SitesBLAST
Comparing WP_225996779.1 NCBI__GCF_000017145.1:WP_225996779.1 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)
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
36% identity, 94% coverage: 15:371/379 of query aligns to 16:363/393 of O50657
- AGV 44:46 (≠ SAI 43:45) 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 (= P53) 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 (≠ A323) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ T326) 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 (≠ A330) 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 (= G357) mutation to D: Loss of dimer formation and decarboxylase activity.
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
36% identity, 94% coverage: 15:371/379 of query aligns to 17:364/385 of 5gjoA
- active site: K52 (= K50), H180 (= H178), E256 (= E255)
- binding pyridoxal-5'-phosphate: A50 (= A48), K52 (= K50), D71 (= D69), H180 (= H178), S183 (= S181), G219 (= G217), G220 (= G218), E256 (= E255), G258 (= G257), R259 (= R258), Y353 (= Y359)
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
35% identity, 94% coverage: 15:371/379 of query aligns to 16:355/381 of 5gjpA
- active site: K51 (= K50), H171 (= H178), E247 (= E255)
- binding pentane-1,5-diamine: Y290 (≠ D301), D291 (≠ E302), Y344 (= Y359)
- binding pyridoxal-5'-phosphate: A49 (= A48), K51 (= K50), H171 (= H178), S174 (= S181), G211 (= G218), E247 (= E255), G249 (= G257), R250 (= R258), Y344 (= Y359)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
35% identity, 94% coverage: 15:371/379 of query aligns to 16:352/369 of 5gjnA
2pljA Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from vibrio vulnificus (see paper)
32% identity, 93% coverage: 19:372/379 of query aligns to 29:365/376 of 2pljA
- active site: K60 (= K50), H179 (= H178), E255 (= E255)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K50), H179 (= H178), S182 (= S181), G220 (= G218), E255 (= E255), G257 (= G257), R258 (= R258), D299 (≠ E302), Y353 (= Y359)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
32% identity, 93% coverage: 19:372/379 of query aligns to 25:360/370 of 2plkA
P07805 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Trypanosoma brucei brucei (see 3 papers)
33% identity, 97% coverage: 12:379/379 of query aligns to 29:407/423 of P07805
- K67 (= K50) modified: N6-(pyridoxal phosphate)lysine
- S198 (= S181) binding pyridoxal 5'-phosphate
- G235 (= G218) binding pyridoxal 5'-phosphate
- EPGR 272:275 (= EPGR 255:258) binding pyridoxal 5'-phosphate
- YD 329:330 (≠ -D 301) binding in other chain
- C358 (= C327) 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 (= D328) binding substrate
- Y387 (= Y359) binding pyridoxal 5'-phosphate
1f3tB Crystal structure of trypanosoma brucei ornithine decarboxylase (odc) complexed with putrescine, odc's reaction product. (see paper)
34% identity, 98% coverage: 7:379/379 of query aligns to 1:368/381 of 1f3tB
- active site: K50 (= K50), H171 (= H178), E248 (= E255)
- binding pyridoxal-5'-phosphate: K50 (= K50), R135 (= R135), H171 (= H178), G210 (= G217), G211 (= G218), E248 (= E255), G250 (= G257), R251 (= R258), Y348 (= Y359)
- binding 1,4-diaminobutane: D291 (= D301), Y348 (= Y359)
2todA Ornithine decarboxylase from trypanosoma brucei k69a mutant in complex with alpha-difluoromethylornithine (see paper)
33% identity, 95% coverage: 20:379/379 of query aligns to 3:352/353 of 2todA
- active site: A33 (≠ K50), H153 (= H178), E230 (= E255)
- binding alpha-difluoromethylornithine: D275 (= D301), C303 (= C327), D304 (= D328), Y332 (= Y359), F340 (= F368)
- binding pyridoxal-5'-phosphate: H153 (= H178), S156 (= S181), G192 (= G217), G193 (= G218), E230 (= E255), G232 (= G257), R233 (= R258), Y332 (= Y359)
2oo0A A structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane (see paper)
33% identity, 94% coverage: 23:379/379 of query aligns to 52:406/419 of 2oo0A
- active site: K79 (= K50), H207 (= H178), E284 (= E255)
- binding pentane-1,5-diamine: P249 (= P220), G250 (≠ T221), S251 (≠ K222), V254 (≠ R225), R287 (= R258), N382 (≠ G355)
- binding pyridoxal-5'-phosphate: A77 (= A48), K79 (= K50), D98 (= D69), H207 (= H178), S210 (= S181), G247 (= G218), E284 (= E255), G286 (= G257), R287 (= R258), Y386 (= Y359)
- binding 3-aminooxy-1-aminopropane: C174 (≠ W145), D329 (= D301), Y386 (= Y359)
P11926 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Homo sapiens (Human) (see 5 papers)
33% identity, 94% coverage: 23:379/379 of query aligns to 42:409/461 of P11926
- K69 (= K50) modified: N6-(pyridoxal phosphate)lysine
- S200 (= S181) binding pyridoxal 5'-phosphate
- G237 (= G218) binding pyridoxal 5'-phosphate
- EPGR 274:277 (= EPGR 255:258) binding pyridoxal 5'-phosphate
- C360 (= C327) mutation to A: 25% decrease of in vitro nitrosylation level.
- Y389 (= Y359) binding pyridoxal 5'-phosphate
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)
Q9FPK5 Ornithine decarboxylase, chloroplastic; Lysine decarboxylase; EC 4.1.1.17; EC 4.1.1.18 from Nicotiana glutinosa (Tobacco) (see paper)
33% identity, 93% coverage: 20:372/379 of query aligns to 65:418/432 of Q9FPK5
- K95 (= K50) mutation to A: Loss of activity.
- C96 (≠ A51) mutation to A: Almost unchanged activity.
- C338 (≠ E298) mutation to A: Loss of activity.
- C377 (= C327) mutation to A: Loss of activity.
4zgyA Structure of human ornithine decarboxylase in complex with a c- terminal fragment of antizyme (see paper)
33% identity, 94% coverage: 23:379/379 of query aligns to 18:371/383 of 4zgyA