SitesBLAST
Comparing 3607967 FitnessBrowser__Dino:3607967 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)
2pljA Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from vibrio vulnificus (see paper)
35% identity, 89% coverage: 37:390/398 of query aligns to 27:364/376 of 2pljA
- active site: K60 (= K71), H179 (= H199), E255 (= E274)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K71), H179 (= H199), S182 (= S202), G220 (= G239), E255 (= E274), G257 (= G276), R258 (= R277), D299 (≠ E321), Y353 (= Y378)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
35% identity, 89% coverage: 37:390/398 of query aligns to 23:359/370 of 2plkA
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
32% identity, 88% coverage: 40:390/398 of query aligns to 21:363/393 of O50657
- AG-V 44:46 (≠ GTLI 63:66) mutation to VTP: 2-fold increase in substrate specificity towards ornithine. 5-fold increase in substrate specificity towards ornithine; when associated with D-54. 70-fold increase in substrate specificity towards ornithine; when associated with D-54 and A-322. 16-fold increase in substrate specificity towards ornithine; when associated with D-54; T-322 and L-326.
- P54 (= P74) mutation to D: 3-fold increase in substrate specificity towards ornithine. 5-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46. 70-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46 and A-322. 16-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46; T-322 and L-326.
- G319 (≠ A342) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (= S345) mutation to A: 29-fold increase in substrate specificity towards ornithine. 70-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46 and D-54.; mutation to T: 16-fold increase in substrate specificity towards ornithine; when associated with L-326. 16-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46; D-54 and L-326.
- I326 (≠ A349) mutation to L: 16-fold increase in substrate specificity towards ornithine; when associated with T-322. 16-fold increase in substrate specificity towards ornithine; when associated with 44-V--P-46; D-54 and T-322.
- G350 (= G376) mutation to D: Loss of dimer formation and decarboxylase activity.
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
32% identity, 88% coverage: 40:390/398 of query aligns to 22:364/385 of 5gjoA
- active site: K52 (= K71), H180 (= H199), E256 (= E274)
- binding pyridoxal-5'-phosphate: A50 (= A69), K52 (= K71), D71 (= D90), H180 (= H199), S183 (= S202), G219 (= G238), G220 (= G239), E256 (= E274), G258 (= G276), R259 (= R277), Y353 (= Y378)
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
32% identity, 88% coverage: 40:390/398 of query aligns to 21:355/381 of 5gjpA
- active site: K51 (= K71), H171 (= H199), E247 (= E274)
- binding pentane-1,5-diamine: Y290 (≠ E320), D291 (≠ E321), Y344 (= Y378)
- binding pyridoxal-5'-phosphate: A49 (= A69), K51 (= K71), H171 (= H199), S174 (= S202), G211 (= G239), E247 (= E274), G249 (= G276), R250 (= R277), Y344 (= Y378)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
32% identity, 88% coverage: 40:390/398 of query aligns to 21:352/369 of 5gjnA
2nvaA The x-ray crystal structure of the paramecium bursaria chlorella virus arginine decarboxylase bound to agmatine (see paper)
29% identity, 83% coverage: 67:398/398 of query aligns to 44:369/369 of 2nvaA
- active site: K48 (= K71), H176 (= H199), E249 (= E274)
- binding (4-{[(4-{[amino(imino)methyl]amino}butyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: D67 (= D90), L145 (= L168), H176 (= H199), S179 (= S202), G215 (= G238), G216 (= G239), E249 (= E274), G251 (= G276), R252 (= R277), E293 (= E321), C321 (= C346), D322 (= D347), Y350 (= Y378)
2nv9B The x-ray crystal structure of the paramecium bursaria chlorella virus arginine decarboxylase (see paper)
