SitesBLAST
Comparing WP_012991310.1 NCBI__GCF_000025605.1:WP_012991310.1 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)
5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
45% identity, 95% coverage: 25:644/653 of query aligns to 1:602/603 of 5ks8C
- active site: D11 (= D35), D115 (= D139), K172 (= K196), H201 (= H227), H203 (= H229)
- binding manganese (ii) ion: D11 (= D35), K172 (= K196), H201 (= H227), H203 (= H229)
- binding pyruvic acid: L79 (= L103), R81 (= R105), F114 (= F138), M174 (≠ A198)
5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
44% identity, 95% coverage: 25:644/653 of query aligns to 2:580/580 of 5ks8D
- active site: D12 (= D35), D116 (= D139), K173 (= K196), H202 (= H227), H204 (= H229)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D51 (= D74), Y56 (= Y79), M299 (= M324), T337 (= T362), S340 (= S365), Q341 (= Q366)
- binding manganese (ii) ion: D12 (= D35), K173 (= K196), H202 (= H227), H204 (= H229)
- binding pyruvic acid: Q15 (= Q38), G47 (= G70), L80 (= L103), R82 (= R105), T337 (= T362)
2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
44% identity, 69% coverage: 24:471/653 of query aligns to 5:453/453 of 2nx9B
Q70AC7 Methylmalonyl-CoA carboxyltransferase 5S subunit; Transcarboxylase 5S subunit; EC 2.1.3.1 from Propionibacterium freudenreichii subsp. shermanii (see paper)
43% identity, 76% coverage: 24:517/653 of query aligns to 12:503/505 of Q70AC7
- A59 (= A71) mutation to T: Decreases activity by 96%.
- K184 (= K196) modified: N6-carboxylysine; partial; mutation K->A,E: Loss of activity.
- M186 (≠ A198) mutation to I: Decreases activity by 98%.
1rqhA Propionibacterium shermanii transcarboxylase 5s subunit bound to pyruvic acid (see paper)
45% identity, 69% coverage: 24:474/653 of query aligns to 9:456/471 of 1rqhA
- active site: D20 (= D35), D124 (= D139), K181 (= K196), H212 (= H227), H214 (= H229), T346 (= T362)
- binding cobalt (ii) ion: D20 (= D35), K181 (= K196), H212 (= H227), H214 (= H229)
- binding pyruvic acid: Q23 (= Q38), G55 (= G70), L88 (= L103), K181 (= K196)
1rr2A Propionibacterium shermanii transcarboxylase 5s subunit bound to 2- ketobutyric acid (see paper)
45% identity, 69% coverage: 24:474/653 of query aligns to 10:457/472 of 1rr2A
- active site: D21 (= D35), D125 (= D139), K182 (= K196), H213 (= H227), H215 (= H229), T347 (= T362)
- binding 2-ketobutyric acid: Q24 (= Q38), G56 (= G70), L89 (= L103), K182 (= K196)
- binding cobalt (ii) ion: D21 (= D35), K182 (= K196), H213 (= H227), H215 (= H229)
1rqeA Propionibacterium shermanii transcarboxylase 5s subunit bound to oxaloacetate (see paper)
45% identity, 69% coverage: 24:474/653 of query aligns to 10:457/472 of 1rqeA
1rqbA Propionibacterium shermanii transcarboxylase 5s subunit (see paper)
45% identity, 69% coverage: 24:474/653 of query aligns to 10:457/472 of 1rqbA
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
31% identity, 95% coverage: 26:643/653 of query aligns to 533:1146/1150 of A0A0H3JRU9
- RDAHQ 541:545 (≠ RDGQQ 34:38) binding substrate
- D542 (= D35) binding Mn(2+)
- A580 (= A71) mutation to T: Complete loss of catalytic activity.
- R614 (= R105) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y112) mutation to A: Complete loss of catalytic activity.
- K712 (= K196) binding Mn(2+)
- H741 (= H227) binding Mn(2+)
- H743 (= H229) binding Mn(2+)
- Q838 (≠ M324) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T362) mutation to A: Complete loss of catalytic activity.
- S879 (= S365) mutation to A: About 2-fold loss of catalytic activity.
- K880 (≠ Q366) mutation to T: Complete loss of catalytic activity.
Sites not aligning to the query:
- 21 R→A: Complete loss of catalytic activity.
