SitesBLAST

Comparing WP_012590227.1 NCBI__GCF_000021745.1:WP_012590227.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

2e9fB Crystal structure of t.Th.Hb8 argininosuccinate lyase complexed with l-arginine
52% identity, 94% coverage: 13:452/466 of query aligns to 1:441/450 of 2e9fB

• active site: E71 (= E83), T146 (= T156), H147 (= H157), S268 (= S278), S269 (= S279), K274 (= K284), E281 (= E291)
• binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y308 (= Y318), Q313 (= Q323), K316 (= K326)

1tj7B Structure determination and refinement at 2.44 a resolution of argininosuccinate lyase from e. Coli (see paper)
50% identity, 95% coverage: 9:449/466 of query aligns to 1:441/451 of 1tj7B

• active site: H150 (= H157), S271 (= S278), K277 (= K284), E284 (= E291)
• binding phosphate ion: S271 (= S278), M274 (= M281), K277 (= K284)

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)
42% identity, 97% coverage: 3:453/466 of query aligns to 8:456/468 of P24058

• W11 (= W6) 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 (= S24) binding in chain A; mutation to A: 10% decrease in catalytic efficiency.
• D33 (= D28) mutation to N: 99% decrease in catalytic efficiency.
• D89 (= D84) mutation to N: Loss of activity.
• N116 (= N111) binding in chain A; mutation to D: 99% decrease in catalytic efficiency.
• D117 (= D112) mutation to A: 55% decrease in catalytic efficiency.; mutation to E: 58% decrease in catalytic efficiency.
• T161 (= T156) 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 (= H157) mutation to E: Loss of activity.
• R238 (= R233) mutation to Q: Loss of activity.
• T281 (= T276) mutation to V: 80% decrease in catalytic efficiency.
• S283 (= S278) 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 (= N286) binding in chain B; mutation to L: Loss of activity.
• D293 (= D288) mutation to N: 99% decrease in catalytic efficiency.
• E296 (= E291) mutation to D: Loss of activity.
• Y323 (= Y318) binding in chain A
• K325 (= K320) mutation to N: 99% decrease in catalytic efficiency.
• Q328 (= Q323) binding in chain A
• D330 (= D325) mutation to N: Loss of activity.
• K331 (= K326) binding in chain A; mutation to Q: Loss of activity.

P04424 Argininosuccinate lyase; ASAL; Arginosuccinase; EC 4.3.2.1 from Homo sapiens (Human) (see 12 papers)
42% identity, 99% coverage: 2:463/466 of query aligns to 5:464/464 of P04424

• R12 (= R9) to Q: in ARGINSA; 18-fold reduction in catalytic efficiency toward argininosuccinate; dbSNP:rs145138923
• D31 (= D28) to N: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs754995756
• K51 (≠ D48) mutation to N: 2-fold reduction in activity.
• K69 (≠ A66) modified: N6-acetyllysine
• E73 (= E70) to K: in ARGINSA; complete loss of argininosuccinate lyase activity; abolishes protein expression
• D87 (= D84) to G: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs752100894
• H89 (= H86) mutation to Q: 10-fold reduction in activity.
• R94 (≠ S91) to C: in ARGINSA; severe; dbSNP:rs374304304
• R95 (= R92) to C: in ARGINSA; loss of argininosuccinate lyase activity; dbSNP:rs28940585
• R113 (= R110) to Q: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on nitric oxide production; dbSNP:rs752783461
• D120 (= D117) to E: in ARGINSA; severe
• V178 (≠ E175) to M: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941473
• T181 (≠ A178) to S: in a breast cancer sample; somatic mutation
• R182 (= R179) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs751590073
• R186 (= R183) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs752397242
• G200 (= G197) to V: in a breast cancer sample; somatic mutation
• R236 (= R233) to W: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; no effect on NOS complex formation; dbSNP:rs761268464
• D237 (= D234) to N: in ARGINSA; severe; dbSNP:rs552951774
• Q286 (= Q283) to R: in ARGINSA; complete loss of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs28941472
• K288 (≠ R285) 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 (= R294) to Q: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression; dbSNP:rs750431938
• R306 (≠ A303) to W: in ARGINSA; severe; dbSNP:rs868834862
• Q326 (= Q323) to L: in ARGINSA; severe
• V335 (≠ A332) to L: in ARGINSA; reduction of argininosuccinate lyase activity; no effect on protein expression
• M360 (= M357) to T: in ARGINSA; loss of argininosuccinate lyase activity; may cause protein misfolding; dbSNP:rs875989948
• M382 (≠ L381) to R: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression
• R385 (= R384) to L: in ARGINSA; severe
• H388 (= H387) to Q: in ARGINSA; severe
• A398 (= A397) to D: in ARGINSA; impairs tetramer formation likely due to protein misfolding; loss of argininosuccinate lyase activity
• R456 (≠ L455) to W: in ARGINSA; reduction of argininosuccinate lyase activity; reduces protein expression; dbSNP:rs759396688

