SitesBLAST
Comparing GFF2304 FitnessBrowser__psRCH2:GFF2304 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 20 (the maximum) hits to proteins with known functional sites (download)
3va7A Crystal structure of the kluyveromyces lactis urea carboxylase (see paper)
43% identity, 83% coverage: 202:1196/1199 of query aligns to 133:1129/1130 of 3va7A
- active site: H138 (= H207), E205 (= E274), E219 (= E288), N221 (= N290), V226 (= V295), E227 (= E296), R269 (= R340), A550 (= A621), I648 (≠ L714), L730 (≠ I791), D760 (= D818), N762 (≠ V820), F895 (≠ Y954)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y633 (= Y699), T641 (= T707), P653 (= P719), G656 (= G722), F658 (= F724), P943 (= P1001), G944 (= G1002), K1096 (= K1163)
- binding urea: D893 (= D952), Y937 (= Y996), G944 (= G1002), G945 (= G1003), Y946 (= Y1004)
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)
47% identity, 37% coverage: 1:438/1199 of query aligns to 1:454/681 of Q5LUF3
Sites not aligning to the query:
- 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
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
47% identity, 36% coverage: 2:438/1199 of query aligns to 1:419/646 of 3n6rG
- active site: K115 (= K116), K157 (= K157), D180 (≠ A194), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E288), N275 (= N290), R277 (= R292), E281 (= E296), R323 (= R340)
Sites not aligning to the query:
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
44% identity, 37% coverage: 4:446/1199 of query aligns to 2:441/448 of 2vpqB
- active site: V116 (≠ T118), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E288), N289 (= N290), R291 (= R292), E295 (= E296), R337 (= R340)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K116), I154 (≠ M155), K156 (= K157), G161 (= G162), G163 (= G164), I166 (≠ M167), F200 (≠ Y201), I201 (= I202), E273 (= E274), I275 (≠ V276), M286 (≠ L287), E287 (= E288)
- binding magnesium ion: E273 (= E274), E287 (= E288)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
45% identity, 36% coverage: 1:430/1199 of query aligns to 1:428/654 of P9WPQ3
- K322 (≠ L320) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
43% identity, 37% coverage: 1:446/1199 of query aligns to 1:439/444 of 2vr1A
- active site: K116 (= K116), K159 (= K157), D194 (≠ A194), H207 (= H207), R233 (= R233), T272 (= T272), E274 (= E274), E286 (= E288), N288 (= N290), R290 (= R292), E294 (= E296), R336 (= R340)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K157), R165 (≠ I165), M167 (= M167), Y201 (= Y201), L202 (≠ I202), E274 (= E274), L276 (≠ V276), E286 (= E288), N288 (= N290), I435 (≠ T442)
7ybuA Human propionyl-coenzyme a carboxylase
42% identity, 37% coverage: 2:445/1199 of query aligns to 5:446/670 of 7ybuA
Sites not aligning to the query:
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
41% identity, 37% coverage: 4:446/1199 of query aligns to 5:454/1129 of 3tw6B
- active site: K124 (= K116), K162 (= K157), H212 (= H207), R238 (= R233), T277 (= T272), E279 (= E274), E293 (= E288), N295 (= N290), R297 (= R292), E301 (= E296), R349 (= R340)
- binding adenosine-5'-diphosphate: K124 (= K116), K162 (= K157), G167 (= G162), G169 (= G164), M172 (= M167), E204 (= E199), L206 (≠ Y201), V207 (≠ I202), H212 (= H207), Q236 (= Q231), N239 (= N234), L281 (≠ V276), E293 (= E288), T450 (= T442)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R340), D395 (= D387)
- binding magnesium ion: E279 (= E274), E293 (= E288)
Sites not aligning to the query:
- active site: 544, 650, 713, 742, 744, 877
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 1102
- binding magnesium ion: 529, 530, 532, 763
- binding zinc ion: 544, 713, 742, 744
P05165 Propionyl-CoA carboxylase alpha chain, mitochondrial; PCCase subunit alpha; Propanoyl-CoA:carbon dioxide ligase subunit alpha; EC 6.4.1.3 from Homo sapiens (Human) (see 6 papers)
42% identity, 37% coverage: 2:445/1199 of query aligns to 63:504/728 of P05165