SitesBLAST
Comparing WP_010876500.1 NCBI__GCF_000008645.1:WP_010876500.1 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 6 hits to proteins with known functional sites (download)
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)
43% identity, 99% coverage: 1:407/411 of query aligns to 283:695/703 of Q8YMD9
- N524 (= N236) binding NAD(+)
- A525 (= A237) binding NAD(+)
- D603 (= D315) binding NAD(+)
- S635 (≠ T347) binding NAD(+)
- M636 (= M348) binding NAD(+)
- L637 (= L349) binding NAD(+)
- H638 (= H350) binding NAD(+)
- D656 (= D368) binding NAD(+)
- D679 (= D391) binding NAD(+)
- V680 (= V392) 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.
P74535 Bifunctional arginine dihydrolase/ornithine cyclodeaminase ArgZ; EC 3.5.3.27; EC 4.3.1.12 from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 283:696/705 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.
6lrgB Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 280:681/681 of 6lrgB
Sites not aligning to the query:
6lrgA Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 282:675/678 of 6lrgA
- binding nicotinamide-adenine-dinucleotide: P477 (= P209), V478 (≠ A210), G503 (= G235), N504 (= N236), A505 (= A237), H537 (= H269), S579 (= S311), R581 (= R313), D582 (= D314), D583 (= D315), S614 (≠ A346), S615 (≠ T347), M616 (= M348), H618 (= H350), D636 (= D368), I637 (= I369), D659 (= D391), V660 (= V392)
Sites not aligning to the query:
6lrhA Crystal structure of the binary complex of agre c264a mutant with l- arginine (see paper)
42% identity, 99% coverage: 1:407/411 of query aligns to 282:673/675 of 6lrhA
Sites not aligning to the query:
- binding arginine: 20, 64, 67, 70, 89, 138, 166, 167, 169, 257, 263
Q9SMZ4 Alpha-aminoadipic semialdehyde synthase; cAt-LKR/SDH; LKR/SDH; EC 1.5.1.8; EC 1.5.1.9 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
31% identity, 16% coverage: 6:72/411 of query aligns to 482:548/1064 of Q9SMZ4
Sites not aligning to the query:
- 238 modified: Phosphothreonine; mutation T->A,D: No effect on LKR and SDH activity.
- 407 S→A: No effect on LKR and SDH activity.; S→D: No LKR activity, but no effect on SDH activity.
- 458 modified: Phosphoserine; S→A: Reduced LKR activity, but no effect on SDH activity.; S→D: No effect on LKR and SDH activity.
- 551:554 NEDY→IEGR: Loss of LKR activity stimulation by NaCl.
Query Sequence
>WP_010876500.1 NCBI__GCF_000008645.1:WP_010876500.1
MNTREVELRGHIIDSLILPRALDIIMDMGGDFQILEIDIGKRKSDPSHARILVEAETPSL
LNQILDELGEIGASIAEIKEAELRRAPMDRVLPDDFYSTTNHQTFIYHGGEWVEVEGIEM
DCMIVVDPESRTARCKPIREIKKGDLVVVGREGIKVVPPERPRGKQGVFEFMGSEVSSEK
PLVTTIKKIASEITEIKKRGGRIGLVGGPAIVHTGSAPVIAEMIRLGFIDVLFAGNALAT
HDIECALYGTSLGVDIDRGEAVSRGHRHHINAINEINRAGSIRDAVEQGVLTSGIMYECV
KNDVPFVLAGSIRDDGPLPDVITDVMEAQNEMRKYVQDLDMVIMIATMLHSIATGNILPS
RVKTICVDINPATVTKLSDRGSSQAVSVVTDVGAFIPILLHEIKKMNGLGD
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