SitesBLAST
Comparing WP_058929592.1 NCBI__GCF_001484605.1:WP_058929592.1 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)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
50% identity, 70% coverage: 19:443/604 of query aligns to 5:427/456 of 8hz4A
P11154 Pyruvate carboxylase 1; Pyruvic carboxylase 1; PCB 1; EC 6.4.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
46% identity, 75% coverage: 17:466/604 of query aligns to 20:469/1178 of P11154
Sites not aligning to the query:
- 1135 modified: N6-biotinyllysine
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
46% identity, 73% coverage: 16:453/604 of query aligns to 2:435/442 of 4mv4A
- active site: K116 (= K130), K159 (= K172), D193 (≠ G209), H206 (= H222), R232 (= R248), T271 (= T287), E273 (= E289), E285 (= E302), N287 (= N304), R289 (= R306), E293 (= E310), R335 (= R350)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K172), G164 (≠ R180), M166 (≠ I182), E198 (= E214), Y200 (≠ F216), L201 (= L217), H233 (≠ N249), L275 (= L291), E285 (= E302)
- binding magnesium ion: E273 (= E289), E285 (= E302)
4mv3A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and bicarbonate (see paper)
46% identity, 73% coverage: 16:453/604 of query aligns to 2:432/439 of 4mv3A
- active site: K116 (= K130), K159 (= K172), D190 (≠ G209), H203 (= H222), R229 (= R248), T268 (= T287), E270 (= E289), E282 (= E302), N284 (= N304), R286 (= R306), E290 (= E310), R332 (= R350)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K172), M163 (≠ I182), E195 (= E214), Y197 (≠ F216), L198 (= L217), E270 (= E289), L272 (= L291), E282 (= E302)
- binding bicarbonate ion: R286 (= R306), Q288 (= Q308), V289 (= V309)
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)
46% identity, 73% coverage: 16:453/604 of query aligns to 2:433/440 of 6oi8A
- active site: K116 (= K130), K159 (= K172), D191 (≠ G209), H204 (= H222), R230 (= R248), T269 (= T287), E271 (= E289), E283 (= E302), N285 (= N304), R287 (= R306), E291 (= E310), R333 (= R350)
- 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 (≠ A170), K159 (= K172), M164 (≠ I182), E196 (= E214), Y198 (≠ F216), L199 (= L217), H204 (= H222), Q228 (= Q246), E271 (= E289), L273 (= L291), E283 (= E302), I432 (= I452)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
46% identity, 70% coverage: 19:440/604 of query aligns to 5:430/654 of P9WPQ3
- K322 (≠ E334) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
45% identity, 74% coverage: 18:464/604 of query aligns to 2:447/448 of 2vpqB
- active site: V116 (≠ Q132), K156 (= K172), H206 (= H222), R232 (= R248), T271 (= T287), E273 (= E289), E287 (= E302), N289 (= N304), R291 (= R306), E295 (= E310), R337 (= R350)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K130), I154 (≠ A170), K156 (= K172), G161 (= G177), G163 (= G179), I166 (= I182), F200 (= F216), I201 (≠ L217), E273 (= E289), I275 (≠ L291), M286 (≠ L301), E287 (= E302)
- binding magnesium ion: E273 (= E289), E287 (= E302)
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
44% identity, 75% coverage: 16:466/604 of query aligns to 37:485/1178 of Q05920
- K39 (= K18) modified: N6-acetyllysine
- K79 (≠ L58) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ A126) modified: N6-acetyllysine
- K152 (= K130) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ A219) modified: N6-acetyllysine
- K434 (≠ A406) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
- 589 modified: N6-acetyllysine
- 717 modified: N6-acetyllysine
- 748 modified: N6-acetyllysine; K→Q: Reduced pyruvate carboxylase activity.
