SitesBLAST
Comparing 5210790 FitnessBrowser__PV4:5210790 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)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
40% identity, 29% coverage: 942:1388/1516 of query aligns to 2:440/448 of 2vpqB
- active site: V116 (≠ N1059), K156 (= K1099), H206 (= H1149), R232 (≠ N1175), T271 (= T1214), E273 (= E1216), E287 (= E1230), N289 (= N1232), R291 (= R1234), E295 (= E1238), R337 (= R1278)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K1057), I154 (≠ L1097), K156 (= K1099), G161 (= G1104), G163 (= G1106), I166 (= I1109), F200 (≠ Y1143), I201 (≠ V1144), E273 (= E1216), I275 (= I1218), M286 (= M1229), E287 (= E1230)
- binding magnesium ion: E273 (= E1216), E287 (= E1230)
3ouuA Crystal structure of biotin carboxylase-beta-gamma-atp complex from campylobacter jejuni
40% identity, 30% coverage: 940:1390/1516 of query aligns to 6:445/446 of 3ouuA
- active site: K162 (= K1099), G168 (= G1105), G169 (= G1106), H212 (= H1149), K241 (= K1178), T277 (= T1214), E279 (= E1216), E292 (= E1230), N294 (= N1232), V299 (= V1237), E300 (= E1238), R341 (= R1278)
- binding phosphoaminophosphonic acid-adenylate ester: K120 (= K1057), I160 (≠ L1097), K162 (= K1099), G167 (= G1104), G168 (= G1105), G169 (= G1106), M172 (≠ I1109), E204 (= E1141), Y206 (= Y1143), I207 (≠ V1144), H212 (= H1149), Q236 (= Q1173), H239 (≠ N1176), L281 (≠ I1218), E292 (= E1230), T440 (= T1385)
- binding calcium ion: E279 (= E1216), E292 (= E1230)
3ouzA Crystal structure of biotin carboxylase-adp complex from campylobacter jejuni
40% identity, 30% coverage: 940:1390/1516 of query aligns to 5:444/445 of 3ouzA
- active site: K161 (= K1099), G167 (= G1105), G168 (= G1106), H211 (= H1149), K240 (= K1178), T276 (= T1214), E278 (= E1216), E291 (= E1230), N293 (= N1232), V298 (= V1237), E299 (= E1238), R340 (= R1278)
- binding adenosine-5'-diphosphate: K119 (= K1057), I159 (≠ L1097), K161 (= K1099), G166 (= G1104), G168 (= G1106), M171 (≠ I1109), E203 (= E1141), Y205 (= Y1143), I206 (≠ V1144), H211 (= H1149), Q235 (= Q1173), L280 (≠ I1218), E291 (= E1230), T439 (= T1385)
- binding magnesium ion: E278 (= E1216), E291 (= E1230)
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:440/444 of 2vr1A
- active site: K116 (= K1057), K159 (= K1099), D194 (≠ G1136), H207 (= H1149), R233 (≠ N1175), T272 (= T1214), E274 (= E1216), E286 (= E1230), N288 (= N1232), R290 (= R1234), E294 (= E1238), R336 (= R1278)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K1099), R165 (≠ K1107), M167 (≠ I1109), Y201 (= Y1143), L202 (≠ V1144), E274 (= E1216), L276 (≠ I1218), E286 (= E1230), N288 (= N1232), I435 (≠ T1385)
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)
40% identity, 29% coverage: 942:1388/1516 of query aligns to 6:442/453 of 7kctA
- active site: E276 (= E1216), E289 (= E1230), N291 (= N1232), E297 (= E1238), R339 (= R1278)
- binding adenosine-5'-diphosphate: K117 (= K1057), L157 (= L1097), K159 (= K1099), G164 (= G1104), G165 (= G1105), G166 (= G1106), I169 (= I1109), E201 (= E1141), Y203 (= Y1143), I204 (≠ V1144), H209 (= H1149), Q233 (= Q1173), Q237 (= Q1177), K238 (= K1178), I278 (= I1218), E289 (= E1230), R293 (= R1234), Q295 (= Q1236), V296 (= V1237), E297 (= E1238), R339 (= R1278)
- binding bicarbonate ion: D116 (≠ N1056), R119 (≠ N1059)
- binding magnesium ion: E276 (= E1216), E289 (= E1230)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
38% identity, 30% coverage: 940:1390/1516 of query aligns to 2:439/442 of 4mv4A
- active site: K116 (= K1057), K159 (= K1099), D193 (≠ G1136), H206 (= H1149), R232 (≠ N1175), T271 (= T1214), E273 (= E1216), E285 (= E1230), N287 (= N1232), R289 (= R1234), E293 (= E1238), R335 (= R1278)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K1099), G164 (≠ K1107), M166 (≠ I1109), E198 (= E1141), Y200 (= Y1143), L201 (≠ V1144), H233 (≠ N1176), L275 (≠ I1218), E285 (= E1230)
- binding magnesium ion: E273 (= E1216), E285 (= E1230)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
36% identity, 31% coverage: 937:1400/1516 of query aligns to 1:463/1150 of A0A0H3JRU9
- R21 (= R957) mutation to A: Complete loss of catalytic activity.