- 119 binding ATP
- 161 binding ATP
- 211 binding ATP
- 278 binding ATP
- 411 K→A: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
31% identity, 95% coverage: 26:643/653 of query aligns to 524:1137/1137 of 3bg5A
- active site: D533 (= D35), D639 (= D139), K703 (= K196), H732 (= H227), H734 (= H229), I755 (≠ L250), S761 (≠ P256), M762 (≠ L257), T801 (≠ Q296), T867 (= T362), S869 (= S364), V881 (= V376), N883 (≠ S378), Q888 (≠ Y382)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F579 (≠ Y79)
- binding manganese (ii) ion: D533 (= D35), H732 (= H227), H734 (= H229)
- binding pyruvic acid: L603 (= L103), K703 (= K196)
Sites not aligning to the query:
- active site: 117, 159, 189, 202, 228, 267, 269, 281, 283, 285, 289, 337
- binding adenosine-5'-triphosphate: 117, 157, 159, 196, 197, 202, 226, 229, 269, 271, 281, 283
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 463, 471, 472, 473
3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
31% identity, 95% coverage: 26:643/653 of query aligns to 461:1074/1074 of 3bg5B
- active site: D470 (= D35), D576 (= D139), K640 (= K196), H669 (= H227), H671 (= H229), I692 (≠ L250), S698 (≠ P256), M699 (≠ L257), T738 (≠ Q296), T804 (= T362), S806 (= S364), V818 (= V376), N820 (≠ S378), Q825 (≠ Y382)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F516 (≠ Y79), K518 (= K81)
- binding manganese (ii) ion: D470 (= D35), H669 (= H227), H671 (= H229)
- binding pyruvic acid: Q473 (= Q38), K640 (= K196), T804 (= T362)
Sites not aligning to the query:
- active site: 117, 139, 165, 204, 206, 218, 220, 222, 226, 274
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 403, 408, 409, 410
4hnvB Crystal structure of r54e mutant of s. Aureus pyruvate carboxylase (see paper)
31% identity, 95% coverage: 26:643/653 of query aligns to 420:1033/1033 of 4hnvB
- active site: D429 (= D35), D535 (= D139), K599 (= K196), H628 (= H227), H630 (= H229), I651 (≠ L250), S657 (≠ P256), M658 (≠ L257), T697 (≠ Q296), T763 (= T362), S765 (= S364), V777 (= V376), N779 (≠ S378), Q784 (≠ Y382)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F475 (≠ Y79), K477 (= K81)
- binding manganese (ii) ion: D429 (= D35), K599 (= K196), H628 (= H227), H630 (= H229)
Sites not aligning to the query:
- active site: 117, 139, 165, 204, 206, 218, 220, 222, 226, 274
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 362, 368, 369
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
31% identity, 95% coverage: 26:643/653 of query aligns to 520:1133/1133 of 3hb9A
- active site: D529 (= D35), D635 (= D139), K699 (= K196), H728 (= H227), H730 (= H229), I751 (≠ L250), S757 (≠ P256), M758 (≠ L257), T797 (≠ Q296), T863 (= T362), S865 (= S364), V877 (= V376), N879 (≠ S378), Q884 (≠ Y382)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F575 (≠ Y79), K577 (= K81)
- binding manganese (ii) ion: D529 (= D35), H728 (= H227), H730 (= H229)
Sites not aligning to the query:
- active site: 117, 159, 198, 224, 263, 265, 277, 279, 281, 285, 333
- binding adenosine-5'-diphosphate: 117, 157, 192, 193, 198, 222, 225, 267, 276, 277
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 459, 462, 467, 468
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)
31% identity, 94% coverage: 27:643/653 of query aligns to 558:1169/1178 of P11154
- K1135 (= K609) modified: N6-biotinyllysine
5ks8F Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
41% identity, 50% coverage: 25:350/653 of query aligns to 1:327/482 of 5ks8F
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
