SitesBLAST
Comparing YP_004144858.1 NCBI__GCF_000185905.1:YP_004144858.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
3votA Crystal structure of l-amino acid ligase from bacillus licheniformis (see paper)
23% identity, 82% coverage: 56:389/406 of query aligns to 57:400/411 of 3votA
- binding adenosine-5'-diphosphate: K112 (= K111), K150 (= K151), V155 (≠ T156), E192 (= E193), F194 (= F195), I195 (≠ A196), E199 (≠ H200), F227 (= F224), E267 (= E264), R269 (= R266), I279 (= I275), E280 (= E276)
- binding calcium ion: E83 (= E82), D159 (vs. gap), E163 (≠ I167), E267 (= E264), E280 (= E276), E280 (= E276)
2yw2A Crystal structure of gar synthetase from aquifex aeolicus in complex with atp (see paper)
23% identity, 47% coverage: 93:282/406 of query aligns to 85:289/423 of 2yw2A
- binding adenosine-5'-triphosphate: K103 (= K111), K143 (= K151), G150 (≠ S158), G152 (= G160), A153 (≠ V161), E185 (= E193), F187 (= F195), L188 (≠ A196), E192 (≠ H200), K214 (vs. gap), N224 (≠ H223), L282 (≠ I275)
- binding phosphate ion: R287 (= R280)
Sites not aligning to the query:
3ax6A Crystal structure of n5-carboxyaminoimidazole ribonucleotide synthetase from thermotoga maritima
27% identity, 65% coverage: 18:280/406 of query aligns to 15:248/360 of 3ax6A
Sites not aligning to the query:
3vmmA Crystal structure of bacd, an l-amino acid dipeptide ligase from bacillus subtilis (see paper)
25% identity, 59% coverage: 59:296/406 of query aligns to 85:345/471 of 3vmmA
- binding adenosine-5'-diphosphate: K137 (= K111), I175 (= I149), K177 (= K151), A182 (≠ T156), S184 (= S158), F227 (= F195), L228 (≠ A196), Q267 (≠ H223), F270 (= F224), I322 (= I275), E323 (= E276)
- binding magnesium ion: E108 (= E82), A182 (≠ T156), E310 (= E264), E323 (= E276), E323 (= E276)
- binding (2S)-3-[(S)-[(1R)-1-aminoethyl](phosphonooxy)phosphoryl]-2-benzylpropanoic acid: S183 (≠ G157), E272 (≠ F226), H308 (≠ C262), E310 (= E264), E323 (= E276), R327 (= R280), G330 (= G283)
Sites not aligning to the query:
P39641 Alanine--anticapsin ligase; ATP-dependent dipeptide ligase; Bacilysin synthetase; L-Ala-L-amino acid dipeptide ligase; L-alanine--L-anticapsin ligase; L-amino acid ligase; Lal; EC 6.3.2.49 from Bacillus subtilis (strain 168) (see 2 papers)
25% identity, 59% coverage: 59:296/406 of query aligns to 86:346/472 of P39641
- E109 (= E82) binding ; mutation to A: Loss of ligase activity.
- K138 (= K111) binding
- K178 (= K151) binding
- L182 (≠ G155) binding
- S184 (≠ G157) mutation to A: Almost no effect on catalytic efficiency.
- SS 184:185 (≠ GS 157:158) binding
- EEFL 226:229 (≠ EEFA 193:196) binding
- Q268 (≠ H223) binding
- E273 (≠ F226) binding ; mutation to A: Loss of ligase activity.
- H309 (≠ C262) mutation to R: Loss of ligase activity.
- HTE 309:311 (≠ CIE 262:264) binding
- E311 (= E264) binding ; mutation to D: Loss of ligase activity.
- E324 (= E276) binding ; binding
- R328 (= R280) mutation to K: Loss of ligase activity.
- RFAG 328:331 (≠ RLGG 280:283) binding
- W332 (≠ G284) Plays a key role in restricting the N-terminal substrate specificity to small amino acids such as L-Ala; mutation to A: Hydrolyzes ATP, even in the absence of L-Ala, and the structure appears to show a cavity in the N-terminal substrate-binding pocket. Also alters the substrate specificity and activity depending on the size and shape of substituted amino acids.
