mutation to A: Abolishes the catalytic activity.; mutation to Q: Results in a moderate decrease in the turnover number and a slight increase in the Km value for each substrate.
- H103 (≠ V76) binding ; mutation to A: Substantially impairs catalytic efficiency.
- D123 (≠ P98) binding ; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
- R163 (≠ A145) binding ; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
- S165 (≠ G147) binding ; mutation to A: Results in a moderate decrease in catalytic efficiency.
- E167 (≠ T149) mutation E->A,Q: Abolishes the catalytic activity.
- T197 (= T179) binding ; binding ; mutation to A: Exhibits a 25-fold decrease in catalytic efficiency.; mutation to S: Results in a modest decrease in catalytic efficiency.; mutation to V: Abolishes the catalytic activity.
- E222 (≠ K204) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
- H224 (= H207) binding ; binding
- H226 (= H209) binding ; binding
Sites not aligning to the query:
- 288 R→K: Does not affect the catalytic activity but impairs L-lysine inhibition.
- 332 Y→A: Abolishes the catalytic activity.; Y→F: Results in a decrease in catalytic efficiency.
- 364 Q→R: Does not affect the catalytic activity but impairs L-lysine inhibition.
3ivsA Homocitrate synthase lys4 (see paper)
27% identity, 41% coverage: 112:238/309 of query aligns to 62:219/364 of 3ivsA
Sites not aligning to the query:
Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 66% coverage: 94:298/309 of query aligns to 184:391/503 of Q9FN52
- G263 (= G181) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.
O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
28% identity, 77% coverage: 1:238/309 of query aligns to 1:226/376 of O87198
- R12 (= R12) binding
- E13 (≠ D13) binding
- H72 (≠ V76) binding ; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
- D92 (≠ V96) binding
- R133 (≠ V139) binding
- S135 (≠ G141) binding
- T166 (= T179) binding ; binding
- H195 (= H207) binding
- H197 (= H209) binding
2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
27% identity, 77% coverage: 1:238/309 of query aligns to 1:220/314 of 2zyfA
2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
31% identity, 36% coverage: 164:273/309 of query aligns to 164:266/453 of 2nx9B
Sites not aligning to the query:
Query Sequence
>PP_3394 FitnessBrowser__Putida:PP_3394
MTTITINEVGLRDGLQSLQVIMPTAAKRRWIDAAYGAGVRHMEVASFVPARLLPQMADAR
EVVAHALTYPDLQVTVLAPNLRGARDALESGAHRIVAPVSVSTAHSLANVRRTPVEMVEE
LGRMCQLRTEMGLHGVQVVAGMSVAFGCTRQGEVPLADLCALTRQVIEAGCDLVSLGDTT
GYANPGQVAMVLQAVREIAGDRLKAAHFHDTRGLALANSLVAVQQGIGELDASLAGLGGC
PFAPGASGNTVTEDLVFMLQSMGYDTGIDLPALIETRQVLSEALPGEPLYGFIARAGLPL
NFANTHRHA
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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