SitesBLAST
Comparing WP_009544757.1 NCBI__GCF_000017845.1:WP_009544757.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 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 PCC 6803 / Kazusa) (see paper)
80% identity, 100% coverage: 1:703/703 of query aligns to 1:705/705 of P74535
- N22 (= N22) binding L-arginine; binding L-ornithine; mutation to A: Significant loss of arginine dihydrolase activity.
- D65 (= D65) mutation to A: Significant loss of arginine dihydrolase activity.
- F68 (= F68) mutation to A: Significant loss of arginine dihydrolase activity.
- N71 (= N71) binding L-arginine; binding L-ornithine; mutation to D: Produces equal trace amounts of citrulline and ornithine.; mutation to S: Transforms the enzyme from a dihydrolase to a deiminase.
- R90 (= R90) binding L-arginine; binding L-ornithine; mutation to A: Significant loss of arginine dihydrolase activity.
- E118 (= E118) mutation to A: Complete loss of arginine dihydrolase activity.
- R139 (= R139) binding L-arginine; binding L-ornithine; mutation to A: Significant loss of arginine dihydrolase activity.
- Y167 (= Y167) mutation to A: Significant loss of arginine dihydrolase activity.
- H168 (= H168) binding L-arginine; binding L-ornithine; mutation to F: Complete loss of arginine dihydrolase activity.
- D170 (= D170) binding L-arginine
- A258 (= A258) binding L-arginine; binding L-ornithine
- C264 (= C264) binding covalent; binding L-ornithine; mutation to S: Complete loss of arginine dihydrolase activity.
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)
75% identity, 99% coverage: 1:697/703 of query aligns to 1:698/703 of Q8YMD9
- N22 (= N22) binding L-arginine; binding L-ornithine; mutation to A: Loss of arginine dihydrolase activity.
- D65 (= D65) binding L-arginine; mutation to A: Shows residual arginine dihydrolase activity.
- N71 (= N71) binding L-arginine; mutation N->A,D: Shows residual arginine dihydrolase activity.
- R90 (= R90) binding L-arginine; binding L-ornithine; mutation to A: Loss of arginine dihydrolase activity.
- E118 (= E118) mutation to A: Loss of arginine dihydrolase activity.
- D122 (= D122) mutation D->A,N: Loss of arginine dihydrolase activity.
- R139 (= R139) binding L-arginine; binding L-ornithine; mutation to A: Shows residual arginine dihydrolase activity.
- Y167 (= Y167) mutation to F: Retains 9% of arginine dihydrolase activity.
- H168 (= H168) binding L-ornithine; mutation to A: Loss of arginine dihydrolase activity.
- D170 (= D170) binding L-arginine; mutation D->A,N: Loss of arginine dihydrolase activity.
- N219 (= N219) mutation to A: Loss of arginine dihydrolase activity.
- A258 (= A258) binding L-arginine
- C264 (= C264) binding L-ornithine; mutation to A: Loss of arginine dihydrolase activity.
- N524 (= N523) binding NAD(+)
- A525 (= A524) binding NAD(+)
- D603 (= D602) binding NAD(+)
- S635 (≠ T634) binding NAD(+)
- M636 (= M635) binding NAD(+)
- L637 (= L636) binding NAD(+)
- H638 (= H637) binding NAD(+)
- D656 (= D655) binding NAD(+)
- D679 (= D678) binding NAD(+)
- V680 (= V679) binding NAD(+)
6lrgB Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
75% identity, 98% coverage: 5:694/703 of query aligns to 2:681/681 of 6lrgB
6lrgA Crystal structure of the ternary complex of agre with ornithine and NAD+ (see paper)
74% identity, 99% coverage: 2:697/703 of query aligns to 1:678/678 of 6lrgA