28% identity, 83% coverage: 67:398/398 of query aligns to 44:372/372 of 2nv9B
- active site: K48 (= K71), H176 (= H199), E252 (= E274)
- binding pyridoxal-5'-phosphate: K48 (= K71), D67 (= D90), H176 (= H199), S179 (= S202), G215 (= G238), G216 (= G239), E252 (= E274), G254 (= G276), R255 (= R277), Y353 (= Y378)
4zgyA Structure of human ornithine decarboxylase in complex with a c- terminal fragment of antizyme (see paper)
31% identity, 81% coverage: 68:390/398 of query aligns to 42:362/383 of 4zgyA
- active site: K45 (= K71), H170 (= H199), E247 (= E274)
- binding magnesium ion: G210 (= G239), F211 (= F240), R250 (= R277), Y251 (≠ G278)
- binding pyridoxal-5'-phosphate: K45 (= K71), D64 (= D90), H170 (= H199), G210 (= G239), E247 (= E274), G249 (= G276), R250 (= R277), Y353 (= Y378)
2oo0A A structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane (see paper)
32% identity, 81% coverage: 68:390/398 of query aligns to 76:397/419 of 2oo0A
- active site: K79 (= K71), H207 (= H199), E284 (= E274)
- binding pentane-1,5-diamine: P249 (= P241), G250 (≠ A242), S251 (≠ Y244), V254 (≠ P247), R287 (= R277), N382 (≠ A374)
- binding pyridoxal-5'-phosphate: A77 (= A69), K79 (= K71), D98 (= D90), H207 (= H199), S210 (= S202), G247 (= G239), E284 (= E274), G286 (= G276), R287 (= R277), Y386 (= Y378)
- binding 3-aminooxy-1-aminopropane: C174 (≠ W166), D329 (≠ T318), Y386 (= Y378)
P11926 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Homo sapiens (Human) (see 5 papers)
31% identity, 81% coverage: 68:390/398 of query aligns to 66:400/461 of P11926
- K69 (= K71) modified: N6-(pyridoxal phosphate)lysine
- S200 (= S202) binding
- G237 (= G239) binding
- EPGR 274:277 (= EPGR 274:277) binding
- C360 (= C346) mutation to A: 25% decrease of in vitro nitrosylation level.
- Y389 (= Y378) binding
Sites not aligning to the query:
- 448:461 natural variant: Missing (in BABS; gain-of-function variant resulting in increased putrescine biosynthesis as indicated by higher amount of putrescine in patient red blood cells compared to controls; increased ODC1 protein levels in patient red blood cells)
7u6pA Structure of an intellectual disability-associated ornithine decarboxylase variant g84r (see paper)
31% identity, 81% coverage: 68:390/398 of query aligns to 66:387/409 of 7u6pA
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
31% identity, 89% coverage: 40:393/398 of query aligns to 14:372/405 of B4XMC6
- K46 (= K71) modified: N6-(pyridoxal phosphate)lysine
- I148 (vs. gap) mutation to A: Nearly no change in substrate affinity and 47-fold decrease in catalytic activity.; mutation to D: 2-fold decrease in substrate affinity and 235-fold decrease in catalytic activity.; mutation to F: 4-fold increase in substrate affinity and 23-fold decrease in catalytic activity.; mutation to G: Nearly no change in substrate affinity and 235-fold decrease in catalytic activity.; mutation to K: Nearly no change in substrate affinity and 55-fold decrease in catalytic activity.; mutation to L: 13-fold increase in substrate affinity and 40-fold decrease in catalytic activity.
- G225 (= G239) binding
- EPGR 259:262 (= EPGR 274:277) binding
- Y358 (= Y378) binding
P00860 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Mus musculus (Mouse) (see 5 papers)
30% identity, 81% coverage: 68:390/398 of query aligns to 66:400/461 of P00860
- K69 (= K71) modified: N6-(pyridoxal phosphate)lysine
- G237 (= G239) binding
- EPGR 274:277 (= EPGR 274:277) binding
- S303 (≠ E298) modified: Phosphoserine; by CK2
- C360 (= C346) active site, Proton donor; shared with dimeric partner
- G387 (= G376) mutation to A: Partial loss of activity.; mutation G->C,D,E,F,H,I,K,L,M,N,P,Q,R,S,T,V,W,Y: Loss of activity.