- 892 modified: N6-acetyllysine
- 969 modified: N6-acetyllysine
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
47% identity, 73% coverage: 16:453/604 of query aligns to 2:438/448 of P43873
- K116 (= K130) binding ATP
- K159 (= K172) binding ATP
- EKYL 201:204 (≠ ERFL 214:217) binding ATP
- E276 (= E289) binding ATP; binding Mg(2+)
- E288 (= E302) binding ATP; binding Mg(2+)
- N290 (= N304) binding Mg(2+)
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
47% identity, 73% coverage: 16:453/604 of query aligns to 2:438/445 of 6ojhA
- active site: K116 (= K130), K159 (= K172), D196 (≠ G209), H209 (= H222), R235 (= R248), T274 (= T287), E276 (= E289), E288 (= E302), N290 (= N304), R292 (= R306), E296 (= E310), R338 (= R350)
- binding calcium ion: E276 (= E289), E288 (= E302), N290 (= N304)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K172), M169 (≠ I182), E201 (= E214), Y203 (≠ F216), L204 (= L217), H236 (≠ N249), L278 (= L291), E288 (= E302), I437 (= I452)
2vqdA Crystal structure of biotin carboxylase from pseudomonas aeruginosa complexed with ampcp (see paper)
46% identity, 74% coverage: 16:461/604 of query aligns to 2:444/447 of 2vqdA
- active site: K116 (= K130), K159 (= K172), P196 (≠ G209), H209 (= H222), R235 (= R248), T274 (= T287), E276 (= E289), E288 (= E302), N290 (= N304), R292 (= R306), E296 (= E310), R338 (= R350)
- binding phosphomethylphosphonic acid adenosyl ester: K116 (= K130), I157 (≠ A170), K159 (= K172), G164 (= G177), G166 (= G179), F203 (= F216), L204 (= L217), H209 (= H222), Q233 (= Q246), H236 (≠ N249), L278 (= L291), E288 (= E302), I437 (= I452)
- binding magnesium ion: E276 (= E289), E288 (= E302)
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)
44% identity, 71% coverage: 16:443/604 of query aligns to 2:451/681 of Q5LUF3
- F348 (= F360) binding biotin
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
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)
44% identity, 73% coverage: 16:458/604 of query aligns to 4:443/453 of 7kctA
- active site: E276 (= E289), E289 (= E302), N291 (= N304), E297 (= E310), R339 (= R350)
- binding adenosine-5'-diphosphate: K117 (= K130), L157 (≠ A170), K159 (= K172), G164 (= G177), G165 (= G178), G166 (= G179), I169 (= I182), E201 (= E214), Y203 (≠ F216), I204 (≠ L217), H209 (= H222), Q233 (= Q246), Q237 (= Q250), K238 (= K251), I278 (≠ L291), E289 (= E302), R293 (= R306), Q295 (= Q308), V296 (= V309), E297 (= E310), R339 (= R350)
- binding bicarbonate ion: D116 (= D129), R119 (≠ Q132)
- binding magnesium ion: E276 (= E289), E289 (= E302)
4mv1A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with adp and phosphate (see paper)
45% identity, 73% coverage: 16:453/604 of query aligns to 2:424/430 of 4mv1A
- active site: K116 (= K130), K159 (= K172), D182 (≠ G209), H195 (= H222), R221 (= R248), T260 (= T287), E262 (= E289), E274 (= E302), N276 (= N304), R278 (= R306), E282 (= E310), R324 (= R350)
- binding adenosine-5'-diphosphate: K159 (= K172), E187 (= E214), K188 (≠ R215), Y189 (≠ F216), L190 (= L217), L264 (= L291)
- binding phosphate ion: K224 (= K251), R278 (= R306), Q280 (= Q308), V281 (= V309), E282 (= E310)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
44% identity, 75% coverage: 16:466/604 of query aligns to 6:454/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ I32), T26 (≠ R36), R46 (≠ V56), Q47 (≠ R57), K48 (≠ L58), A49 (= A59), D50 (= D60), R367 (≠ K371), R414 (= R417), E418 (= E421), R420 (≠ V423), R422 (≠ G425)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K172), G168 (= G177), G169 (= G178), M173 (≠ I182), F207 (= F216), I208 (≠ L217), P211 (= P220), H240 (≠ N249)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
