SitesBLAST
Comparing AZOBR_RS00105 FitnessBrowser__azobra:AZOBR_RS00105 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)
35% identity, 95% coverage: 12:370/378 of query aligns to 16:363/393 of O50657
- AGV 44:46 (≠ AKI 40:42) 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 (= P50) 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 (≠ A322) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ T325) 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 (≠ A329) 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 (= G356) mutation to D: Loss of dimer formation and decarboxylase activity.
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
35% identity, 95% coverage: 12:370/378 of query aligns to 17:364/385 of 5gjoA
- active site: K52 (= K47), H180 (= H175), E256 (= E252)
- binding pyridoxal-5'-phosphate: A50 (= A45), K52 (= K47), D71 (= D66), H180 (= H175), S183 (= S178), G219 (= G214), G220 (= G215), E256 (= E252), G258 (= G254), R259 (= R255), Y353 (= Y358)
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
35% identity, 95% coverage: 12:370/378 of query aligns to 16:355/381 of 5gjpA
- active site: K51 (= K47), H171 (= H175), E247 (= E252)
- binding pentane-1,5-diamine: Y290 (≠ D298), D291 (≠ E299), Y344 (= Y358)
- binding pyridoxal-5'-phosphate: A49 (= A45), K51 (= K47), H171 (= H175), S174 (= S178), G211 (= G215), E247 (= E252), G249 (= G254), R250 (= R255), Y344 (= Y358)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
35% identity, 95% coverage: 12:370/378 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, 96% coverage: 17:378/378 of query aligns to 30:372/376 of 2pljA
- active site: K60 (= K47), H179 (= H175), E255 (= E252)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K47), H179 (= H175), S182 (= S178), G220 (= G215), E255 (= E252), G257 (= G254), R258 (= R255), D299 (≠ E299), Y353 (= Y358)
P11926 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Homo sapiens (Human) (see 5 papers)
34% identity, 93% coverage: 20:370/378 of query aligns to 42:400/461 of P11926
- K69 (= K47) modified: N6-(pyridoxal phosphate)lysine
- S200 (= S178) binding
- G237 (= G215) binding
- EPGR 274:277 (= EPGR 252:255) binding
- C360 (= C326) mutation to A: 25% decrease of in vitro nitrosylation level.
- Y389 (= Y358) 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)
2oo0A A structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane (see paper)
34% identity, 93% coverage: 20:370/378 of query aligns to 52:397/419 of 2oo0A
- active site: K79 (= K47), H207 (= H175), E284 (= E252)
- binding pentane-1,5-diamine: P249 (= P217), G250 (≠ T218), S251 (≠ R219), V254 (≠ T222), R287 (= R255), N382 (≠ A354)
- binding pyridoxal-5'-phosphate: A77 (= A45), K79 (= K47), D98 (= D66), H207 (= H175), S210 (= S178), G247 (= G215), E284 (= E252), G286 (= G254), R287 (= R255), Y386 (= Y358)
- binding 3-aminooxy-1-aminopropane: C174 (≠ W142), D329 (= D298), Y386 (= Y358)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
31% identity, 96% coverage: 17:378/378 of query aligns to 26:367/370 of 2plkA
P07805 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Trypanosoma brucei brucei (see 3 papers)
33% identity, 94% coverage: 17:370/378 of query aligns to 37:398/423 of P07805
- K67 (= K47) modified: N6-(pyridoxal phosphate)lysine
- S198 (= S178) binding
- G235 (= G215) binding
- EPGR 272:275 (= EPGR 252:255) binding
- YD 329:330 (≠ -D 298) binding in other chain
- C358 (= C326) 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 (= D327) binding
- Y387 (= Y358) binding
7u6pA Structure of an intellectual disability-associated ornithine decarboxylase variant g84r (see paper)
34% identity, 93% coverage: 20:370/378 of query aligns to 42:387/409 of 7u6pA
1f3tB Crystal structure of trypanosoma brucei ornithine decarboxylase (odc) complexed with putrescine, odc's reaction product. (see paper)
35% identity, 94% coverage: 17:370/378 of query aligns to 20:359/381 of 1f3tB
- active site: K50 (= K47), H171 (= H175), E248 (= E252)
- binding pyridoxal-5'-phosphate: K50 (= K47), R135 (= R132), H171 (= H175), G210 (= G214), G211 (= G215), E248 (= E252), G250 (= G254), R251 (= R255), Y348 (= Y358)
- binding 1,4-diaminobutane: D291 (= D298), Y348 (= Y358)
