SitesBLAST
Comparing WP_011383514.1 NCBI__GCF_000009985.1:WP_011383514.1 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)
32% identity, 90% coverage: 20:379/400 of query aligns to 6:363/393 of O50657
- AGV 44:46 (≠ GQV 57:59) 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 (= P67) 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 (= G332) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ T337) 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 (≠ L341) 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 (= G366) 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, 90% coverage: 20:379/400 of query aligns to 7:364/385 of 5gjoA
- active site: K52 (= K64), H180 (= H194), E256 (= E269)
- binding pyridoxal-5'-phosphate: A50 (= A62), K52 (= K64), D71 (= D84), H180 (= H194), S183 (= S197), G219 (= G230), G220 (= G231), E256 (= E269), G258 (= G271), R259 (= R272), Y353 (= Y368)
2oo0A A structural insight into the inhibition of human and leishmania donovani ornithine decarboxylases by 3-aminooxy-1-aminopropane (see paper)
33% identity, 80% coverage: 60:380/400 of query aligns to 75:398/419 of 2oo0A
- active site: K79 (= K64), H207 (= H194), E284 (= E269)
- binding pentane-1,5-diamine: P249 (= P233), G250 (vs. gap), S251 (vs. gap), V254 (vs. gap), R287 (= R272), N382 (≠ Q364)
- binding pyridoxal-5'-phosphate: A77 (= A62), K79 (= K64), D98 (= D84), H207 (= H194), S210 (= S197), G247 (= G231), E284 (= E269), G286 (= G271), R287 (= R272), Y386 (= Y368)
- binding 3-aminooxy-1-aminopropane: C174 (≠ L163), D329 (≠ A310), Y386 (= Y368)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
31% identity, 90% coverage: 20:379/400 of query aligns to 6:352/369 of 5gjnA
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
31% identity, 90% coverage: 20:379/400 of query aligns to 6:355/381 of 5gjpA
- active site: K51 (= K64), H171 (= H194), E247 (= E269)
- binding pentane-1,5-diamine: Y290 (≠ A308), D291 (≠ L309), Y344 (= Y368)
- binding pyridoxal-5'-phosphate: A49 (= A62), K51 (= K64), H171 (= H194), S174 (= S197), G211 (= G231), E247 (= E269), G249 (= G271), R250 (= R272), Y344 (= Y368)
7u6pA Structure of an intellectual disability-associated ornithine decarboxylase variant g84r (see paper)
32% identity, 80% coverage: 60:380/400 of query aligns to 65:388/409 of 7u6pA
P11926 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Homo sapiens (Human) (see 5 papers)
32% identity, 80% coverage: 60:380/400 of query aligns to 65:401/461 of P11926
- K69 (= K64) modified: N6-(pyridoxal phosphate)lysine
- S200 (= S197) binding
- G237 (= G231) binding
- EPGR 274:277 (= EPGR 269:272) binding
- C360 (= C338) mutation to A: 25% decrease of in vitro nitrosylation level.
- Y389 (= Y368) 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)
2pljA Crystal structure of lysine/ornithine decarboxylase complexed with putrescine from vibrio vulnificus (see paper)
32% identity, 89% coverage: 35:389/400 of query aligns to 30:374/376 of 2pljA
- active site: K60 (= K64), H179 (= H194), E255 (= E269)
- binding (4-{[(4-aminobutyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: K60 (= K64), H179 (= H194), S182 (= S197), G220 (= G231), E255 (= E269), G257 (= G271), R258 (= R272), D299 (≠ L309), Y353 (= Y368)
1f3tB Crystal structure of trypanosoma brucei ornithine decarboxylase (odc) complexed with putrescine, odc's reaction product. (see paper)
33% identity, 80% coverage: 60:380/400 of query aligns to 46:360/381 of 1f3tB
- active site: K50 (= K64), H171 (= H194), E248 (= E269)
- binding pyridoxal-5'-phosphate: K50 (= K64), R135 (= R153), H171 (= H194), G210 (= G230), G211 (= G231), E248 (= E269), G250 (= G271), R251 (= R272), Y348 (= Y368)
- binding 1,4-diaminobutane: D291 (≠ A306), Y348 (= Y368)
P00860 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Mus musculus (Mouse) (see 5 papers)
32% identity, 80% coverage: 60:380/400 of query aligns to 65:401/461 of P00860
- K69 (= K64) modified: N6-(pyridoxal phosphate)lysine
- G237 (= G231) binding
- EPGR 274:277 (= EPGR 269:272) binding
- S303 (vs. gap) modified: Phosphoserine; by CK2
- C360 (= C338) active site, Proton donor; shared with dimeric partner
- G387 (= G366) 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 (= Y368) binding
4zgyA Structure of human ornithine decarboxylase in complex with a c- terminal fragment of antizyme (see paper)
32% identity, 80% coverage: 60:380/400 of query aligns to 41:363/383 of 4zgyA