Sites not aligning to the query:
- 75 Y→F: Almost no effect on catalytic efficiency.
3wo0A Crystal structure of bacillus subtilis ywfe, an l-amino acid ligase, with bound adp-mg-ala (see paper)
25% identity, 59% coverage: 59:296/406 of query aligns to 83:343/465 of 3wo0A
- binding adenosine-5'-diphosphate: K135 (= K111), I173 (= I149), K175 (= K151), A180 (≠ T156), S181 (≠ G157), S182 (= S158), E223 (= E193), F225 (= F195), L226 (≠ A196), Q265 (≠ H223), F268 (= F224), I320 (= I275), E321 (= E276)
- binding alanine: E270 (≠ F226), H306 (≠ C262), E308 (= E264), R325 (= R280), G328 (= G283)
- binding magnesium ion: E308 (= E264), E321 (= E276)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
25% identity, 62% coverage: 57:306/406 of query aligns to 70:323/1129 of 3tw6B
- active site: K124 (= K111), K162 (= K151), H212 (≠ Y201), R238 (= R227), T277 (= T261), E279 (≠ I263), E293 (= E276), N295 (= N278), R297 (= R280), E301 (≠ G284)
- binding adenosine-5'-diphosphate: K124 (= K111), K162 (= K151), G167 (≠ T156), G169 (≠ S158), M172 (≠ V161), E204 (= E193), L206 (≠ F195), V207 (≠ A196), H212 (≠ Y201), Q236 (≠ V225), N239 (≠ G228), L281 (= L265), E293 (= E276)
- binding magnesium ion: E279 (≠ I263), E293 (= E276)
Sites not aligning to the query:
- active site: 349, 544, 650, 713, 742, 744, 877
- binding adenosine-5'-diphosphate: 450
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 349, 395, 1102
- binding magnesium ion: 529, 530, 532, 763
- binding zinc ion: 544, 713, 742, 744
3vpdA Lysx from thermus thermophilus complexed with amp-pnp (see paper)
30% identity, 44% coverage: 102:278/406 of query aligns to 80:251/281 of 3vpdA
- binding phosphoaminophosphonic acid-adenylate ester: V127 (≠ I149), K129 (= K151), W135 (≠ G157), G136 (≠ S158), L139 (≠ C164), Q169 (≠ E193), V172 (≠ A196), K174 (≠ G198), D178 (≠ H200), R194 (≠ D219), W199 (≠ F224), T201 (vs. gap), F239 (≠ R266), E249 (= E276)
Sites not aligning to the query:
7lgmA Cyanophycin synthetase from a. Baylyi dsm587 with atp (see paper)
35% identity, 18% coverage: 99:172/406 of query aligns to 206:279/719 of 7lgmA
Sites not aligning to the query:
Q5LUF3 Propionyl-CoA carboxylase alpha chain; EC 6.4.1.3 from Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) (see paper)
21% identity, 74% coverage: 20:321/406 of query aligns to 18:333/681 of Q5LUF3
Sites not aligning to the query:
- 348 binding
- 515 W→L: No effect on holoenzyme formation.