4zgyA Structure of human ornithine decarboxylase in complex with a c- terminal fragment of antizyme (see paper)
34% identity, 93% coverage: 20:370/378 of query aligns to 18:362/383 of 4zgyA
- active site: K45 (= K47), H170 (= H175), E247 (= E252)
- binding magnesium ion: G210 (= G215), F211 (= F216), R250 (= R255), Y251 (≠ S256)
- binding pyridoxal-5'-phosphate: K45 (= K47), D64 (= D66), H170 (= H175), G210 (= G215), E247 (= E252), G249 (= G254), R250 (= R255), Y353 (= Y358)
2todA Ornithine decarboxylase from trypanosoma brucei k69a mutant in complex with alpha-difluoromethylornithine (see paper)
34% identity, 94% coverage: 17:370/378 of query aligns to 3:343/353 of 2todA
- active site: A33 (≠ K47), H153 (= H175), E230 (= E252)
- binding alpha-difluoromethylornithine: D275 (= D298), C303 (= C326), D304 (= D327), Y332 (= Y358), F340 (= F367)
- binding pyridoxal-5'-phosphate: H153 (= H175), S156 (= S178), G192 (= G214), G193 (= G215), E230 (= E252), G232 (= G254), R233 (= R255), Y332 (= Y358)
P00860 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Mus musculus (Mouse) (see 5 papers)
33% identity, 93% coverage: 20:370/378 of query aligns to 42:400/461 of P00860
- K69 (= K47) modified: N6-(pyridoxal phosphate)lysine
- G237 (= G215) binding
- EPGR 274:277 (= EPGR 252:255) binding
- S303 (≠ A276) modified: Phosphoserine; by CK2
- C360 (= C326) active site, Proton donor; shared with dimeric partner
- G387 (= G356) 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 (= Y358) binding
1szrC A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
34% identity, 94% coverage: 17:370/378 of query aligns to 3:339/347 of 1szrC
Q9FPK5 Ornithine decarboxylase, chloroplastic; Lysine decarboxylase; EC 4.1.1.17; EC 4.1.1.18 from Nicotiana glutinosa (Tobacco) (see paper)
31% identity, 95% coverage: 12:370/378 of query aligns to 60:417/432 of Q9FPK5
- K95 (= K47) mutation to A: Loss of activity.
- C96 (≠ A48) mutation to A: Almost unchanged activity.
- C338 (≠ E295) mutation to A: Loss of activity.
- C377 (= C326) mutation to A: Loss of activity.
1njjA Crystal structure determination of t. Brucei ornithine decarboxylase bound to d-ornithine and to g418 (see paper)
34% identity, 91% coverage: 17:361/378 of query aligns to 12:337/349 of 1njjA
- active site: K42 (= K47), H160 (= H175), E237 (= E252)
- binding geneticin: D206 (= D223), L287 (≠ I305), L327 (≠ R351), E329 (≠ H353), D330 (≠ A354)
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A40 (= A45), K42 (= K47), H160 (= H175), G199 (= G214), G200 (= G215), E237 (= E252), G239 (= G254), R240 (= R255), Y279 (≠ M297), D280 (= D298), Y334 (= Y358)
Sites not aligning to the query:
1szrA A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
34% identity, 94% coverage: 17:370/378 of query aligns to 3:336/345 of 1szrA
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
32% identity, 93% coverage: 12:364/378 of query aligns to 9:364/405 of B4XMC6
- K46 (= K47) 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 (= G215) binding
- EPGR 259:262 (= EPGR 252:255) binding
- Y358 (= Y358) binding
3c5qA Crystal structure of diaminopimelate decarboxylase (i148l mutant) from helicobacter pylori complexed with l-lysine
32% identity, 93% coverage: 12:364/378 of query aligns to 7:357/394 of 3c5qA
- active site: K44 (= K47), H183 (= H175), E257 (= E252)
- binding lysine: L146 (vs. gap), R260 (= R255), R294 (≠ A294), Y298 (≠ D298), Y351 (= Y358)
- binding pyridoxal-5'-phosphate: K44 (= K47), D63 (= D66), H183 (= H175), S186 (= S178), G223 (= G215), E257 (= E252), P258 (= P253), G259 (= G254), R260 (= R255), Y351 (= Y358)
Query Sequence
>AZOBR_RS00105 FitnessBrowser__azobra:AZOBR_RS00105
MTDKIARFFEEQRPQTPCLVVDLDVVEANYHDLEEALPDAKIFYAVKANPAPEILGLLTR
LGSAFDTASVPEIQMVLAAGCAPERISYGNTIKKEADIRRAFELGVRLFAFDSEAELEKI
ARAAPGARVFCRILTSGEGAEWPLSRKFGCDLAMARELLLKAKGMNVVPYGVSFHVGSQQ
KDLMQWDHAIFQVAQLFRELEVLGVDLGMINLGGGFPTRYRTDVPETTAYGQAIFESLRT
HFGNRLPEAIVEPGRSMVGNAGIIESEVVLVSRKSANDVKRWVYLDIGKFSGLAETMDEA
IQYPIQVMGDDGEGDSEAVVLAGPTCDSADVLYERAEYKLPMDLKAGDRVRIHATGAYTT
TYSAVCFNGFAPLQQICI
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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