- active site: K45 (= K64), H170 (= H194), E247 (= E269)
- binding magnesium ion: G210 (= G231), F211 (= F232), R250 (= R272), Y251 (≠ A273)
- binding pyridoxal-5'-phosphate: K45 (= K64), D64 (= D84), H170 (= H194), G210 (= G231), E247 (= E269), G249 (= G271), R250 (= R272), Y353 (= Y368)
2plkA Crystal structure of lysine/ornithine decarboxylase complexed with cadaverine from vibrio vulnificus (see paper)
32% identity, 89% coverage: 35:389/400 of query aligns to 26:369/370 of 2plkA
P07805 Ornithine decarboxylase; ODC; EC 4.1.1.17 from Trypanosoma brucei brucei (see 3 papers)
32% identity, 80% coverage: 60:380/400 of query aligns to 63:399/423 of P07805
- K67 (= K64) modified: N6-(pyridoxal phosphate)lysine
- S198 (= S197) binding
- G235 (= G231) binding
- EPGR 272:275 (= EPGR 269:272) binding
- YD 329:330 (≠ WR 311:312) binding in other chain
- C358 (= C338) 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 (= D339) binding
- Y387 (= Y368) binding
2todA Ornithine decarboxylase from trypanosoma brucei k69a mutant in complex with alpha-difluoromethylornithine (see paper)
33% identity, 80% coverage: 60:380/400 of query aligns to 29:344/353 of 2todA
- active site: A33 (≠ K64), H153 (= H194), E230 (= E269)
- binding alpha-difluoromethylornithine: D275 (≠ A306), C303 (= C338), D304 (= D339), Y332 (= Y368), F340 (= F376)
- binding pyridoxal-5'-phosphate: H153 (= H194), S156 (= S197), G192 (= G230), G193 (= G231), E230 (= E269), G232 (= G271), R233 (= R272), Y332 (= Y368)
1szrC A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
32% identity, 80% coverage: 60:380/400 of query aligns to 29:340/347 of 1szrC
1szrA A dimer interface mutant of ornithine decarboxylase reveals structure of gem diamine intermediate (see paper)
32% identity, 80% coverage: 60:380/400 of query aligns to 29:337/345 of 1szrA
1njjA Crystal structure determination of t. Brucei ornithine decarboxylase bound to d-ornithine and to g418 (see paper)
32% identity, 77% coverage: 60:368/400 of query aligns to 38:334/349 of 1njjA
- active site: K42 (= K64), H160 (= H194), E237 (= E269)
- binding geneticin: D206 (≠ P241), L287 (vs. gap), L327 (≠ E361), E329 (≠ G363), D330 (≠ Q364)
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A40 (= A62), K42 (= K64), H160 (= H194), G199 (= G230), G200 (= G231), E237 (= E269), G239 (= G271), R240 (= R272), Y279 (≠ I318), D280 (≠ K319), Y334 (= Y368)
Sites not aligning to the query:
2nv9B The x-ray crystal structure of the paramecium bursaria chlorella virus arginine decarboxylase (see paper)
29% identity, 80% coverage: 61:379/400 of query aligns to 45:364/372 of 2nv9B
- active site: K48 (= K64), H176 (= H194), E252 (= E269)
- binding pyridoxal-5'-phosphate: K48 (= K64), D67 (= D84), H176 (= H194), S179 (= S197), G215 (= G230), G216 (= G231), E252 (= E269), G254 (= G271), R255 (= R272), Y353 (= Y368)
2nvaA The x-ray crystal structure of the paramecium bursaria chlorella virus arginine decarboxylase bound to agmatine (see paper)
29% identity, 80% coverage: 61:379/400 of query aligns to 45:361/369 of 2nvaA
- active site: K48 (= K64), H176 (= H194), E249 (= E269)
- binding (4-{[(4-{[amino(imino)methyl]amino}butyl)amino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: D67 (= D84), L145 (= L165), H176 (= H194), S179 (= S197), G215 (= G230), G216 (= G231), E249 (= E269), G251 (= G271), R252 (= R272), E293 (≠ L309), C321 (= C338), D322 (= D339), Y350 (= Y368)
Q9FPK5 Ornithine decarboxylase, chloroplastic; Lysine decarboxylase; EC 4.1.1.17; EC 4.1.1.18 from Nicotiana glutinosa (Tobacco) (see paper)
31% identity, 80% coverage: 60:380/400 of query aligns to 91:418/432 of Q9FPK5
- K95 (= K64) mutation to A: Loss of activity.
- C96 (= C65) mutation to A: Almost unchanged activity.
- C338 (vs. gap) mutation to A: Loss of activity.
- C377 (= C338) mutation to A: Loss of activity.
Query Sequence
>WP_011383514.1 NCBI__GCF_000009985.1:WP_011383514.1
MTVARYHARTRSLFGSTGALPSVRAAVLALRPEVPMLCLRPAKASREAARFVDSFPGQVL
YAVKCNPDEAVLRALAAGGIGHFDAASIAEVRLVRRLFPEAGIHFMHPVKARSAIREAYG
LHGVRDFVLDGAGELDKIVAETEGASDLRLIVRLGLAKGDARLDLSGKFGASADDAVRLL
RRCAAVGRVGLSFHVGSQCCDPSAWERALAQADAVIRAAAIQLDVLDVGGGFPVAYPGMR
PPPLAAFMAAIRRGVARMGLPSGCVLWCEPGRALVAGCQSLVVQVQARRGDMLFINDGVY
GTLSDAGALAWRYPCRLIKAAGASHETLQAFGFFGPTCDSLDRMPGPFLLPADTAEGDWI
EIGQLGAYGACLRTGFNGFNDLLRVEVGEPAVPSQASRAA
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