SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing RR42_RS01535 FitnessBrowser__Cup4G11:RR42_RS01535 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)

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)
40% identity, 96% coverage: 8:214/215 of query aligns to 542:744/758 of 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, 85% coverage: 10:191/215 of query aligns to 8:183/198 of P9WK95

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K154 (≠ T162) 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)
38% identity, 51% coverage: 20:128/215 of query aligns to 13:110/170 of Q58667

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R26 (= R33) 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 (≠ I34) 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)
38% identity, 51% coverage: 20:128/215 of query aligns to 13:110/167 of 2pkpA

query
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binding zinc ion: D13 (≠ N20), C63 (= C81)

P09339 Aconitate hydratase A; ACN; Aconitase; Aconitate/2-methylaconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.- from Bacillus subtilis (strain 168) (see 2 papers)
36% identity, 35% coverage: 72:146/215 of query aligns to 781:854/909 of P09339

query
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Sites not aligning to the query:

1 modified: Initiator methionine, Removed
450 C→S: Loss of aconitase activity. It is glutamate auxotroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of inactive aconitase.
741 R→E: Same aconitase activity compared to the wild-type. It is glutamate prototroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of active aconitase.

2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
41% identity, 31% coverage: 66:131/215 of query aligns to 757:826/888 of 2b3xA

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active site: S777 (= S83), R779 (= R85)

Sites not aligning to the query:

active site: 124, 125, 204, 535
binding iron/sulfur cluster: 175, 206, 436, 502, 505, 506, 534

P21399 Cytoplasmic aconitate hydratase; Aconitase; Citrate hydro-lyase; Ferritin repressor protein; Iron regulatory protein 1; IRP1; Iron-responsive element-binding protein 1; IRE-BP 1; EC 4.2.1.3 from Homo sapiens (Human) (see 2 papers)
41% identity, 31% coverage: 66:131/215 of query aligns to 758:827/889 of P21399

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S778 (= S83) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
R780 (= R85) mutation to Q: Nearly abolishes RNA binding.

Sites not aligning to the query:

300 C→S: No effect on aconitase activity or on RNA binding.
318 T → M: in dbSNP:rs150373174
437 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
503 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
506 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
536 R→Q: Strongly reduced RNA binding.
541 R→Q: Strongly reduced RNA binding.
699 R→K: No effect on RNA binding.

A0QX20 Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; Iron-responsive protein-like; IRP-like; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
33% identity, 40% coverage: 46:130/215 of query aligns to 782:869/943 of A0QX20

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Sites not aligning to the query:

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

Query Sequence

>RR42_RS01535 FitnessBrowser__Cup4G11:RR42_RS01535
MPDYDSDLIAALGAPLPIGNLDTDQIMPKQFLRIIDKAGLDRGLFYDMRFDAQGVPRPAF
ALNQARYQGAGVLVAGPNFGCGSSREHAVWGLQQYGIRAVIAPSFGEIFYSNAINNRLLL
VMLPQAEVDALMAAVSGSAPARIEIDLAAMSVSAGALRFAFTLAERHRTMFRQGLDMIGA
TLAQSSQIAAFTRRHHQSQPWLQDVAAKTMARLSA

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