SitesBLAST
Comparing WP_089303086.1 NCBI__GCF_900188115.1:WP_089303086.1 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)
6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
69% identity, 92% coverage: 26:466/481 of query aligns to 1:441/454 of 6ienB
- binding argininosuccinate: S97 (= S122), R98 (= R123), N99 (= N124), T144 (= T169), H145 (= H170), S266 (= S291), S267 (= S292), M269 (= M294), K272 (= K297), Y306 (= Y331), Q311 (= Q336), K314 (= K339)
6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
69% identity, 92% coverage: 26:466/481 of query aligns to 1:439/452 of 6ienA
- binding argininosuccinate: R98 (= R123), N99 (= N124), V102 (= V127), T144 (= T169), H145 (= H170), Y304 (= Y331), Q309 (= Q336), K312 (= K339)
- binding fumaric acid: S266 (= S291), S267 (= S292), K270 (= K297), N272 (= N299)
6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
64% identity, 92% coverage: 26:466/481 of query aligns to 1:405/418 of 6ienC
- binding arginine: R98 (= R123), N99 (= N124), V102 (= V127), Y306 (= Y331), Q311 (= Q336), K314 (= K339)
- binding argininosuccinate: T144 (= T169), H145 (= H170), S266 (= S291), S267 (= S292), M269 (= M294), K272 (= K297)
- binding fumaric acid: S97 (= S122), R98 (= R123), N99 (= N124)
P24058 Argininosuccinate lyase; ASAL; Arginosuccinase; Delta crystallin II; Delta-2 crystallin; EC 4.3.2.1 from Anas platyrhynchos (Mallard) (Anas boschas) (see 4 papers)
44% identity, 94% coverage: 16:467/481 of query aligns to 9:458/468 of P24058
- W11 (= W18) mutation to A: 98% decrease in catalytic efficiency.; mutation to F: 90% decrease in catalytic efficiency.; mutation to M: 99% decrease in catalytic efficiency.; mutation to R: 97% decrease in catalytic efficiency.; mutation to Y: 50% decrease in catalytic efficiency.
- S29 (= S36) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
- D33 (= D40) mutation to N: 99% decrease in catalytic efficiency.
- D89 (= D96) mutation to N: Loss of activity.
- N116 (= N124) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
- D117 (= D125) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
- T161 (= T169) binding in chain C; mutation to A: Loss of activity.; mutation to D: Loss of activity.; mutation to S: 30% decrease in catalytic efficiency.; mutation to V: Loss of activity.
- H162 (= H170) mutation to E: Loss of activity.
- R238 (= R246) mutation to Q: Loss of activity.
- T281 (= T289) mutation to V: 80% decrease in catalytic efficiency.
- S283 (= S291) mutation to A: Loss of activity.; mutation to C: Loss of activity.; mutation to D: Loss of activity.; mutation to H: Loss of activity.; mutation to T: Loss of activity.
- N291 (= N299) binding in chain B; mutation to L: Loss of activity.
- D293 (= D301) mutation to N: 99% decrease in catalytic efficiency.
- E296 (= E304) mutation to D: Loss of activity.
- Y323 (= Y331) binding in chain A
- K325 (≠ R333) mutation to N: 99% decrease in catalytic efficiency.
- Q328 (= Q336) binding in chain A
- D330 (= D338) mutation to N: Loss of activity.
- K331 (= K339) binding in chain A; mutation to Q: Loss of activity.
1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
44% identity, 91% coverage: 30:467/481 of query aligns to 6:441/450 of 1k7wD
- active site: E71 (= E95), T144 (= T169), H145 (= H170), A266 (≠ S291), S267 (= S292), K272 (= K297), E279 (= E304)
- binding argininosuccinate: R98 (= R123), N99 (= N124), V102 (= V127), T144 (= T169), H145 (= H170), Y306 (= Y331), Q311 (= Q336), K314 (= K339)
1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
43% identity, 91% coverage: 30:467/481 of query aligns to 4:439/447 of 1hy0A
P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
43% identity, 96% coverage: 6:467/481 of query aligns to 2:456/464 of P04424
- R12 (= R21) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
- D31 (= D40) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
- K51 (≠ S60) mutation to N: 2-fold reduction in activity.
- K69 (≠ Q78) modified: N6-acetyllysine
- E73 (≠ D82) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
- D87 (= D96) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
- H89 (= H98) mutation to Q: 10-fold reduction in activity.