44% identity, 75% coverage: 16:466/604 of query aligns to 5:453/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K172), G167 (= G177), G168 (= G178), F206 (= F216), Q236 (= Q246), H239 (≠ N249), E292 (= E302)
- binding coenzyme a: F21 (≠ I32), R22 (= R33), T25 (≠ R36), R45 (≠ V56), Q46 (≠ R57), K47 (≠ L58), A48 (= A59), D49 (= D60), E50 (= E61), R366 (≠ K371), R413 (= R417), A416 (≠ E420), R419 (≠ V423)
Sites not aligning to the query:
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
44% identity, 75% coverage: 16:466/604 of query aligns to 37:485/1178 of P11498
- V145 (≠ A123) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R134) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R248) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y282) to C: in PC deficiency
- R451 (≠ V423) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
Sites not aligning to the query:
- 572 binding Mn(2+)
- 583 R → L: in PC deficiency; dbSNP:rs119103242
- 610 A → T: in PC deficiency; mild; dbSNP:rs28940589
- 631 R → Q: in PC deficiency; dbSNP:rs113994145
- 741 binding via carbamate group; modified: N6-carboxylysine
- 743 M → I: in PC deficiency; mild; dbSNP:rs28940590
- 771 binding Mn(2+)
- 773 binding Mn(2+)
- 1077 mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- 1131:1133 natural variant: Missing (in PC deficiency)
- 1144 modified: N6-biotinyllysine
2vr1A Crystal structure of biotin carboxylase from e. Coli in complex with atp analog, adpcf2p. (see paper)
44% identity, 73% coverage: 16:453/604 of query aligns to 2:436/444 of 2vr1A
- active site: K116 (= K130), K159 (= K172), D194 (≠ G209), H207 (= H222), R233 (= R248), T272 (= T287), E274 (= E289), E286 (= E302), N288 (= N304), R290 (= R306), E294 (= E310), R336 (= R350)
- binding phosphodifluoromethylphosphonic acid-adenylate ester: K159 (= K172), R165 (= R180), M167 (≠ I182), Y201 (≠ F216), L202 (= L217), E274 (= E289), L276 (= L291), E286 (= E302), N288 (= N304), I435 (= I452)
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)
41% identity, 76% coverage: 11:472/604 of query aligns to 58:511/728 of P05165
- A75 (= A28) to P: in PA-1; dbSNP:rs794727479
- R77 (= R30) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (≠ G91) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (= I117) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ D150) to E: in PA-1
- M229 (≠ I182) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q250) to R: in PA-1
- D368 (= D321) to G: in PA-1
- M373 (≠ Q326) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G332) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ F349) to R: in PA-1
- R399 (= R350) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P373) 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)
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
40% identity, 77% coverage: 19:484/604 of query aligns to 1:456/657 of 8sgxX
Sites not aligning to the query:
Query Sequence
>WP_058929592.1 NCBI__GCF_001484605.1:WP_058929592.1
MSANLEQSASPVQSNLTKVLIANRGEIAVRIIRAARDEGIASVAVYADPDRDALHVRLAD
EAYSLGGNTAAESYLVMDKIIDVARQSGADGIHPGYGFLAENAEFAAKVIDAGITWIGPS
PEAISALGDKVQARHIAEKVGAPQVPGTADPVQSAEEILEFVDKFGLPVAIKAAFGGGGR
GIKVARTREEIPELFESAVREATAAFGRGECFIERFLDAPRHVETQCLADAHGNVVVIST
RDCSLQRRNQKLVEEAPAPFLTEEQNRRLYESSKAILKEAGYLGAGTCEFLVGQDGTISF
LEVNTRLQVEHCVSEEVTGIDLVREQFRLARGEELGYGDPEVRGHSFEFRITGEDPGRNF
MPAPGTITTLKNPTGPGIRIDSGVEEGDVISGNFDSMLSKLIVTGATRAQALQRSRRALE
EMVVGGIPTVIPFDLAVVSDPAFAPAEGPFSIHTRWIETEFVNNIPAWTPDGTAEASGDA
GERQRVVVEVGGKRLEVVLPASLGSIGAGSAAGAKSNKSKKRLRSGGAAASAAGDALTSP
MQGTIVKVAVTNGDVVSEGDLVVVLEAMKMEQPLTAHRSGIITGLSAVAGETVSAGAVIA
TIED
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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