30% identity, 95% coverage: 24:642/653 of query aligns to 524:1137/1138 of 7zz3A
- binding acetyl coenzyme *a: K1016 (≠ E510), T1017 (≠ K511), L1018 (≠ F512), R1045 (≠ E540)
- binding biotin: K1104 (= K609)
- binding magnesium ion: D754 (= D248)
- binding manganese (ii) ion: D535 (= D35), K704 (= K196), H733 (= H227), H735 (= H229)
- binding pyruvic acid: R534 (= R34), Q538 (= Q38), L605 (= L103), K704 (= K196), T868 (= T362)
Sites not aligning to the query:
- binding acetyl coenzyme *a: 22, 43, 44, 45, 46, 48, 363, 413, 414, 416, 418, 459, 461
- binding adenosine-5'-triphosphate: 117, 156, 158, 163, 164, 165, 168, 200, 202, 203, 208, 232, 235, 277, 287, 289, 443
- binding bicarbonate ion: 237, 291, 293, 295
- binding biotin: 84, 294, 342
- binding magnesium ion: 275, 287, 520, 523
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
30% identity, 95% coverage: 24:642/653 of query aligns to 530:1143/1144 of 5vyzA
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: Q719 (≠ F205), Y722 (= Y208), S752 (≠ M240), G753 (≠ M241), Q756 (≠ L244)
- binding manganese (ii) ion: D541 (= D35), K710 (= K196), H739 (= H227), H741 (= H229)
Sites not aligning to the query:
- binding adenosine-5'-diphosphate: 123, 162, 164, 168, 170, 171, 174, 208, 209, 214, 238, 241, 283, 293, 449
- binding magnesium ion: 281, 293
5vyzC Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
30% identity, 95% coverage: 24:642/653 of query aligns to 469:1082/1083 of 5vyzC
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: P657 (= P204), Y661 (= Y208), S691 (≠ M240), Q695 (≠ L244)
- binding manganese (ii) ion: D480 (= D35), K649 (= K196), H678 (= H227), H680 (= H229)
Sites not aligning to the query:
4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
30% identity, 95% coverage: 23:643/653 of query aligns to 469:1080/1081 of 4qshC
- active site: K650 (= K196)
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: Y662 (= Y208), Y689 (≠ V237), A693 (≠ M241), S696 (≠ L244)
- binding manganese (ii) ion: D481 (= D35), H679 (= H227), H681 (= H229)
2qf7A Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
30% identity, 94% coverage: 24:639/653 of query aligns to 468:1073/1076 of 2qf7A
- active site: D479 (= D35), D585 (= D139), K648 (= K196), H677 (= H227), H679 (= H229), T812 (= T362)
- binding coenzyme a: I956 (= I506), K960 (≠ E510), L962 (≠ F512), N985 (≠ Q543)
- binding magnesium ion: D698 (= D248)
- binding zinc ion: D479 (= D35), K648 (= K196), H677 (= H227), H679 (= H229)
Sites not aligning to the query:
- active site: 124, 147, 173, 212, 214, 228, 230, 232, 236, 284
- binding phosphothiophosphoric acid-adenylate ester: 147, 171, 214, 216, 228, 385
- binding coenzyme a: 400, 401, 402, 403, 404
- binding magnesium ion: 214, 228, 464, 465, 467
Query Sequence
>WP_012991310.1 NCBI__GCF_000025605.1:WP_012991310.1
MHVMEIVEDIQEKLKEVEKKGFRKKILITDLTPRDGQQCKLATRVRTDDLLPLCEKMDKV
GFYAVEVWGGATYDVCLRYLKEDPWERLRRIKEVMPNTKLQMLFRGQNIVGYRPKSDKLV
YKFVERAIANGITVFRVFDALNDNRNIKTAVKAIKELGGEVHAEISYTRSPIHTYQKWIE
YALEIAEMGADWLSFKDATGIIMPFEVYAIIKGIKEATGGKLPVLLHNHDMSGTAIVNHM
MAVLAGVDMLDTVLSPLAFGSSHPATESVVAMLEGTPFDTGLDMRLIDECAEIARQIKKK
YKKYETEYAGVNAKVLIHKIPGGMISNMVAQLIEANALDKIEEVLKEVPNVERDLGYPPL
LTPSSQIVGVQAVLNVLSGERYKVITKEVRDYVEGKYGKPPGPISKELAEKILGPGKEPD
FSIRAADLADPDDWDKAYEETKALLGREPTDEEVLLYALFPMQAKDFFIAREKGELHPEP
VEEMEAVTEVKGGTVPGAAPVEFEIIYHGEKFKVKVEGVSAHQEPGKPRKYYIRVDGRLE
EVQLTPMREAIPSGGASATAVSTEEKGIPKATQPGDVTPPMPGRVVKILVNEGDAVQEGQ
TVAIVEAMKMENEIHAPVSGVVKKIYAKPGDNVTPDDAIMRIEPVKMEGDNYG
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