SitesBLAST
Comparing GFF3844 FitnessBrowser__Marino:GFF3844 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)
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
33% identity, 93% coverage: 19:383/391 of query aligns to 10:364/385 of 5gjoA
- active site: K52 (= K61), H180 (= H190), E256 (= E268)
- binding pyridoxal-5'-phosphate: A50 (= A59), K52 (= K61), D71 (= D80), H180 (= H190), S183 (= S193), G219 (= G230), G220 (= G231), E256 (= E268), G258 (= G270), R259 (= R271), Y353 (= Y371)
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
33% identity, 93% coverage: 19:383/391 of query aligns to 9:363/393 of O50657
- AGV 44:46 (≠ AKV 54:56) 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 (= P64) 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 (≠ A335) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ T338) 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 (≠ A342) 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 (= G369) mutation to D: Loss of dimer formation and decarboxylase activity.
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
32% identity, 93% coverage: 19:383/391 of query aligns to 9:355/381 of 5gjpA
- active site: K51 (= K61), H171 (= H190), E247 (= E268)
- binding pentane-1,5-diamine: Y290 (≠ D314), D291 (≠ E315), Y344 (= Y371)
- binding pyridoxal-5'-phosphate: A49 (= A59), K51 (= K61), H171 (= H190), S174 (= S193), G211 (= G231), E247 (= E268), G249 (= G270), R250 (= R271), Y344 (= Y371)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
32% identity, 93% coverage: 19:383/391 of query aligns to 9:352/369 of 5gjnA
4zgyA Structure of human ornithine decarboxylase in complex with a c- terminal fragment of antizyme (see paper)
30% identity, 96% coverage: 17:391/391 of query aligns to 1:370/383 of 4zgyA
- active site: K45 (= K61), H170 (= H190), E247 (= E268)
- binding magnesium ion: G210 (= G231), F211 (= F232), R250 (= R271), Y251 (≠ S272)
- binding pyridoxal-5'-phosphate: K45 (= K61), D64 (= D80), H170 (= H190), G210 (= G231), E247 (= E268), G249 (= G270), R250 (= R271), Y353 (= Y371)
2pljA Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from vibrio vulnificus (see paper)
30% identity, 90% coverage: 31:383/391 of query aligns to 30:364/376 of 2pljA
- active site: K60 (= K61), H179 (= H190), E255 (= E268)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K61), H179 (= H190), S182 (= S193), G220 (= G231), E255 (= E268), G257 (= G270), R258 (= R271), D299 (= D314), Y353 (= Y371)
2oo0A A structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane (see paper)
31% identity, 92% coverage: 32:391/391 of query aligns to 50:405/419 of 2oo0A
- active site: K79 (= K61), H207 (= H190), E284 (= E268)
- binding pentane-1,5-diamine: P249 (= P233), G250 (≠ A234), S251 (≠ T240), V254 (≠ L243), R287 (= R271), N382 (≠ S367)
- binding pyridoxal-5'-phosphate: A77 (= A59), K79 (= K61), D98 (= D80), H207 (= H190), S210 (= S193), G247 (= G231), E284 (= E268), G286 (= G270), R287 (= R271), Y386 (= Y371)
- binding 3-aminooxy-1-aminopropane: C174 (≠ W157), D329 (= D314), Y386 (= Y371)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
29% identity, 97% coverage: 6:383/391 of query aligns to 1:359/370 of 2plkA
7u6pA Structure of an intellectual disability-associated ornithine decarboxylase variant g84r (see paper)
31% identity, 92% coverage: 32:391/391 of query aligns to 40:395/409 of 7u6pA
P11926 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Homo sapiens (Human) (see 5 papers)
30% identity, 92% coverage: 32:391/391 of query aligns to 40:408/461 of P11926
- K69 (= K61) modified: N6-(pyridoxal phosphate)lysine
- S200 (= S193) binding
- G237 (= G231) binding
- EPGR 274:277 (= EPGR 268:271) binding
- C360 (= C339) mutation to A: 25% decrease of in vitro nitrosylation level.
- Y389 (= Y371) 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)
1f3tB Crystal structure of trypanosoma brucei ornithine decarboxylase (odc) complexed with putrescine, odc's reaction product. (see paper)
31% identity, 92% coverage: 31:391/391 of query aligns to 20:367/381 of 1f3tB
- active site: K50 (= K61), H171 (= H190), E248 (= E268)
- binding pyridoxal-5'-phosphate: K50 (= K61), R135 (= R146), H171 (= H190), G210 (= G230), G211 (= G231), E248 (= E268), G250 (= G270), R251 (= R271), Y348 (= Y371)
- binding 1,4-diaminobutane: D291 (= D314), Y348 (= Y371)
P00860 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Mus musculus (Mouse) (see 5 papers)
30% identity, 92% coverage: 32:391/391 of query aligns to 40:408/461 of P00860
- K69 (= K61) modified: N6-(pyridoxal phosphate)lysine
- G237 (= G231) binding
- EPGR 274:277 (= EPGR 268:271) binding
- S303 (vs. gap) modified: Phosphoserine; by CK2
- C360 (= C339) active site, Proton donor; shared with dimeric partner
- G387 (= G369) 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 (= Y371) binding
P07805 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Trypanosoma brucei brucei (see 3 papers)
31% identity, 92% coverage: 31:391/391 of query aligns to 37:406/423 of P07805