- Y389 (= Y378) binding
1f3tB Crystal structure of trypanosoma brucei ornithine decarboxylase (odc) complexed with putrescine, odc's reaction product. (see paper)
30% identity, 89% coverage: 35:390/398 of query aligns to 15:359/381 of 1f3tB
- active site: K50 (= K71), H171 (= H199), E248 (= E274)
- binding pyridoxal-5'-phosphate: K50 (= K71), R135 (= R156), H171 (= H199), G210 (= G238), G211 (= G239), E248 (= E274), G250 (= G276), R251 (= R277), Y348 (= Y378)
- binding 1,4-diaminobutane: D291 (≠ T318), Y348 (= Y378)
P07805 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Trypanosoma brucei brucei (see 3 papers)
29% identity, 88% coverage: 40:390/398 of query aligns to 37:398/423 of P07805
- K67 (= K71) modified: N6-(pyridoxal phosphate)lysine
- S198 (= S202) binding
- G235 (= G239) binding
- EPGR 272:275 (= EPGR 274:277) binding
- YD 329:330 (≠ ET 317:318) binding in other chain
- C358 (= C346) active site, Proton donor; shared with dimeric partner; mutation C->S,A: Converts the enzyme into a decarboxylation-dependent transaminase, producing gamma-aminobutyaldehyde (gamma-ABA) and pyridoxamine 5-phosphate (PMP) instead of putrescine.
- D359 (= D347) binding
- Y387 (= Y378) binding
2todA Ornithine decarboxylase from trypanosoma brucei k69a mutant in complex with alpha-difluoromethylornithine (see paper)
29% identity, 88% coverage: 40:390/398 of query aligns to 3:343/353 of 2todA
- active site: A33 (≠ K71), H153 (= H199), E230 (= E274)
- binding alpha-difluoromethylornithine: D275 (≠ E321), C303 (= C346), D304 (= D347), Y332 (= Y378), F340 (= F387)
- binding pyridoxal-5'-phosphate: H153 (= H199), S156 (= S202), G192 (= G238), G193 (= G239), E230 (= E274), G232 (= G276), R233 (= R277), Y332 (= Y378)
Q9FPK5 Ornithine decarboxylase, chloroplastic; Lysine decarboxylase; EC 4.1.1.17; EC 4.1.1.18 from Nicotiana glutinosa (Tobacco) (see paper)
31% identity, 88% coverage: 39:390/398 of query aligns to 64:417/432 of Q9FPK5
- K95 (= K71) mutation to A: Loss of activity.
- C96 (≠ A72) mutation to A: Almost unchanged activity.
- C338 (≠ A322) mutation to A: Loss of activity.
- C377 (= C346) mutation to A: Loss of activity.
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
31% identity, 89% coverage: 40:393/398 of query aligns to 12:365/394 of 3c5qA
- active site: K44 (= K71), H183 (= H199), E257 (= E274)
- binding lysine: L146 (vs. gap), R260 (= R277), R294 (≠ A316), Y298 (vs. gap), Y351 (= Y378)
- binding pyridoxal-5'-phosphate: K44 (= K71), D63 (= D90), H183 (= H199), S186 (= S202), G223 (= G239), E257 (= E274), P258 (= P275), G259 (= G276), R260 (= R277), Y351 (= Y378)
1szrC A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
29% identity, 88% coverage: 40:390/398 of query aligns to 3:339/347 of 1szrC
Query Sequence
>3607967 FitnessBrowser__Dino:3607967
MEMTMNAYVTGLARSRPLAPIETVESRLRGFIDGRIFDRPTLVLDCDAVVAKYHALAHGL
GQGTLIHYAMKANPAPEILRALAAEGCGFDAASRGEIELALAAGATAARISFGNTIKRPS
DIAFAHAHGIDLFAADAEAELDKIAAHAPGARVFLRVLVGATGADWPLSRKFGCAPDTAL
RLMDRAAFLGLRPVGLSFHVGSQTRDPGMWSDTLDQMAEIWHAGRARGHDLNLINIGGGF
PAFYGDPILEAETYAGRVGALVRARFGDATVMAEPGRGLVAEAGMIVAEVLLVSRKSEDD
LCRWVYLDIGKFSGLAETMEEAIRYQFVTPHDGGETGPCIMAGPSCDSADVLYEQRPVHL
PMALQSGDRILIKATGAYTTTYSSVGFNGFPPLDLIVI
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