SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_022670321.1 NCBI__GCF_000420385.1:WP_022670321.1 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 8 hits to proteins with known functional sites (download)

Q58667 Methanogen homoaconitase small subunit; HACN; Homoaconitate hydratase; EC 4.2.1.114 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
55% identity, 98% coverage: 1:159/163 of query aligns to 1:158/170 of Q58667

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Q58667

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R26 (≠ N26) mutation R->K,V: Allows the recognition of substrates of IPMI enzymes since it becomes able to efficiently catalyze citraconate hydration and 3-isopropylmalate dehydration. Largely decreases substrate affinity for cis-homo(1-3)-aconitate.
T27 (= T27) mutation to A: Largely decreases substrate affinity for cis-homo(1-3)-aconitate while slightly increases activity on these substrates, and also decreases substrate affinity for maleate. Gains the ability to hydrate citraconate, an IPMI substrate.

2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
55% identity, 98% coverage: 1:159/163 of query aligns to 1:158/167 of 2pkpA

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2pkpA

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binding zinc ion: D13 (≠ N13), C63 (≠ S63)

O14289 3-isopropylmalate dehydratase; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 55% coverage: 13:102/163 of query aligns to 554:655/758 of O14289

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O14289

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Sites not aligning to the query:

486 modified: Phosphoserine
488 modified: Phosphoserine

P9WK95 3-isopropylmalate dehydratase small subunit; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
40% identity, 54% coverage: 13:100/163 of query aligns to 18:110/198 of P9WK95

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P9WK95

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Sites not aligning to the query:

154 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Q9SIB9 Aconitate hydratase 3, mitochondrial; Aconitase 3; mACO1; Citrate hydro-lyase 3; EC 4.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 31% coverage: 51:100/163 of query aligns to 861:910/990 of Q9SIB9

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Sites not aligning to the query:

91 modified: Phosphoserine

P19414 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
31% identity, 66% coverage: 54:160/163 of query aligns to 655:769/778 of P19414

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P19414

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Sites not aligning to the query:

1:16 modified: transit peptide, Mitochondrion
604 R→K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.

P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
38% identity, 40% coverage: 55:119/163 of query aligns to 661:728/789 of P39533

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Sites not aligning to the query:

610 K→R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
39% identity, 34% coverage: 54:109/163 of query aligns to 658:714/780 of P20004

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P20004

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SR 670:671 (= SR 66:67) binding substrate

Sites not aligning to the query:

99 binding substrate
192:194 binding substrate
385 binding [4Fe-4S] cluster
448 binding [4Fe-4S] cluster
451 binding [4Fe-4S] cluster
474 binding substrate
479 binding substrate
607 binding substrate

Query Sequence

>WP_022670321.1 NCBI__GCF_000420385.1:WP_022670321.1
MRIKGRVWVYPDNVDTDVIIPARYLNTSDPKELAKHCMEDIDENFAEQVKEGDIIVAGYN
FGSGSSREHAPIAIKASGVACVIAKSFSRIFYRNAFNIGLPILESDVSDELEKGDEIEVD
TQKGEIVVLKNGKIFKSSVIPEFMQQLIESGGLFGYAKKLLNV

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