SitesBLAST
Comparing 8499899 FitnessBrowser__Miya:8499899 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)
Q58497 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
26% identity, 90% coverage: 37:462/474 of query aligns to 16:433/438 of Q58497
- K73 (= K90) modified: N6-(pyridoxal phosphate)lysine
- S217 (= S221) binding
- G254 (= G259) binding
- EPGR 294:297 (= EPGR 322:325) binding
- Y391 (= Y421) binding
1twiA Crystal structure of diaminopimelate decarboxylase from m. Jannaschii in co-complex with l-lysine (see paper)
26% identity, 90% coverage: 37:462/474 of query aligns to 12:429/434 of 1twiA
- active site: K69 (= K90), H210 (≠ N218), E290 (= E322)
- binding lysine: S213 (= S221), R293 (= R325), R329 (≠ F362), Y333 (≠ F366), Y387 (= Y421)
- binding pyridoxal-5'-phosphate: A67 (≠ S88), K69 (= K90), D88 (≠ E109), N111 (= N132), H210 (≠ N218), S213 (= S221), G250 (= G259), E290 (= E322), G292 (= G324), R293 (= R325), Y387 (= Y421)
1tufA Crystal structure of diaminopimelate decarboxylase from m. Jannaschi (see paper)
26% identity, 90% coverage: 37:462/474 of query aligns to 12:429/434 of 1tufA
8d5dA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- arginine (see paper)
28% identity, 89% coverage: 37:460/474 of query aligns to 27:453/458 of 8d5dA
- binding (E)-N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-D-arginine: K79 (= K90), H208 (≠ N218), D211 (≠ S221), G249 (= G259), E297 (= E322), G299 (= G324), R300 (= R325), D346 (≠ F362), F350 (= F366), C377 (= C392), D378 (≠ T393), Y412 (= Y421)
8d5rA Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- ornithine (see paper)
27% identity, 89% coverage: 37:460/474 of query aligns to 28:455/461 of 8d5rA
- binding n~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-d-ornithine: A78 (≠ S88), K80 (= K90), H210 (≠ N218), D213 (≠ S221), G251 (= G259), E299 (= E322), G301 (= G324), R302 (= R325), Y414 (= Y421)
- binding 1,4-diaminobutane: Q350 (≠ C364), H351 (≠ D365), D353 (≠ E367)
8d88A Structure of y430f d-ornithine/d-lysine decarboxylase complex with d- lysine (see paper)
27% identity, 89% coverage: 37:460/474 of query aligns to 28:457/461 of 8d88A
- binding pentane-1,5-diamine: Q352 (≠ C364), H353 (≠ D365), D355 (≠ E367)
- binding N~2~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-D-lysine: A78 (≠ S88), K80 (= K90), H212 (≠ N218), D215 (≠ S221), G253 (= G259), E301 (= E322), G303 (= G324), R304 (= R325), Y416 (= Y421)
8d4iA Structure of y430f d-ornithine/d-lysine decarboxylase complex with putrescine (see paper)
27% identity, 89% coverage: 37:460/474 of query aligns to 28:457/462 of 8d4iA
7kh2D Structure of n-citrylornithine decarboxylase bound with plp (see paper)
23% identity, 90% coverage: 26:451/474 of query aligns to 1:412/415 of 7kh2D
P9WIU7 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
26% identity, 90% coverage: 34:460/474 of query aligns to 19:445/447 of P9WIU7
- K72 (= K90) modified: N6-(pyridoxal phosphate)lysine
- C93 (≠ I111) modified: Interchain (with C-375)
- G258 (≠ Y276) binding
- EPGR 300:303 (= EPGR 322:325) binding
- C375 (= C392) modified: Interchain (with C-72)
- Y405 (= Y421) binding
1hkvA Mycobacterium diaminopimelate dicarboxylase (lysa) (see paper)
26% identity, 90% coverage: 34:460/474 of query aligns to 18:444/446 of 1hkvA
- binding lysine: E375 (≠ T393), S376 (≠ R394)
- binding pyridoxal-5'-phosphate: A69 (≠ S88), K71 (= K90), R160 (= R178), H210 (= H216), H212 (≠ N218), G256 (≠ L275), G257 (≠ Y276), E299 (= E322), G301 (= G324), R302 (= R325), Y404 (= Y421)
6n2aA Meso-diaminopimelate decarboxylase from arabidopsis thaliana (isoform 1)
25% identity, 84% coverage: 56:453/474 of query aligns to 31:412/422 of 6n2aA
- binding lysine: K63 (= K90), R281 (= R325), R317 (≠ F362), Y321 (≠ H369), C349 (= C392), E350 (≠ T393), Y378 (= Y421)
- binding pyridoxal-5'-phosphate: K63 (= K90), H202 (≠ N218), S205 (= S221), G242 (= G259), E278 (= E322), G280 (= G324), R281 (= R325), Y378 (= Y421)
5gjpA Crystal structure of srldc in complex with plp and cadaverine (see paper)
29% identity, 85% coverage: 49:452/474 of query aligns to 14:376/381 of 5gjpA
- active site: K51 (= K90), H171 (≠ N218), E247 (= E322)
- binding pentane-1,5-diamine: Y290 (≠ E367), D291 (≠ W368), Y344 (= Y421)
- binding pyridoxal-5'-phosphate: A49 (≠ S88), K51 (= K90), H171 (≠ N218), S174 (= S221), G211 (= G259), E247 (= E322), G249 (= G324), R250 (= R325), Y344 (= Y421)
O50657 Lysine/ornithine decarboxylase; LDC; EC 4.1.1.17; EC 4.1.1.18 from Selenomonas ruminantium (see paper)
28% identity, 85% coverage: 49:452/474 of query aligns to 14:384/393 of O50657
- AGV 44:46 (≠ AML 83:85) 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 (≠ C93) 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 (≠ T388) mutation to W: 7-fold increase in substrate specificity towards ornithine.
