SitesBLAST
Comparing WP_076948772.1 NCBI__GCF_002893965.1:WP_076948772.1 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)
P9WPQ3 Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit; EC 6.3.4.14 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 99% coverage: 4:653/655 of query aligns to 5:652/654 of P9WPQ3
- K322 (≠ R319) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
35% identity, 99% coverage: 1:650/655 of query aligns to 2:677/681 of Q5LUF3
- F348 (= F347) binding biotin
- W515 (≠ P495) mutation to L: No effect on holoenzyme formation.
- L599 (= L584) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- L602 (vs. gap) mutation to A: Loss of holoenzyme formation; when associated with A-602 and A-603.
- M603 (vs. gap) mutation to A: No effect on holoenzyme formation. Loss of holoenzyme formation; when associated with A-602 and A-603.
- K647 (= K620) modified: N6-biotinyllysine
8xl6A Structure of human 3-methylcrotonyl-coa carboxylase at apo-state (mcc- apo)
34% identity, 98% coverage: 1:641/655 of query aligns to 1:647/660 of 8xl6A
8rthA Trypanosoma brucei 3-methylcrotonyl-coa carboxylase (see paper)
34% identity, 100% coverage: 1:654/655 of query aligns to 2:663/666 of 8rthA
3n6rG Crystal structure of the holoenzyme of propionyl-coa carboxylase (pcc) (see paper)
34% identity, 99% coverage: 1:650/655 of query aligns to 1:642/646 of 3n6rG
- active site: K115 (= K115), K157 (= K157), D180 (≠ E188), H193 (= H207), R219 (= R233), T258 (= T272), E260 (= E274), E273 (= E287), N275 (= N289), R277 (= R291), E281 (= E295), R323 (= R337), G519 (≠ D537)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: M611 (= M619), K612 (= K620)
7ybuA Human propionyl-coenzyme a carboxylase (see paper)
34% identity, 99% coverage: 3:650/655 of query aligns to 7:666/670 of 7ybuA
8xl5A Structure of human propionyl-coa carboxylase in complex with propionyl-coa (pcc-pco)
34% identity, 99% coverage: 3:650/655 of query aligns to 5:664/668 of 8xl5A
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)
34% identity, 99% coverage: 3:650/655 of query aligns to 65:724/728 of P05165
- A75 (≠ V13) to P: in PA-1; dbSNP:rs794727479
- R77 (= R15) to W: in PA-1; loss of function; dbSNP:rs141371306
- A138 (= A76) to T: in PA-1; loss of function; dbSNP:rs202247814
- I164 (≠ V102) to T: in PA-1; loss of function; dbSNP:rs202247815
- G197 (≠ E135) to E: in PA-1
- M229 (= M167) to K: in PA-1; dbSNP:rs375628794
- Q297 (= Q235) to R: in PA-1; dbSNP:rs2063109875
- D368 (= D306) to G: in PA-1
- M373 (≠ Q311) to K: in PA-1; unstable protein; loss of function; dbSNP:rs121964958
- G379 (= G317) to V: in PA-1; dbSNP:rs794727087
- C398 (≠ A336) to R: in PA-1
- R399 (= R337) to Q: in PA-1; dbSNP:rs1301904623
- P423 (= P360) to L: in PA-1; dbSNP:rs1443858896
- L532 (≠ W477) natural variant: Missing (in PA-1)
- V551 (≠ I496) to F: in dbSNP:rs61749895
- W559 (≠ A504) to L: in PA-1; dbSNP:rs118169528
- G631 (= G567) to R: in PA-1; loss of function; dbSNP:rs796052018
- G668 (= G595) to R: in PA-1; loss of biotinylation; dbSNP:rs771438170
- K694 (= K620) modified: N6-biotinyllysine; by HLCS
- C712 (≠ V638) natural variant: Missing (in PA-1; loss of biotinylation)
Sites not aligning to the query:
- 1:52 modified: transit peptide, Mitochondrion
8j78I Human 3-methylcrotonyl-coa carboxylase in bccp-h2 state
32% identity, 98% coverage: 1:641/655 of query aligns to 4:636/651 of 8j78I
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)
40% identity, 75% coverage: 2:495/655 of query aligns to 20:511/1178 of P11154
Sites not aligning to the query:
- 1135 modified: N6-biotinyllysine
8sgxX Leishmania tarentolae propionyl-coa carboxylase (alpha-4-beta-6) (see paper)
33% identity, 99% coverage: 4:650/655 of query aligns to 1:653/657 of 8sgxX
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
41% identity, 67% coverage: 1:441/655 of query aligns to 37:484/1178 of P11498
- V145 (≠ S108) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (≠ K119) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R233) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y267) to C: in PC deficiency
- R451 (≠ S408) 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
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
41% identity, 67% coverage: 1:441/655 of query aligns to 6:453/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ A17), T26 (≠ R21), R46 (= R42), Q47 (≠ L43), K48 (vs. gap), A49 (= A44), D50 (= D45), R367 (≠ W359), R414 (= R402), E418 (≠ D406), R420 (≠ S408), R422 (≠ F410)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K157), G168 (= G162), G169 (= G163), M173 (= M167), F207 (≠ L201), I208 (≠ V202), P211 (= P205), H240 (≠ N234)