- R94 (= R103) to C: in ARGINSA; severe; dbSNP:rs374304304
- R95 (≠ G104) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
- R113 (= R123) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
- D120 (≠ Q130) to E: in ARGINSA; severe
- V178 (≠ Q188) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
- T181 (≠ L191) to S: in a breast cancer sample; somatic mutation
- R182 (= R192) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
- R186 (= R196) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
- G200 (= G210) to V: in a breast cancer sample; somatic mutation
- R236 (= R246) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
- D237 (= D247) to N: in ARGINSA; severe; dbSNP:rs552951774
- Q286 (= Q296) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
- K288 (= K298) modified: N6-acetyllysine; mutation to R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure.
- R297 (= R307) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
- R306 (≠ N316) to W: in ARGINSA; severe; dbSNP:rs868834862
- Q326 (= Q336) to L: in ARGINSA; severe
- V335 (≠ S345) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
- M360 (= M370) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
- M382 (≠ V393) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
- R385 (= R396) to L: in ARGINSA; severe
- H388 (= H399) to Q: in ARGINSA; severe
- A398 (= A409) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
- R456 (= R467) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688
2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
46% identity, 92% coverage: 25:468/481 of query aligns to 1:445/450 of 2e9fB
- active site: E71 (= E95), T146 (= T169), H147 (= H170), S268 (= S291), S269 (= S292), K274 (= K297), E281 (= E304)
- binding arginine: R98 (= R123), N99 (= N124), V102 (= V127), Y308 (= Y331), Q313 (= Q336), K316 (= K339)
P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
41% identity, 94% coverage: 16:467/481 of query aligns to 7:456/466 of P02521
Sites not aligning to the query:
- 2 modified: Blocked amino end (Ala)
1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
43% identity, 92% coverage: 21:461/481 of query aligns to 1:441/451 of 1tj7B
6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
33% identity, 90% coverage: 46:476/481 of query aligns to 38:467/496 of 6g3iA
Sites not aligning to the query:
6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
33% identity, 90% coverage: 46:476/481 of query aligns to 38:467/497 of 6g3hA
Sites not aligning to the query:
6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
33% identity, 90% coverage: 46:476/481 of query aligns to 38:467/497 of 6g3gA
6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
33% identity, 90% coverage: 46:476/481 of query aligns to 38:467/497 of 6g3fA
3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
23% identity, 65% coverage: 117:427/481 of query aligns to 132:450/463 of 3r6vG
3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
23% identity, 65% coverage: 117:427/481 of query aligns to 131:449/462 of 3r6qA
Q9X0I0 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; EC 4.3.2.2 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
24% identity, 62% coverage: 104:401/481 of query aligns to 72:374/431 of Q9X0I0
- H141 (= H170) active site, Proton donor/acceptor
4adlA Crystal structures of rv1098c in complex with malate (see paper)
31% identity, 35% coverage: 151:316/481 of query aligns to 160:335/459 of 4adlA
Sites not aligning to the query:
P9WN93 Fumarate hydratase class II; Fumarase C; Aerobic fumarase; Iron-independent fumarase; EC 4.2.1.2 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
31% identity, 35% coverage: 151:316/481 of query aligns to 168:343/474 of P9WN93
- T186 (= T169) binding
- S318 (= S291) active site; mutation S->A,C: Absence of fumarase activity.
- S319 (= S292) binding
- KVN 324:326 (≠ KKN 297:299) binding
Sites not aligning to the query:
- 104:106 binding
- 138:140 binding
4apbD Crystal structure of mycobacterium tuberculosis fumarase (rv1098c) s318c in complex with fumarate (see paper)
30% identity, 35% coverage: 151:316/481 of query aligns to 160:335/462 of 4apbD
Sites not aligning to the query:
Query Sequence
>WP_089303086.1 NCBI__GCF_900188115.1:WP_089303086.1
MTGSGSTESGEVGPVQLWGGRFASGPAEAMAALSASTHFDWRLARHDIAGSRAHARVLRS
AGLLTEGELTGLLAALDQLESDVVSGTFTPTVADEDVHTALERGLLERAGSDLGGKLRAG
RSRNDQVATQMRMWLRDAARGVAQGTLAVVDALTAQAERHPDAVLPGRTHLQHAQPVLLA
HHLLAHAQALLRDVDRLRDWDRRTDESPYGSGALAGSSLDLDPDAVATELGFARAVDNSI
DGVASRDFAAEFAFAVAMLGVNLSRIAEEVIIWNTAEFGYVTLDDAWATGSSIMPQKKNP
DVAELTRGKAGRLIGNLSGLLATLKAQTLAYNRDLQEDKEPLFDSVEQLELLLPAIAGMI
DTMAFHTERMAELAPAGFTLATDIAEWLVRKGVAFRRAHEISGECVRVAERNGAGLDELT
DEELGAIDPQLTPEVREVLTVAGSIASRDARGGTAPPRVAEQLDGVRRRSAGARAWAVGD
S
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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