SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing AZOBR_RS14135 FitnessBrowser__azobra:AZOBR_RS14135 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 7 hits to proteins with known functional sites (download)

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)
64% identity, 98% coverage: 3:201/203 of query aligns to 539:734/758 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)
39% identity, 95% coverage: 1:192/203 of query aligns to 1:185/198 of P9WK95

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K154 (≠ E161) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

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)
35% identity, 66% coverage: 18:151/203 of query aligns to 13:126/170 of Q58667

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R26 (≠ K31) 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 (= T32) 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)
35% identity, 66% coverage: 18:151/203 of query aligns to 13:126/167 of 2pkpA

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2pkpA

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binding zinc ion: D13 (≠ N18), C63 (= C79)

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
44% identity, 25% coverage: 70:119/203 of query aligns to 658:707/780 of P20004

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SR 670:671 (= SR 82:83) 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

D9X0I3 Aconitate hydratase A; ACN; Aconitase; EC 4.2.1.3 from Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) (see paper)
34% identity, 28% coverage: 70:125/203 of query aligns to 805:860/931 of D9X0I3

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Sites not aligning to the query:

125:129 mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
538 C→A: Loss of aconitase activity. Cannot rescue the growth defect of a disruption mutant and results in only a slight increase in PTT production in the mutant. Shows weak IRE-binding activity.
763 R→E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
767 Q→E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.

5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
42% identity, 25% coverage: 70:119/203 of query aligns to 631:680/754 of 5acnA

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active site: S642 (= S81), R644 (= R83)
binding tricarballylic acid: R666 (≠ D105)

Sites not aligning to the query:

active site: 100, 101, 165, 447
binding fe3-s4 cluster: 145, 147, 167, 358, 421, 424, 446
binding tricarballylic acid: 198, 235

Query Sequence

>AZOBR_RS14135 FitnessBrowser__azobra:AZOBR_RS14135
MEKFTVLTGVAAPLPMINVDTDMIIPKQFLKTIKRTGLGKHLFDEMRYTPDGAEVAEFVL
NKPAYRSAKILVSGDNFGCGSSREHAPWALADFGIRCIIAPSFADIFFNNCFKNGILPIK
LPKEQVDLLLDDASRGSNAIVSVDLEKQEITGPDGGKISFEVDPFRKHCLLNGLDDIGLT
MQQAAFIDQYEGKQRGGQPWLWG

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