- K119 (= K1057) binding
- K161 (= K1099) binding
- H211 (= H1149) binding
- E278 (= E1216) binding
- K411 (= K1348) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding
- 542 binding
- 580 A→T: Complete loss of catalytic activity.
- 614 R→A: Complete loss of catalytic activity.
- 621 Y→A: Complete loss of catalytic activity.
- 712 binding
- 741 binding
- 743 binding
- 838 Q→A: About 2.5-fold loss of catalytic activity.
- 876 T→A: Complete loss of catalytic activity.
- 879 S→A: About 2-fold loss of catalytic activity.
- 880 K→T: Complete loss of catalytic activity.
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 30% coverage: 941:1388/1516 of query aligns to 3:443/654 of P9WPQ3
- K322 (≠ S1262) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
38% identity, 30% coverage: 932:1388/1516 of query aligns to 57:504/728 of P05165
- A75 (= A952) to P: in PA-1; dbSNP:rs794727479
- R77 (≠ K954) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A1018) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V1044) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (= G1077) to E: in PA-1
- M229 (≠ I1109) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q1177) to R: in PA-1
- D368 (= D1249) to G: in PA-1
- M373 (≠ G1254) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G1260) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ V1277) to R: in PA-1
- R399 (= R1278) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P1307) to L: in PA-1; dbSNP:rs1443858896
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
- 532 natural variant: Missing (in PA-1)
- 551 V → F: in dbSNP:rs61749895
- 559 W → L: in PA-1; dbSNP:rs118169528
- 631 G → R: in PA-1; loss of function; dbSNP:rs796052018
- 668 G → R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- 694 modified: N6-biotinyllysine; by HLCS
- 712 natural variant: Missing (in PA-1; loss of biotinylation)
7ybuA Human propionyl-coenzyme a carboxylase
39% identity, 30% coverage: 938:1388/1516 of query aligns to 3:446/670 of 7ybuA
Sites not aligning to the query:
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
38% identity, 30% coverage: 940:1390/1516 of query aligns to 2:436/439 of 4mv3A
- active site: K116 (= K1057), K159 (= K1099), D190 (≠ G1136), H203 (= H1149), R229 (≠ N1175), T268 (= T1214), E270 (= E1216), E282 (= E1230), N284 (= N1232), R286 (= R1234), E290 (= E1238), R332 (= R1278)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K1099), M163 (≠ I1109), E195 (= E1141), Y197 (= Y1143), L198 (≠ V1144), E270 (= E1216), L272 (≠ I1218), E282 (= E1230)
- binding bicarbonate ion: R286 (= R1234), Q288 (= Q1236), V289 (= V1237)
6oi8A Crystal structure of haemophilus influenzae biotin carboxylase complexed with 7-((1r,5s,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)- 6-(2-chloro-6-(pyridin-3-yl)phenyl)pyrido[2,3-d]pyrimidin-2-amine (see paper)