1k7wD Crystal structure of s283a duck delta 2 crystallin mutant (see paper)
42% identity, 94% coverage: 15:453/466 of query aligns to 3:439/450 of 1k7wD

• active site: E71 (= E83), T144 (= T156), H145 (= H157), A266 (≠ S278), S267 (= S279), K272 (= K284), E279 (= E291)
• binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y306 (= Y318), Q311 (= Q323), K314 (= K326)

1hy0A Crystal structure of wild type duck delta 1 crystallin (eye lens protein) (see paper)
40% identity, 94% coverage: 15:454/466 of query aligns to 1:438/447 of 1hy0A

• active site: E69 (= E83), T142 (= T156), H143 (= H157), S264 (= S278), S265 (= S279), K270 (= K284), E277 (= E291)
• binding sulfate ion: S264 (= S278), M267 (= M281), N272 (= N286)

P02521 Delta-1 crystallin; Delta crystallin I from Gallus gallus (Chicken) (see paper)
39% identity, 97% coverage: 3:454/466 of query aligns to 6:455/466 of P02521

Sites not aligning to the query:

• 2 modified: Blocked amino end (Ala)

6ienB Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 94% coverage: 14:450/466 of query aligns to 1:437/454 of 6ienB

• binding argininosuccinate: S97 (= S109), R98 (= R110), N99 (= N111), T144 (= T156), H145 (= H157), S266 (= S278), S267 (= S279), M269 (= M281), K272 (= K284), Y306 (= Y318), Q311 (= Q323), K314 (= K326)

6ienA Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
44% identity, 94% coverage: 14:450/466 of query aligns to 1:435/452 of 6ienA

• binding argininosuccinate: R98 (= R110), N99 (= N111), V102 (= V114), T144 (= T156), H145 (= H157), Y304 (= Y318), Q309 (= Q323), K312 (= K326)
• binding fumaric acid: S266 (= S278), S267 (= S279), K270 (= K284), N272 (= N286)

6ienC Substrate/product bound argininosuccinate lyase from mycobacterium tuberculosis (see paper)
41% identity, 94% coverage: 14:450/466 of query aligns to 1:401/418 of 6ienC

• binding arginine: R98 (= R110), N99 (= N111), V102 (= V114), Y306 (= Y318), Q311 (= Q323), K314 (= K326)
• binding argininosuccinate: T144 (= T156), H145 (= H157), S266 (= S278), S267 (= S279), M269 (= M281), K272 (= K284)
• binding fumaric acid: S97 (= S109), R98 (= R110), N99 (= N111)

6g3hA Crystal structure of edds lyase in complex with ss-edds (see paper)
37% identity, 79% coverage: 40:405/466 of query aligns to 44:398/497 of 6g3hA

• binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286), D286 (= D288), R290 (≠ L292)

Sites not aligning to the query:

• binding (2~{S})-2-[2-[[(2~{S})-1,4-bis(oxidanyl)-1,4-bis(oxidanylidene)butan-2-yl]amino]ethylamino]butanedioic acid: 22

6g3gA Crystal structure of edds lyase in complex with succinate (see paper)
37% identity, 79% coverage: 40:405/466 of query aligns to 44:398/497 of 6g3gA

• binding succinic acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286)

6g3fA Crystal structure of edds lyase in complex with fumarate (see paper)
37% identity, 79% coverage: 40:405/466 of query aligns to 44:398/497 of 6g3fA

• binding fumaric acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286)

6g3iA Crystal structure of edds lyase in complex with n-(2-aminoethyl) aspartic acid (aeaa) (see paper)
37% identity, 79% coverage: 40:405/466 of query aligns to 44:398/496 of 6g3iA

• binding (2~{S})-2-(2-azanylethylamino)butanedioic acid: S276 (= S278), S277 (= S279), M279 (= M281), K282 (= K284), N284 (= N286), D286 (= D288)
• binding fumaric acid: R290 (≠ L292)

Sites not aligning to the query:

• binding fumaric acid: 22

Q9LCC6 Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Bacillus sp. (see 3 papers)
28% identity, 48% coverage: 79:302/466 of query aligns to 113:342/468 of Q9LCC6

