SitesBLAST
Comparing 5208717 Shew_1220 pyruvate carboxylase subunit B (RefSeq) 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)
2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
69% identity, 75% coverage: 3:451/601 of query aligns to 5:453/453 of 2nx9B
5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
51% identity, 99% coverage: 7:600/601 of query aligns to 5:578/580 of 5ks8D
- active site: D12 (= D14), D116 (= D118), K173 (= K175), H202 (≠ Q204), H204 (= H206)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D51 (= D53), Y56 (= Y58), M299 (= M301), T337 (= T339), S340 (= S342), Q341 (= Q343)
- binding manganese (ii) ion: D12 (= D14), K173 (= K175), H202 (≠ Q204), H204 (= H206)
- binding pyruvic acid: Q15 (= Q17), G47 (= G49), L80 (= L82), R82 (= R84), T337 (= T339)
5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
50% identity, 99% coverage: 7:600/601 of query aligns to 4:600/603 of 5ks8C
- active site: D11 (= D14), D115 (= D118), K172 (= K175), H201 (≠ Q204), H203 (= H206)
- binding manganese (ii) ion: D11 (= D14), K172 (= K175), H201 (≠ Q204), H203 (= H206)
- binding pyruvic acid: L79 (= L82), R81 (= R84), F114 (= F117), M174 (= M177)
Q70AC7 Methylmalonyl-CoA carboxyltransferase 5S subunit; Transcarboxylase 5S subunit; EC 2.1.3.1 from Propionibacterium freudenreichii subsp. shermanii (see paper)
49% identity, 82% coverage: 3:494/601 of query aligns to 12:495/505 of Q70AC7
- A59 (= A50) mutation to T: Decreases activity by 96%.
- K184 (= K175) modified: N6-carboxylysine; partial; mutation K->A,E: Loss of activity.
- M186 (= M177) mutation to I: Decreases activity by 98%.
1rr2A Propionibacterium shermanii transcarboxylase 5s subunit bound to 2- ketobutyric acid (see paper)
51% identity, 75% coverage: 3:451/601 of query aligns to 10:454/472 of 1rr2A
- active site: D21 (= D14), D125 (= D118), K182 (= K175), H213 (≠ Q204), H215 (= H206), T347 (= T339)
- binding 2-ketobutyric acid: Q24 (= Q17), G56 (= G49), L89 (= L82), K182 (= K175)
- binding cobalt (ii) ion: D21 (= D14), K182 (= K175), H213 (≠ Q204), H215 (= H206)
1rqeA Propionibacterium shermanii transcarboxylase 5s subunit bound to oxaloacetate (see paper)
51% identity, 75% coverage: 3:451/601 of query aligns to 10:454/472 of 1rqeA
1rqbA Propionibacterium shermanii transcarboxylase 5s subunit (see paper)
51% identity, 75% coverage: 3:451/601 of query aligns to 10:454/472 of 1rqbA
1rqhA Propionibacterium shermanii transcarboxylase 5s subunit bound to pyruvic acid (see paper)
51% identity, 75% coverage: 3:451/601 of query aligns to 9:453/471 of 1rqhA
- active site: D20 (= D14), D124 (= D118), K181 (= K175), H212 (≠ Q204), H214 (= H206), T346 (= T339)
- binding cobalt (ii) ion: D20 (= D14), K181 (= K175), H212 (≠ Q204), H214 (= H206)
- binding pyruvic acid: Q23 (= Q17), G55 (= G49), L88 (= L82), K181 (= K175)
4hnvB Crystal structure of r54e mutant of s. Aureus pyruvate carboxylase (see paper)
35% identity, 99% coverage: 7:600/601 of query aligns to 422:1032/1033 of 4hnvB