- binding nicotinamide-adenine-dinucleotide: P477 (= P496), V478 (= V497), G503 (= G522), N504 (= N523), A505 (= A524), H537 (= H556), S579 (= S598), R581 (= R600), D582 (= D601), D583 (= D602), S614 (= S633), S615 (≠ T634), M616 (= M635), H618 (= H637), D636 (= D655), I637 (= I656), D659 (= D678), V660 (= V679)
- binding L-ornithine: I20 (= I21), D64 (= D65), F67 (= F68), N70 (= N71), R89 (= R90), R138 (= R139), Y166 (= Y167), H167 (= H168), C263 (= C264)
6lrhA Crystal structure of the binary complex of agre c264a mutant with l- arginine (see paper)
73% identity, 99% coverage: 2:696/703 of query aligns to 1:675/675 of 6lrhA
- binding arginine: I20 (= I21), D64 (= D65), F67 (= F68), N70 (= N71), R89 (= R90), R138 (= R139), Y166 (= Y167), H167 (= H168), D169 (= D170), A257 (= A258), A263 (≠ C264)
6jv0A Crystal structure of n-terminal domain of argz, bound to product, an arginine dihydrolase from the ornithine-ammonia cycle in cyanobacteria (see paper)
81% identity, 39% coverage: 3:274/703 of query aligns to 1:272/273 of 6jv0A
- binding L-ornithine: I19 (= I21), M23 (= M25), D63 (= D65), F66 (= F68), N69 (= N71), R88 (= R90), R137 (= R139), Y165 (= Y167), H166 (= H168), A256 (= A258), C262 (= C264)
6juzA Crystal structure of n-terminal domain of argz(n71s) covalently bond to a reaction intermediate (see paper)
81% identity, 38% coverage: 5:274/703 of query aligns to 2:271/272 of 6juzA
Q9I4E3 N(G),N(G)-dimethylarginine dimethylaminohydrolase; DDAH; Dimethylarginine dimethylaminohydrolase; Dimethylargininase; EC 3.5.3.18 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 2 papers)
22% identity, 35% coverage: 20:268/703 of query aligns to 14:253/254 of Q9I4E3
- E114 (≠ P116) mutation to Q: Abolishes enzyme activity.
- H162 (= H168) mutation H->G,F: Abolishes enzyme activity.
- C249 (= C264) mutation to S: Abolishes enzyme activity.
3rhyA Crystal structure of the dimethylarginine dimethylaminohydrolase adduct with 4-chloro-2-hydroxymethylpyridine (see paper)
22% identity, 34% coverage: 28:268/703 of query aligns to 16:247/248 of 3rhyA
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)
41% identity, 11% coverage: 288:361/703 of query aligns to 482:552/1064 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.
1h70A Ddah from pseudomonas aeruginosa. C249s mutant complexed with citrulline (see paper)
21% identity, 35% coverage: 20:268/703 of query aligns to 15:254/255 of 1h70A
- binding citrulline: L19 (≠ W24), D61 (= D65), F64 (= F68), E66 (≠ A70), D67 (≠ N71), R86 (= R90), R133 (= R139), H163 (= H168), I244 (≠ A258), D245 (≠ G259), S250 (≠ C264)
Query Sequence
>WP_009544757.1 NCBI__GCF_000017845.1:WP_009544757.1
MTDPIRILMCAPDHYDVDYVINPWMEGNIHKSTRDRSVEQWNQLYHAIKERAIVELVEPQ
KGWPDMVFTANAGLVLGDNAIVSRFYHKERQGEEPYFKEWFAANGFNVYELPKDLPFEGA
GDALFDREGRWLWAGYGFRSELDSHPYIAQWLDTEVLSLRLIDERFYHLDTCFCPLTGGY
LLYYPPAFDAYSNRLIELRIPQDKRIVVEEPDAVKFACNAVNINHTIIMNQISDSLKQRL
NEVGFEVVQTPLSEFLKAGGAAKCLTLRVNEPVLEEVHASTPVESRTIQLTGHLLDAGIM
NKALDMIVENGGSFKVLNFELGLERQSTSAAEVRVSAPDHDVMEEIMTQLIDLGAVAPPQ
EVCDINTETVTKAGVAPDDFYVSTIYPTEVRVNCEWVKVQNQRMDAAIVVDPQKMTAECK
LLRDLAVGDRVMVGFDGIRTVRQVEDRDQRNGKKEFTFMGSGVSSERRVELLVEQIAWEM
RQVRDQGGKVVVTAGPVVIHTGGAQHLAKLIREGYVHALLGGNAIAVHDIEQAMMGTSLG
VDMQRGIPVSGGHRHHLKVINTVRRYGSIAQAVEQGAISKGVMYECVKHNVPFVLAGSIR
DDGPLPDTEMDLIKAQSRYAELIQGTDMILMLSTMLHSIGVGNMTPAGVKMVCVDINPAV
VTKLSDRGSVESVGIVTDVGLFLSLLVQQLDKLTHPYPLVGTV
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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