- 599 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 602 L→A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- 603 M→A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- 647 modified: N6-biotinyllysine
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
23% identity, 56% coverage: 95:320/406 of query aligns to 100:332/447 of 2vqdA
- active site: K116 (= K111), K159 (= K151), P196 (= P188), H209 (≠ Y201), R235 (≠ P221), T274 (≠ C262), E276 (= E264), E288 (= E276), N290 (= N278), R292 (= R280), E296 (≠ G284)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K111), I157 (= I149), K159 (= K151), G164 (≠ T156), G166 (≠ S158), F203 (= F195), L204 (≠ A196), H209 (≠ Y201), Q233 (≠ D219), H236 (≠ P222), L278 (≠ R266), E288 (= E276)
- binding magnesium ion: E276 (= E264), E288 (= E276)
Sites not aligning to the query:
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
22% identity, 74% coverage: 20:320/406 of query aligns to 18:334/654 of P9WPQ3
- K322 (≠ E308) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
27% identity, 57% coverage: 76:306/406 of query aligns to 86:321/445 of 3ouzA
- active site: K161 (= K151), G167 (= G157), G168 (≠ S158), H211 (≠ Y201), K240 (≠ F224), T276 (= T261), E278 (≠ I263), E291 (= E276), N293 (= N278), V298 (≠ P285), E299 (= E286)
- binding adenosine-5'-diphosphate: K119 (= K111), I159 (= I149), K161 (= K151), G166 (≠ T156), G168 (≠ S158), M171 (≠ V161), E203 (= E193), Y205 (≠ F195), I206 (≠ A196), H211 (≠ Y201), Q235 (≠ D219), L280 (= L265), E291 (= E276)
- binding magnesium ion: E278 (≠ I263), E291 (= E276)
Sites not aligning to the query:
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
26% identity, 57% coverage: 76:306/406 of query aligns to 87:322/446 of 3ouuA
- active site: K162 (= K151), G168 (= G157), G169 (≠ S158), H212 (≠ Y201), K241 (≠ F224), T277 (= T261), E279 (≠ I263), E292 (= E276), N294 (= N278), V299 (≠ P285), E300 (= E286)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K111), I160 (= I149), K162 (= K151), G167 (≠ T156), G168 (= G157), G169 (≠ S158), M172 (≠ V161), E204 (= E193), Y206 (≠ F195), I207 (≠ A196), H212 (≠ Y201), Q236 (≠ D219), H239 (≠ P222), L281 (= L265), E292 (= E276)
- binding calcium ion: E279 (≠ I263), E292 (= E276)
Sites not aligning to the query:
7kctA Crystal structure of the hydrogenobacter thermophilus 2-oxoglutarate carboxylase (ogc) biotin carboxylase (bc) domain dimer in complex with adenosine 5'-diphosphate magnesium salt (mgadp), adenosine 5'- diphosphate (adp, and bicarbonate anion (hydrogen carbonate/hco3-) (see paper)
26% identity, 60% coverage: 76:317/406 of query aligns to 84:326/453 of 7kctA
- active site: E276 (= E264), E289 (= E276), N291 (= N278), E297 (≠ G284)
- binding adenosine-5'-diphosphate: K117 (= K111), L157 (≠ I149), K159 (= K151), G164 (≠ T156), G165 (= G157), G166 (≠ S158), I169 (≠ V161), E201 (= E193), Y203 (≠ F195), I204 (≠ A196), H209 (≠ Y201), Q233 (≠ D219), Q237 (≠ H223), K238 (≠ F224), I278 (≠ R266), E289 (= E276), R293 (= R280), Q295 (≠ G282), V296 (≠ G283), E297 (≠ G284)
- binding bicarbonate ion: D116 (= D110), R119 (≠ V113)
- binding magnesium ion: E276 (= E264), E289 (= E276)
Sites not aligning to the query:
Query Sequence
>YP_004144858.1 NCBI__GCF_000185905.1:YP_004144858.1
MARRSLILVEAGRSNGLMYVQAAQRLGLHPITLSTDPTQYDYLATRSIDAVRIDTDNLDA
LIRECSQLRATYDIAGITSSAEPFCAKVGKLCRHFDLPGPDPTSIERCCDKFVQRQLLAE
AGVPIPAYRVATNVADVESSAAEIGLPVILKPAVGTGSQGVRLCRNIHELAEHTTYLLGG
KHIWRSPPRILVEEFAEGPHYITHVMGHEVIGIEAADFDRPPHFVFRGGIFPAPLTDDEH
KRIIDTSLSCLQALSLGWGPTCIELRWTKCGPVVIEVNPRLGGGPEHIQLAYGIDLITEH
IKLVTGDEWDLRKRHSEIAGWRNLLPDHEGTLDWIDDGSRAAAVPGVAEIKLWVKPKMPI
VRKGDYLDSMGYVIAFSRSHTRTEAILQSAVELINWSITPFPPVSE
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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