SitesBLAST
Comparing WP_084057564.1 NCBI__GCF_900176285.1:WP_084057564.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 5 hits to proteins with known functional sites (download)
P74535 Bifunctional arginine dihydrolase/ornithine cyclodeaminase ArgZ; EC 3.5.3.27; EC 4.3.1.12 from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa) (see paper)
35% identity, 92% coverage: 23:363/371 of query aligns to 365:694/705 of P74535
Sites not aligning to the query:
- 22 binding L-arginine; binding L-ornithine; N→A: Significant loss of arginine dihydrolase activity.
- 65 D→A: Significant loss of arginine dihydrolase activity.
- 68 F→A: Significant loss of arginine dihydrolase activity.
- 71 binding L-arginine; binding L-ornithine; N→D: Produces equal trace amounts of citrulline and ornithine.; N→S: Transforms the enzyme from a dihydrolase to a deiminase.
- 90 binding L-arginine; binding L-ornithine; R→A: Significant loss of arginine dihydrolase activity.
- 118 E→A: Complete loss of arginine dihydrolase activity.
- 139 binding L-arginine; binding L-ornithine; R→A: Significant loss of arginine dihydrolase activity.
- 167 Y→A: Significant loss of arginine dihydrolase activity.
- 168 binding L-arginine; binding L-ornithine; H→F: Complete loss of arginine dihydrolase activity.
- 170 binding L-arginine
- 258 binding L-arginine; binding L-ornithine
- 264 binding covalent; binding L-ornithine; C→S: Complete loss of arginine dihydrolase activity.
6lrgA Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
32% identity, 91% coverage: 28:363/371 of query aligns to 369:673/678 of 6lrgA
- binding nicotinamide-adenine-dinucleotide: P477 (≠ A157), V478 (= V158), G503 (= G183), N504 (= N184), A505 (= A185), H537 (= H217), S579 (= S259), R581 (= R261), D582 (= D262), D583 (= D263), S614 (≠ A294), S615 (≠ T295), M616 (≠ Q296), H618 (= H298), D636 (= D326), I637 (≠ M327), D659 (≠ N349), V660 (= V350)
Sites not aligning to the query:
Q8YMD9 Bifunctional arginine dihydrolase/ornithine cyclodeaminase AgrE; Arginine-guanidine removing enzyme; EC 3.5.3.27; EC 4.3.1.12 from Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576) (see paper)
33% identity, 91% coverage: 28:363/371 of query aligns to 370:693/703 of Q8YMD9
- N524 (= N184) binding NAD(+)
- A525 (= A185) binding NAD(+)
- D603 (= D263) binding NAD(+)
- S635 (≠ T295) binding NAD(+)
- M636 (≠ Q296) binding NAD(+)
- L637 (= L297) binding NAD(+)
- H638 (= H298) binding NAD(+)
- D656 (= D326) binding NAD(+)
- D679 (≠ N349) binding NAD(+)
- V680 (= V350) binding NAD(+)
Sites not aligning to the query:
- 22 binding L-arginine; binding L-ornithine; N→A: Loss of arginine dihydrolase activity.
- 65 binding L-arginine; D→A: Shows residual arginine dihydrolase activity.
- 71 binding L-arginine; mutation N->A,D: Shows residual arginine dihydrolase activity.
- 90 binding L-arginine; binding L-ornithine; R→A: Loss of arginine dihydrolase activity.
- 118 E→A: Loss of arginine dihydrolase activity.
- 122 mutation D->A,N: Loss of arginine dihydrolase activity.
- 139 binding L-arginine; binding L-ornithine; R→A: Shows residual arginine dihydrolase activity.
- 167 Y→F: Retains 9% of arginine dihydrolase activity.
- 168 binding L-ornithine; H→A: Loss of arginine dihydrolase activity.
- 170 binding L-arginine; mutation D->A,N: Loss of arginine dihydrolase activity.
- 219 N→A: Loss of arginine dihydrolase activity.
- 258 binding L-arginine
- 264 binding L-ornithine; C→A: Loss of arginine dihydrolase activity.
6lrgB Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
32% identity, 91% coverage: 28:363/371 of query aligns to 367:679/681 of 6lrgB
Sites not aligning to the query:
6lrhA Crystal structure of the binary complex of agre c264a mutant with l- arginine (see paper)
32% identity, 91% coverage: 28:363/371 of query aligns to 369:671/675 of 6lrhA
Sites not aligning to the query:
- binding arginine: 20, 64, 67, 70, 89, 138, 166, 167, 169, 257, 263
Query Sequence
>WP_084057564.1 NCBI__GCF_900176285.1:WP_084057564.1
MFRLPQYSPPDFSDPRFAQAPLVTFREVRKAGVAPEGYHATSVFPEYFHVAPGRWEILRE
SRMDCVVVQRPDGRLDVVEFRRLQPGDRVAVGRRENAEEGIFVHAEAFQGMSGTGDKFAF
RTRLTRETSFSIDYDEFYDLLVHERNHGTIVWVLGPAVVFDQDARSAFSSLIRRGYVHAL
LAGNALATHDLEGALFGTALGQEIYSKRSAPLGHYHHLDAINRLRELGSIEEAMQRGVVT
DGVMHAAVTQGIPVVLAGSIRDDGPLPGVIADVYEAQDRMRDQVRRATTVVALATQLHAI
ATGNMAPSYRVLDDGTVRPVYFYSVDMSEFAVQKLANRGSLTARSILTNVQDFMVTVERG
LRRRETNEEIA
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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