- active site: D429 (= D14), D535 (= D118), K599 (= K175), H628 (≠ Q204), H630 (= H206), I651 (≠ L227), S657 (= S233), M658 (= M234), T697 (≠ E273), T763 (= T339), S765 (≠ T341), V777 (vs. gap), N779 (vs. gap), Q784 (vs. gap)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F475 (≠ Y58), K477 (≠ G60)
- binding manganese (ii) ion: D429 (= D14), K599 (= K175), H628 (≠ Q204), H630 (= H206)
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
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
35% identity, 99% coverage: 7:600/601 of query aligns to 526:1136/1137 of 3bg5A
- active site: D533 (= D14), D639 (= D118), K703 (= K175), H732 (≠ Q204), H734 (= H206), I755 (≠ L227), S761 (= S233), M762 (= M234), T801 (≠ E273), T867 (= T339), S869 (≠ T341), V881 (vs. gap), N883 (vs. gap), Q888 (vs. gap)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F579 (≠ Y58)
- binding manganese (ii) ion: D533 (= D14), H732 (≠ Q204), H734 (= H206)
- binding pyruvic acid: L603 (= L82), K703 (= K175)
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)
35% identity, 99% coverage: 7:600/601 of query aligns to 463:1073/1074 of 3bg5B
- active site: D470 (= D14), D576 (= D118), K640 (= K175), H669 (≠ Q204), H671 (= H206), I692 (≠ L227), S698 (= S233), M699 (= M234), T738 (≠ E273), T804 (= T339), S806 (≠ T341), V818 (vs. gap), N820 (vs. gap), Q825 (vs. gap)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F516 (≠ Y58), K518 (≠ G60)
- binding manganese (ii) ion: D470 (= D14), H669 (≠ Q204), H671 (= H206)
- binding pyruvic acid: Q473 (= Q17), K640 (= K175), T804 (= T339)
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
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
35% identity, 99% coverage: 7:600/601 of query aligns to 535:1145/1150 of A0A0H3JRU9
- RDAHQ 541:545 (= RDAHQ 13:17) binding
- D542 (= D14) binding
- A580 (= A50) mutation to T: Complete loss of catalytic activity.
- R614 (= R84) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y91) mutation to A: Complete loss of catalytic activity.
- K712 (= K175) binding
- H741 (≠ Q204) binding
- H743 (= H206) binding
- Q838 (≠ M301) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T339) mutation to A: Complete loss of catalytic activity.
- S879 (= S342) mutation to A: About 2-fold loss of catalytic activity.
- K880 (≠ Q343) mutation to T: Complete loss of catalytic activity.
Sites not aligning to the query:
- 21 R→A: Complete loss of catalytic activity.
- 119 binding
- 161 binding
- 211 binding
- 278 binding
- 411 K→A: Complete loss of catalytic activity.
5ks8F Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
51% identity, 54% coverage: 7:332/601 of query aligns to 4:329/482 of 5ks8F
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
35% identity, 99% coverage: 7:600/601 of query aligns to 522:1132/1133 of 3hb9A
- active site: D529 (= D14), D635 (= D118), K699 (= K175), H728 (≠ Q204), H730 (= H206), I751 (≠ L227), S757 (= S233), M758 (= M234), T797 (≠ E273), T863 (= T339), S865 (≠ T341), V877 (vs. gap), N879 (vs. gap), Q884 (vs. gap)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: F575 (≠ Y58), K577 (≠ G60)
- binding manganese (ii) ion: D529 (= D14), H728 (≠ Q204), H730 (= H206)
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
8gk8A R21a staphylococcus aureus pyruvate carboxylase