38% identity, 30% coverage: 940:1390/1516 of query aligns to 2:437/440 of 6oi8A
- active site: K116 (= K1057), K159 (= K1099), D191 (≠ G1136), H204 (= H1149), R230 (≠ N1175), T269 (= T1214), E271 (= E1216), E283 (= E1230), N285 (= N1232), R287 (= R1234), E291 (= E1238), R333 (= R1278)
- binding 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-6-[2-chloro-6-(pyridin-3-yl)phenyl]pyrido[2,3-d]pyrimidin-2-amine: I157 (≠ L1097), K159 (= K1099), M164 (≠ I1109), E196 (= E1141), Y198 (= Y1143), L199 (≠ V1144), H204 (= H1149), Q228 (= Q1173), E271 (= E1216), L273 (≠ I1218), E283 (= E1230), I432 (≠ T1385)
3rupA Crystal structure of e.Coli biotin carboxylase in complex with two adp and two ca ions (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/444 of 3rupA
- active site: K116 (= K1057), K159 (= K1099), D196 (≠ G1136), H209 (= H1149), R235 (≠ N1175), T274 (= T1214), E276 (= E1216), E288 (= E1230), N290 (= N1232), R292 (= R1234), E296 (= E1238), R338 (= R1278)
- binding adenosine-5'-diphosphate: Y82 (≠ I1023), G83 (= G1024), K116 (= K1057), K159 (= K1099), G164 (= G1104), G164 (= G1104), G165 (= G1105), G166 (= G1106), R167 (≠ K1107), M169 (≠ I1109), F193 (= F1133), E201 (= E1141), K202 (= K1142), Y203 (= Y1143), L204 (≠ V1144), H209 (= H1149), Q233 (= Q1173), H236 (≠ N1176), K238 (= K1178), L278 (≠ I1218), E288 (= E1230), R292 (= R1234), V295 (= V1237), E296 (= E1238), R338 (= R1278), D382 (= D1329), I437 (≠ T1385)
- binding calcium ion: E87 (= E1028), E276 (= E1216), E288 (= E1230), E288 (= E1230), N290 (= N1232)
3g8cA Crystal structure of biotin carboxylase in complex with biotin, bicarbonate, adp and mg ion (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/444 of 3g8cA
- active site: K116 (= K1057), K159 (= K1099), D196 (≠ G1136), H209 (= H1149), R235 (≠ N1175), T274 (= T1214), E276 (= E1216), E288 (= E1230), N290 (= N1232), R292 (= R1234), E296 (= E1238), R338 (= R1278)
- binding adenosine-5'-diphosphate: I157 (≠ L1097), K159 (= K1099), G164 (= G1104), M169 (≠ I1109), E201 (= E1141), K202 (= K1142), Y203 (= Y1143), L204 (≠ V1144), Q233 (= Q1173), H236 (≠ N1176), L278 (≠ I1218), E288 (= E1230), I437 (≠ T1385)
- binding bicarbonate ion: K238 (= K1178), R292 (= R1234), Q294 (= Q1236), V295 (= V1237), E296 (= E1238)
- binding biotin: Y82 (≠ I1023), F84 (= F1025), R292 (= R1234), V295 (= V1237), R338 (= R1278), D382 (= D1329)
- binding magnesium ion: E276 (= E1216), E288 (= E1230)
3jziA Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazole series (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/445 of 3jziA
- active site: K116 (= K1057), K159 (= K1099), D196 (≠ G1136), H209 (= H1149), R235 (≠ N1175), T274 (= T1214), E276 (= E1216), E288 (= E1230), N290 (= N1232), R292 (= R1234), E296 (= E1238), R338 (= R1278)