- S322 (≠ V391) 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 (≠ S395) 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 (= G419) mutation to D: Loss of dimer formation and decarboxylase activity.
5gjoA Crystal structure of srldc mutant (a225c/t302c) in complex with plp (see paper)
28% identity, 85% coverage: 49:452/474 of query aligns to 15:385/385 of 5gjoA
- active site: K52 (= K90), H180 (≠ N218), E256 (= E322)
- binding pyridoxal-5'-phosphate: A50 (≠ S88), K52 (= K90), D71 (≠ E109), H180 (≠ N218), S183 (= S221), G219 (= G258), G220 (= G259), E256 (= E322), G258 (= G324), R259 (= R325), Y353 (= Y421)
5gjnA Crystal structure of lysine decarboxylase from selenomonas ruminantium in p43212 space group (see paper)
28% identity, 83% coverage: 49:441/474 of query aligns to 14:362/369 of 5gjnA
B4XMC6 Diaminopimelate decarboxylase; DAP decarboxylase; DAPDC; EC 4.1.1.20 from Helicobacter pylori (Campylobacter pylori) (see paper)
25% identity, 89% coverage: 48:467/474 of query aligns to 6:405/405 of B4XMC6
- K46 (= K90) 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 (= G259) binding
- EPGR 259:262 (= EPGR 322:325) binding
- Y358 (= Y421) binding
5x7mA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
24% identity, 92% coverage: 26:460/474 of query aligns to 9:442/443 of 5x7mA
5x7nA Crystal structure of meso-diaminopimelate decarboxylase (dapdc) from corynebacterium glutamicum (see paper)
24% identity, 92% coverage: 26:460/474 of query aligns to 9:442/442 of 5x7nA
- binding lysine: K73 (= K90), R341 (≠ F362), Y345 (≠ F366), Y402 (= Y421), M406 (= M427)
- binding pyridoxal-5'-phosphate: K73 (= K90), H115 (≠ N132), H214 (≠ N218), G254 (= G258), G255 (= G259), E297 (= E322), G299 (= G324), R300 (= R325), Y402 (= Y421)
7ru7A Crystal structure of btrk, a decarboxylase involved in butirosin biosynthesis
21% identity, 85% coverage: 47:450/474 of query aligns to 9:400/412 of 7ru7A
2yxxA Crystal structure analysis of diaminopimelate decarboxylate (lysa)
26% identity, 85% coverage: 48:451/474 of query aligns to 5:374/385 of 2yxxA
- active site: K45 (= K90), H178 (≠ G257), E245 (= E322)
- binding pyridoxal-5'-phosphate: K45 (= K90), D64 (≠ E109), H178 (≠ G257), S181 (vs. gap), G213 (≠ A286), E245 (= E322), G247 (= G324), R248 (= R325), Y342 (= Y421)
Query Sequence
>8499899 FitnessBrowser__Miya:8499899
MSVLGGIGGVLRRFSCLRQKRQGKPPLSLWDVTDEGGVLAVGGMPCTRLARDYGTPLLVV
DAAALRRRVQDVQAALDEVLPGAMLAYSYKTNCIPGILRMLHDAGVGAEVISPYEYWLSE
SLGVDGGQVVYNGVDKSRESIARAVARGTLVNIDSRDEVDVVLAAAREQRRTARVGLRLA
LNRSAQFGLDPEGDDLAHVVRNCLDAPDHADLVALHFNVTSNARHSGYHARCLSRALDVM
SWLAREHGVRIRLLDVGGGFGVETSKNMSGAEYGLYRLFGVQPGAAWMDPFQDFRLYLRD
LADTLRAFCAQNDLPVPGVCIEPGRLLTSKAELLLTQVKAVKERPGAEPFAITDAGRLSQ
AFPCDFEWHEAFLASDLRRPPSRPYTVTGRVCTRSDWLYRGKLLPELATGDVLAVMDAGA
YFSSYAMNFAFPRAAVVAVEDGRARVLRRREDFRHLVGMDDVALADVTWDGGER
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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