Sites not aligning to the query:
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
41% identity, 67% coverage: 1:441/655 of query aligns to 5:452/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K157), G167 (= G162), G168 (= G163), F206 (≠ L201), Q236 (= Q231), H239 (≠ N234), E292 (= E287)
- binding coenzyme a: F21 (≠ A17), R22 (= R18), T25 (≠ R21), R45 (= R42), Q46 (≠ L43), K47 (vs. gap), A48 (= A44), D49 (= D45), E50 (≠ H46), R366 (≠ W359), R413 (= R402), A416 (≠ T405), R419 (≠ S408)
Sites not aligning to the query:
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
40% identity, 67% coverage: 1:441/655 of query aligns to 37:484/1178 of Q05920
- K39 (≠ R3) modified: N6-acetyllysine
- K79 (vs. gap) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L111) modified: N6-acetyllysine
- K152 (= K115) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ R204) modified: N6-acetyllysine
- K434 (≠ P391) 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
2vpqB Crystal structure of biotin carboxylase from s. Aureus complexed with amppnp (see paper)
38% identity, 67% coverage: 3:441/655 of query aligns to 2:443/448 of 2vpqB
- active site: V116 (≠ R117), K156 (= K157), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E287 (= E287), N289 (= N289), R291 (= R291), E295 (= E295), R337 (= R337)
- binding phosphoaminophosphonic acid-adenylate ester: K114 (= K115), I154 (≠ L155), K156 (= K157), G161 (≠ K165), G163 (≠ M167), I166 (≠ L170), F200 (≠ L201), I201 (≠ V202), E273 (= E274), I275 (≠ L276), M286 (≠ L286), E287 (= E287)
- binding magnesium ion: E273 (= E274), E287 (= E287)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate (see paper)
40% identity, 69% coverage: 4:458/655 of query aligns to 5:456/456 of 8hz4A
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
39% identity, 67% coverage: 1:442/655 of query aligns to 2:441/442 of 4mv4A
- active site: K116 (= K115), K159 (= K157), D193 (≠ G194), H206 (= H207), R232 (= R233), T271 (= T272), E273 (= E274), E285 (= E287), N287 (= N289), R289 (= R291), E293 (= E295), R335 (= R337)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K157), G164 (= G163), M166 (≠ K165), E198 (= E199), Y200 (≠ L201), L201 (≠ V202), H233 (≠ N234), L275 (= L276), E285 (= E287)
- binding magnesium ion: E273 (= E274), E285 (= E287)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
38% identity, 67% coverage: 1:440/655 of query aligns to 4:452/1150 of A0A0H3JRU9
- R21 (= R18) mutation to A: Complete loss of catalytic activity.
- K119 (= K115) binding ATP
- K161 (= K157) binding ATP
- H211 (= H207) binding ATP
- E278 (= E274) binding ATP
- K411 (≠ S399) mutation to A: Complete loss of catalytic activity.
Sites not aligning to the query:
- 541:545 binding substrate
- 542 binding Mn(2+)
- 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 Mn(2+)
- 741 binding Mn(2+)
- 743 binding Mn(2+)
- 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.
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)
39% identity, 67% coverage: 1:442/655 of query aligns to 2:439/440 of 6oi8A
- active site: K116 (= K115), K159 (= K157), D191 (≠ G194), H204 (= H207), R230 (= R233), T269 (= T272), E271 (= E274), E283 (= E287), N285 (= N289), R287 (= R291), E291 (= E295), R333 (= R337)
- 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 (≠ L155), K159 (= K157), M164 (≠ K165), E196 (= E199), Y198 (≠ L201), L199 (≠ V202), H204 (= H207), Q228 (= Q231), E271 (= E274), L273 (= L276), E283 (= E287), I432 (≠ T435)
Query Sequence
>WP_076948772.1 NCBI__GCF_002893965.1:WP_076948772.1
MTRLLIANRGEIVTRIARTARRLGMSVVTISSPVDSHAQWHRLADHTVLLDGDIPSESYT
NSDQIIAAALAADCDAVHPGYGFLSEDSDFAEAVVAAGLTFVGPAAESIALLGDKARAKK
AAADAGIPTLTAWGEASADPDTVLGHVRSLDVPVLLKPVFGGGGKGMVRLHPGDDAREVI
TSAIGLNERNFGRGDLMIETLVERPRHIEVQVLFDSFGTGVHFFTRECSLQRRNQKIIEQ
APASSVPESVLGAMQHDALRLLGGVGYVNAATVEFLVDAENRYYFLEVNTRLQVEHTVTE
EVTGVDLVELQLDIALGARLPLQQRHIALRGFAVQARIYAEDPSNGFRPAPSHSVDIAWP
SGVRIDSAFEGAGSIPPFYDPMIAKVIASGPTRSTALESLDRALTDSSYFGGTSNIGFLR
LLLATPAVRADDIHTSFVDEHLTRLIPDSAELQATAAAVAMVWTSVEEQSPVTGSSWTGP
HGLHRETLRKLGSDPIGRELIADARVVPTTVISQRSNHWIVAADGRNISVVVRGGTDEVT
LSLVADGLTTTAGRLGVGTGTWVCVGGWTVKVDEKVYTAKDSDLSDGEITSKMPGTVLAV
LQTGTRVSEGDVVAVVEAMKMETALRASSPGIVSAVTVTVGDVIDAGQVLAAVAP
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