- binding 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide: K116 (= K1057), K159 (= K1099), A160 (= A1100), G164 (= G1104), G165 (= G1105), M169 (≠ I1109), Y199 (= Y1139), E201 (= E1141), K202 (= K1142), Y203 (= Y1143), H209 (= H1149), Q233 (= Q1173), H236 (≠ N1176), L278 (≠ I1218), I287 (≠ M1229), E288 (= E1230)
2w6oA Crystal structure of biotin carboxylase from e. Coli in complex with 4-amino-7,7-dimethyl-7,8-dihydro-quinazolinone fragment (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/445 of 2w6oA
- active site: K116 (= K1057), K159 (= K1099), D196 (≠ G1136), H209 (= H1149), R235 (≠ N1175), T274 (= T1214), E276 (= E1216), E288 (= E1230), N290 (= N1232), R292 (= R1234), E296 (= E1238), R338 (= R1278)
- binding 4-amino-7,7-dimethyl-7,8-dihydroquinazolin-5(6H)-one: K159 (= K1099), K202 (= K1142), Y203 (= Y1143), L204 (≠ V1144), L278 (≠ I1218), I437 (≠ T1385)
2w6nA Crystal structure of biotin carboxylase from e. Coli in complex with amino-oxazole fragment series (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/445 of 2w6nA
- active site: K116 (= K1057), K159 (= K1099), D196 (≠ G1136), H209 (= H1149), R235 (≠ N1175), T274 (= T1214), E276 (= E1216), E288 (= E1230), N290 (= N1232), R292 (= R1234), E296 (= E1238), R338 (= R1278)
- binding 2-amino-n,n-bis(phenylmethyl)-1,3-oxazole-5-carboxamide: I157 (≠ L1097), K159 (= K1099), M169 (≠ I1109), E201 (= E1141), K202 (= K1142), Y203 (= Y1143), L278 (≠ I1218)
2v59A Crystal structure of biotin carboxylase from e.Coli in complex with potent inhibitor 2 (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/445 of 2v59A
- active site: K116 (= K1057), K159 (= K1099), D196 (≠ G1136), H209 (= H1149), R235 (≠ N1175), T274 (= T1214), E276 (= E1216), E288 (= E1230), N290 (= N1232), R292 (= R1234), E296 (= E1238), R338 (= R1278)
- binding 6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine: K159 (= K1099), Y203 (= Y1143), L204 (≠ V1144), H209 (= H1149), Q233 (= Q1173), H236 (≠ N1176), L278 (≠ I1218), I437 (≠ T1385)
P24182 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Escherichia coli (strain K12) (see 3 papers)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 2:442/449 of P24182
- R19 (= R957) mutation to E: Loss of homodimerization. No effect on ATP binding.
- E23 (≠ D961) mutation to R: Loss of homodimerization. No effect on ATP binding.
- K116 (= K1057) binding
- K159 (= K1099) binding
- GG 165:166 (= GG 1105:1106) binding
- EKYL 201:204 (≠ EKYV 1141:1144) binding
- H209 (= H1149) binding
- H236 (≠ N1176) binding
- K238 (= K1178) binding
- E276 (= E1216) binding ; binding
- E288 (= E1230) binding ; binding
- R292 (= R1234) active site; binding
- V295 (= V1237) binding
- E296 (= E1238) mutation to A: Severe reduction in catalytic activity.
- R338 (= R1278) binding ; binding ; mutation to A: Severe reduction in catalytic activity.
- F363 (≠ D1310) mutation to A: Loss of homodimerization. No effect on ATP binding.
- R366 (≠ E1313) mutation to E: Loss of homodimerization. No effect on ATP binding.