• H134 (≠ R103) mutation to A: Retains full activity. Shows a slightly stronger affinity for L-aspartate. Does not affect tertiary structure.
• S140 (= S109) binding L-aspartate; mutation to A: 27-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation S->K,R: Loss of activity.
• T141 (≠ R110) binding L-aspartate; mutation to A: 15-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to K: 40000-fold decrease in catalytic efficiency.; mutation T->V,R: Loss of activity.
• N142 (= N111) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation to Q: 3000-fold decrease in catalytic efficiency.
• K183 (≠ M152) mutation to A: Loss of activity. Does not affect tertiary structure.
• T187 (= T156) binding L-aspartate; mutation to A: 6280-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to S: 2.3-fold decrease in catalytic efficiency.
• H188 (= H157) binding L-aspartate; mutation to A: 100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation H->K,Q,R: Loss of activity.
• S318 (= S278) mutation to A: Loss of activity.
• S319 (= S279) binding L-aspartate; mutation to A: Almost no change in catalytic efficiency.
• I320 (= I280) mutation to A: 50-fold decrease in catalytic efficiency.
• M321 (= M281) mutation to A: 338-fold decrease in catalytic efficiency.
• P322 (= P282) mutation to A: Almost no change in catalytic efficiency.
• K324 (= K284) binding L-aspartate; mutation to A: Loss of activity. Does not result in any major conformational changes.; mutation K->D,H,R,S,V: Loss of activity.
• N326 (= N286) mutation to A: 22500-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; mutation to Q: 168750-fold decrease in catalytic efficiency.

Sites not aligning to the query:

• 101 binding L-aspartate; T→A: 7100-fold decrease in catalytic efficiency. Does not result in any major conformational changes.; T→S: 80-fold decrease in catalytic efficiency.

3r6vG Crystal structure of aspartase from bacillus sp. Ym55-1 with bound l- aspartate (see paper)
28% identity, 48% coverage: 79:302/466 of query aligns to 110:339/463 of 3r6vG

• active site: H185 (= H157), S315 (= S278), K321 (= K284), E328 (= E291)
• binding aspartic acid: G314 (= G277), S315 (= S278), S316 (= S279)

3r6qA A triclinic-lattice structure of aspartase from bacillus sp. Ym55-1 (see paper)
28% identity, 48% coverage: 79:302/466 of query aligns to 109:338/462 of 3r6qA

• active site: H184 (= H157), S314 (= S278), K320 (= K284), E327 (= E291)

Sites not aligning to the query:

• binding calcium ion: 389, 391

P12047 Adenylosuccinate lyase; ASL; Adenylosuccinase; ASase; Glutamyl--tRNA ligase regulatory factor; EC 4.3.2.2 from Bacillus subtilis (strain 168) (see paper)
25% identity, 67% coverage: 48:358/466 of query aligns to 44:342/431 of P12047

• H89 (= H105) mutation to Q: Abolishes enzyme activity.
• H141 (= H157) mutation to Q: Abolishes enzyme activity.
• Q212 (≠ S229) mutation to E: Decreases catalytic activity 1000-fold.; mutation to M: Abolishes enzyme activity.
• N270 (= N286) mutation N->D,L: Abolishes enzyme activity.
• R301 (≠ K320) mutation R->K,Q: Abolishes enzyme activity.

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)
34% identity, 36% coverage: 133:302/466 of query aligns to 163:342/474 of P9WN93

• T186 (= T156) binding substrate
• S318 (= S278) active site; mutation S->A,C: Absence of fumarase activity.
• S319 (= S279) binding substrate
• KVN 324:326 (≠ KRN 284:286) binding substrate

Sites not aligning to the query:

• 104:106 binding substrate
• 138:140 binding substrate

4adlA Crystal structures of rv1098c in complex with malate (see paper)
34% identity, 36% coverage: 133:302/466 of query aligns to 155:334/459 of 4adlA

• active site: T178 (= T156), H179 (= H157), S310 (= S278), S311 (= S279), K316 (= K284), E323 (= E291)

Sites not aligning to the query:

• binding (2S)-2-hydroxybutanedioic acid: 96, 98, 130, 131, 132

Query Sequence

>WP_012590227.1 NCBI__GCF_000021745.1:WP_012590227.1
MSNKMWGGRFASGPDAIMEEINASIGFDYRLAMQDIAGSKAHVAMLADVGIVSADDAADI
TQGLEAIKAEIESGAFTFSRALEDIHMNVESRLAALIGPAAGRLHTARSRNDQVALDFRL
WVRDTIDALDGQLRGLQLALAEKAKLYAGAVMPGFTHMQSAQPVTFGHHLLAYVEMFARD
RSRLRDARARLNESPLGAAALAGTSFPIDRHATARALGFDRPTANSLDSVSDRDFVLETL
SAAAIAAVHLSRFAEEIVLWSTPQFGFARLSDKFSTGSSIMPQKRNPDAAELVRGKAGRV
IGALTGLLVVMKGLPLTYSKDMQEDKEGAFDALHSLSLCLAAMTGMVKDIEPDTERMKAA
AGAGYATATDLADWLVKALGLPFREAHHVTGRLVAAASAQDKGLEELALAEMQAVEPRIN
AGVFAVLGVENSVRSRMSYGGTAPANVSEQAERWLGALAAEPASKI