39% identity, 74% coverage: 7:452/601 of query aligns to 517:970/1041 of 8gk8A
Sites not aligning to the query:
- binding acetyl coenzyme *a: 400, 402, 404, 445, 447, 1026, 1030
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 457, 462, 463, 464
- binding coenzyme a: 42, 43, 45, 46, 47, 48
3ho8A Crystal structure of s. Aureus pyruvate carboxylase in complex with coenzyme a (see paper)
38% identity, 74% coverage: 7:452/601 of query aligns to 468:926/994 of 3ho8A
- active site: D475 (= D14), D581 (= D118), K645 (= K175), H674 (≠ Q204), H676 (= H206), I697 (≠ L227), S703 (= S233), M704 (= M234), T743 (≠ E273), T809 (= T339), S811 (≠ T341), V823 (vs. gap), N825 (vs. gap), Q830 (vs. gap)
- binding manganese (ii) ion: D475 (= D14), H674 (≠ Q204), H676 (= H206)
Sites not aligning to the query:
- active site: 117, 144, 170, 209, 211, 223, 225, 227, 231, 279
- binding coenzyme a: 42, 43, 48, 351, 353, 355, 395, 396, 398, 957, 981, 986
8gk8D R21a staphylococcus aureus pyruvate carboxylase
38% identity, 74% coverage: 7:452/601 of query aligns to 413:868/950 of 8gk8D
Sites not aligning to the query:
4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
33% identity, 99% coverage: 7:600/601 of query aligns to 474:1079/1081 of 4qshC
- active site: K650 (= K175)
- 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 (≠ F187), Y689 (≠ A214), A693 (≠ K218), S696 (≠ E221)
- binding manganese (ii) ion: D481 (= D14), H679 (≠ Q204), H681 (= H206)
8gk8C R21a staphylococcus aureus pyruvate carboxylase
38% identity, 74% coverage: 7:452/601 of query aligns to 463:921/993 of 8gk8C
Sites not aligning to the query:
- binding acetyl coenzyme *a: 19, 20, 43, 44, 45, 46, 49
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 403, 404, 409, 934
- binding coenzyme a: 346, 348, 350, 390, 391, 393, 394, 952, 976, 977, 981
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
32% identity, 100% coverage: 2:600/601 of query aligns to 523:1137/1138 of 7zz3A
- binding acetyl coenzyme *a: K1016 (≠ Q465), T1017 (≠ A466), L1018 (vs. gap), R1045 (≠ F497)
- binding biotin: K1104 (= K567)
- binding magnesium ion: T523 (≠ S2), D754 (= D225)
- binding manganese (ii) ion: D535 (= D14), K704 (= K175), H733 (≠ Q204), H735 (= H206)
- binding pyruvic acid: R534 (= R13), Q538 (= Q17), L605 (= L82), K704 (= K175), T868 (= T339)
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
Query Sequence
>5208717 Shew_1220 pyruvate carboxylase subunit B (RefSeq)
MSKPLALTDVVLRDAHQSILATRLRIDDMLPIAPLLDKVGFWSLESWGGATFDACIRYLG
EDPWERIRELKKAMPNTPQQMLLRGQNLLGYRHYGDDLVHRFVERAHQNGVDVFRIFDAM
NDVRNLETAVKSVVEVGGHAQGTISYTTSPVHTLDTWVDMAKRLEDMGCHSLCIKDMAGL
LKPFDAFDLISQLKAQTNLIISMQCHATTGLSTATYQKAIEAGIDVLDTAISSMSQTYGH
SATETLVAMVEDTDRATGYDMALLEQIAAYFREVRKKYVAFEGELKGIDSRILRAQVPGG
MLTNMENQLREQGAADKLDLVLEEIPKVREDLGFIPLVTPTSQIVGTQAVINVLTGERYK
SLTKETEGVLKGEYGATPAPVNRELQARVLAGAEAICCRPADLLPAELDSLRAELSEKAA
SEQISLAAELDDDVLTYALFPQIGLKFLKNRDNPDAFEPKPEAPQATTQAATVSEPASAR
QPQGKETYTVNVQGQSFVVEVSPGGDISQIVPSENVVPFAAPEPVAPVVGEGSPMNAPLS
GNIFKVNVQPGDAVKAGDVVIILEAMKMETEIRAESDGVVAKVWVKEGDSVAVGNQLLAI
A
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