3jzfB Crystal structure of biotin carboxylase from e. Coli in complex with benzimidazoles series (see paper)
39% identity, 30% coverage: 940:1390/1516 of query aligns to 4:444/447 of 3jzfB
- active site: K118 (= K1057), K161 (= K1099), D198 (≠ G1136), H211 (= H1149), R237 (≠ N1175), T276 (= T1214), E278 (= E1216), E290 (= E1230), N292 (= N1232), R294 (= R1234), E298 (= E1238), R340 (= R1278)
- binding 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide: K118 (= K1057), K161 (= K1099), A162 (= A1100), G166 (= G1104), G168 (= G1106), R169 (≠ K1107), G170 (= G1108), M171 (≠ I1109), Y201 (= Y1139), E203 (= E1141), K204 (= K1142), Y205 (= Y1143), H211 (= H1149), H238 (≠ N1176), L280 (≠ I1218), I289 (≠ M1229), E290 (= E1230)
Query Sequence
>5210790 FitnessBrowser__PV4:5210790
MTSNNQPTNTTQVQTADPLFLQAEHLAQDFSLFPKHSKQSLSQQIKGLLSDDEIQANLKE
LEQLDVDGYVAKVIQPTLDKSRPGAKRVIADLKGKLIVEKHMGPFYSAEIELNFGSRTRR
IGFIAQERSTSNGAWMPEHHLAACTAIRHFAELSMPIVYLIDTPGADAGEIANSQNQAHT
ISKAIAESANVDVPTVGIVIGAGYSGGAIPLAAANILLSLRDGIFNTIQPQGLQSIARKY
NLSWQECAKSVGVSPEELYTSGCIDGIIDFSPSDKDERQHNLRRAIISSIEAVEHAAVQF
VRESKDLREHYDRSLHRFLEPSKNLEALEHHAELSVANNPTMHLNLFGSSYRYLRYLTLR
SRIHSISQEQYGRLSKVSVPEGDLLARIQQEQDKVFQSWLSSPDKLVYDEELNKLWSNFT
AKRDEVSTERNMLTRLILGEPKQNYKKARKALLFNIGWSLYHRWKSNAENNFKGLIHYLE
SLPDEVTQADWPELNQLTVLDVIVHEELREDFIWQCYNILIFNALYDNVVGNLASIAKEA
MMSKSLSRASVDGLLHDSIDRAISKQDTANDKNKFYKWLKYFMSQSNRADLLTKTEQWKS
VGFPQLNDSLFVILTYFFERLLPEYFASEEESSEYTGAINPVRIGRRKDFWNRLTMGYQD
LLIQKVLRDEKRAGKMSWENVIAKFFTEFEELNGDKMSANLLNFPGFRLSIEDALDKGIR
PCGLITGTADFEHHGQTMRVGVAVSNTAFQAGAFDMASAEKFSALLIECAKRKLPVICFI
SSGGMQTKEGAAALFSMAVVNDRITRFVRDNELPVLMFGFGDCTGGAQASFVTHPLVQTY
YFSGTNMPFAGQMVVPAYLPSTSTLSNYLSKVPGAMNALVTNPFSDTIDDQLSSIDPLMP
KPTAKVVDVIGNAISTLVPEMLITEEELVQDDPRQLMKPIDKVLVHARGCTAVKLIRKAH
DNNIKVVLVASDPDMTSVPADMLNENDKLVCIGGNTSDESYLNAYSVLKVAEYEQVDALH
PGIGFLSESPQFAALCVNNGVNFVGPSVHSMTTMGNKSNAIKTSQSQNVPVVPGSHGILT
NAEQAVNVANEIGYPVLLKAVQGGGGKGIQVVQRPEDMISLFQKTSTEAAAAFGNGDLYL
EKYVTSLRHIEVQLLRDKFGNTKVLGLRDCSVQRNNQKVIEESGSTMLPEELKQQVMEYT
RALGDATDYMGAGTVEFIYNLDANEVYFMEMNTRLQVEHPVTEATSGIDIVSAGFDIAAG
RSIEDLEPQEIGYAIEVRVTAEKAALDSNGVLQLLPHPGMITECVIPERDDIEIISIAGE
GKEVSPYYDSLIAQIICRGESREDVINKLHDYLANQVVIKGIATNIPLLTRILKDGTFNE
GVYDTNYLPRFMAELDIPALIAEMEAAAETVGVDTESLRVGESNELKVLAQGAGIFYTSP
APGEADFVKEGDIVTVDQTLALTEAMKMFSQVTLAGFNRQGAVLYPEDKQYRIERILNSN
GQQVSQGELLFVVSPV
Or try a new SitesBLAST search
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