SitesBLAST
Comparing Ga0059261_3753 FitnessBrowser__Korea:Ga0059261_3753 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)
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
33% identity, 79% coverage: 45:362/402 of query aligns to 48:363/393 of O50657
- P54 (= P51) 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 (≠ Y317) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ T320) 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 (≠ M324) 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 (= G349) mutation to D: Loss of dimer formation and decarboxylase activity.
Sites not aligning to the query:
- 44:46 AGV→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.
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
33% identity, 79% coverage: 45:362/402 of query aligns to 49:364/385 of 5gjoA
- active site: K52 (= K48), H180 (= H179), E256 (= E254)
- binding pyridoxal-5'-phosphate: A50 (= A46), K52 (= K48), D71 (= D68), H180 (= H179), S183 (= S182), G219 (= G215), G220 (= G216), E256 (= E254), G258 (= G256), R259 (= R257), Y353 (= Y351)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
32% identity, 79% coverage: 45:362/402 of query aligns to 48:352/369 of 5gjnA
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
32% identity, 79% coverage: 45:362/402 of query aligns to 48:355/381 of 5gjpA
- active site: K51 (= K48), H171 (= H179), E247 (= E254)
- binding pentane-1,5-diamine: Y290 (≠ H293), D291 (≠ V294), Y344 (= Y351)
- binding pyridoxal-5'-phosphate: A49 (= A46), K51 (= K48), H171 (= H179), S174 (= S182), G211 (= G216), E247 (= E254), G249 (= G256), R250 (= R257), Y344 (= Y351)
2pljA Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from vibrio vulnificus (see paper)
31% identity, 86% coverage: 19:362/402 of query aligns to 30:364/376 of 2pljA
- active site: K60 (= K48), H179 (= H179), E255 (= E254)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K48), H179 (= H179), S182 (= S182), G220 (= G216), E255 (= E254), G257 (= G256), R258 (= R257), D299 (= D290), Y353 (= Y351)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
30% identity, 86% coverage: 19:362/402 of query aligns to 26:359/370 of 2plkA
1f3tB Crystal structure of trypanosoma brucei ornithine decarboxylase (odc) complexed with putrescine, odc's reaction product. (see paper)
32% identity, 82% coverage: 42:370/402 of query aligns to 44:367/381 of 1f3tB
- active site: K50 (= K48), H171 (= H179), E248 (= E254)
- binding pyridoxal-5'-phosphate: K50 (= K48), R135 (= R139), H171 (= H179), G210 (= G215), G211 (= G216), E248 (= E254), G250 (= G256), R251 (= R257), Y348 (= Y351)
- binding 1,4-diaminobutane: D291 (= D290), Y348 (= Y351)
2oo0A A structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane (see paper)
29% identity, 84% coverage: 42:378/402 of query aligns to 73:413/419 of 2oo0A
- active site: K79 (= K48), H207 (= H179), E284 (= E254)
- binding pentane-1,5-diamine: P249 (= P218), G250 (≠ S219), S251 (≠ T220), V254 (vs. gap), R287 (= R257), N382 (≠ M347)
- binding pyridoxal-5'-phosphate: A77 (= A46), K79 (= K48), D98 (= D68), H207 (= H179), S210 (= S182), G247 (= G216), E284 (= E254), G286 (= G256), R287 (= R257), Y386 (= Y351)
- binding 3-aminooxy-1-aminopropane: C174 (≠ L147), D329 (= D290), Y386 (= Y351)
7u6pA Structure of an intellectual disability-associated ornithine decarboxylase variant g84r (see paper)
29% identity, 84% coverage: 42:378/402 of query aligns to 63:403/409 of 7u6pA
P11926 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Homo sapiens (Human) (see 5 papers)
29% identity, 84% coverage: 42:378/402 of query aligns to 63:416/461 of P11926
- K69 (= K48) modified: N6-(pyridoxal phosphate)lysine
- S200 (= S182) binding
- G237 (= G216) binding
- EPGR 274:277 (= EPGR 254:257) binding
- C360 (= C321) mutation to A: 25% decrease of in vitro nitrosylation level.
- Y389 (= Y351) 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)
P07805 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Trypanosoma brucei brucei (see 3 papers)
30% identity, 82% coverage: 42:370/402 of query aligns to 61:406/423 of P07805
- K67 (= K48) modified: N6-(pyridoxal phosphate)lysine
- S198 (= S182) binding
- G235 (= G216) binding
- EPGR 272:275 (= EPGR 254:257) binding
- YD 329:330 (≠ FD 289:290) binding in other chain
- C358 (= C321) 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 (= D322) binding
- Y387 (= Y351) binding
P00860 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Mus musculus (Mouse) (see 5 papers)
29% identity, 85% coverage: 42:382/402 of query aligns to 63:420/461 of P00860
- K69 (= K48) modified: N6-(pyridoxal phosphate)lysine
- G237 (= G216) binding
- EPGR 274:277 (= EPGR 254:257) binding
- S303 (vs. gap) modified: Phosphoserine; by CK2
- C360 (= C321) active site, Proton donor; shared with dimeric partner
- G387 (= G349) 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 (= Y351) binding
2todA Ornithine decarboxylase from trypanosoma brucei k69a mutant in complex with alpha-difluoromethylornithine (see paper)
31% identity, 82% coverage: 42:370/402 of query aligns to 27:351/353 of 2todA
- active site: A33 (≠ K48), H153 (= H179), E230 (= E254)
- binding alpha-difluoromethylornithine: D275 (= D290), C303 (= C321), D304 (= D322), Y332 (= Y351), F340 (= F359)
- binding pyridoxal-5'-phosphate: H153 (= H179), S156 (= S182), G192 (= G215), G193 (= G216), E230 (= E254), G232 (= G256), R233 (= R257), Y332 (= Y351)
1szrC A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
31% identity, 82% coverage: 42:370/402 of query aligns to 27:347/347 of 1szrC
4zgyA Structure of human ornithine decarboxylase in complex with a c- terminal fragment of antizyme (see paper)
29% identity, 84% coverage: 42:378/402 of query aligns to 39:378/383 of 4zgyA
- active site: K45 (= K48), H170 (= H179), E247 (= E254)
- binding magnesium ion: G210 (= G216), F211 (= F217), R250 (= R257), Y251 (≠ A258)
- binding pyridoxal-5'-phosphate: K45 (= K48), D64 (= D68), H170 (= H179), G210 (= G216), E247 (= E254), G249 (= G256), R250 (= R257), Y353 (= Y351)
1szrA A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
30% identity, 82% coverage: 42:370/402 of query aligns to 27:344/345 of 1szrA
2nv9B The x-ray crystal structure of the paramecium bursaria chlorella virus arginine decarboxylase (see paper)
29% identity, 83% coverage: 39:370/402 of query aligns to 38:372/372 of 2nv9B
- active site: K48 (= K48), H176 (= H179), E252 (= E254)
- binding pyridoxal-5'-phosphate: K48 (= K48), D67 (= D68), H176 (= H179), S179 (= S182), G215 (= G215), G216 (= G216), E252 (= E254), G254 (= G256), R255 (= R257), Y353 (= Y351)
1njjA Crystal structure determination of t. Brucei ornithine decarboxylase bound to d-ornithine and to g418 (see paper)
30% identity, 77% coverage: 42:351/402 of query aligns to 36:334/349 of 1njjA
- active site: K42 (= K48), H160 (= H179), E237 (= E254)
- binding geneticin: D206 (≠ P222), L287 (≠ G306), L327 (≠ E344), E329 (≠ G346), D330 (≠ M347)
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A40 (= A46), K42 (= K48), H160 (= H179), G199 (= G215), G200 (= G216), E237 (= E254), G239 (= G256), R240 (= R257), Y279 (≠ F289), D280 (= D290), Y334 (= Y351)
Sites not aligning to the query:
Q9FPK5 Ornithine decarboxylase, chloroplastic; Lysine decarboxylase; EC 4.1.1.17; EC 4.1.1.18 from Nicotiana glutinosa (Tobacco) (see paper)
31% identity, 81% coverage: 44:367/402 of query aligns to 91:422/432 of Q9FPK5
- K95 (= K48) mutation to A: Loss of activity.
- C96 (≠ A49) mutation to A: Almost unchanged activity.
- C338 (vs. gap) mutation to A: Loss of activity.
- C377 (= C321) mutation to A: Loss of activity.
2nvaA The x-ray crystal structure of the paramecium bursaria chlorella virus arginine decarboxylase bound to agmatine (see paper)
29% identity, 83% coverage: 39:370/402 of query aligns to 38:369/369 of 2nvaA
- active site: K48 (= K48), H176 (= H179), E249 (= E254)
- binding (4-{[(4-{[amino(imino)methyl]amino}butyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: D67 (= D68), L145 (= L149), H176 (= H179), S179 (= S182), G215 (= G215), G216 (= G216), E249 (= E254), G251 (= G256), R252 (= R257), E293 (≠ G295), C321 (= C321), D322 (= D322), Y350 (= Y351)
Query Sequence
>Ga0059261_3753 FitnessBrowser__Korea:Ga0059261_3753
LHKHHSALGLAKALRPVEPVTLVRPHAAKRAARFFVEKFPGTTMYAVKANPSPELLQILW
DAGITHYDVASIGEVRMARRALPKAVLCFMHPVKAEEAIEEAYFVHGVRTFSLDTMDELE
KIVRATRGAQDLNLCVRIRVSSDHSKLSLAAKFGAEPEDVAELLVATRQAADALGICFHV
GSQAMTPAAYAEAMERVRVAIVASSVTVDIVDVGGGFPSTYPGMEPPPLDAYFGVIHNAF
ENLPISYSAELWCEPGRALCAEYSSLIVRVEKRRGDELYINDGAYGALFDAAHVGWRFPV
TLLREGVAAETEAFSFYGPTCDDMDHMAGPFELPADVAAGDYIEVGMLGAYGCAMRTAFN
GFGSDTVHEVTDEPMATLYSGIAIERPTNVVSLDQFKRRARR
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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