2kfu

Solution NMR

Function and Biology Details

Reactions catalysed:
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine
L-arginine + 2-oxoglutarate + O(2) = (3S)-3-hydroxy-L-arginine + succinate + CO(2)
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
(R)-mandelonitrile = cyanide + benzaldehyde
dUTP + H(2)O = dUMP + diphosphate
D-galactose + O(2) = D-galacto-hexodialdose + H(2)O(2)
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
RX + glutathione = HX + R-S-glutathione
An alpha-L-fucoside + H(2)O = L-fucose + an alcohol
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
2 glutathione + ROOH = glutathione disulfide + H(2)O + ROH
ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
Beta-D-ribopyranose = beta-D-ribofuranose
N-(5-phospho-D-ribosyl)-anthranilate + diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate
Formyl-L-methionyl peptide + H(2)O = formate + methionyl peptide
ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + cellular protein(Side 2)
Androstan-3-alpha,17-beta-diol + NAD(+) = 17-beta-hydroxyandrostan-3-one + NADH
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
An acyl-[acyl-carrier protein] + NAD(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH
ATP-dependent breakage, passage and rejoining of double-stranded DNA
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
ATP + UMP = ADP + UDP
NTP + H(2)O = NDP + phosphate
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine
1-haloalkane + H(2)O = a primary alcohol + halide
N-carbamoylputrescine + H(2)O = putrescine + CO(2) + NH(3)
Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin
Cleavage of peptide bonds with very broad specificity.
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Maltose = alpha,alpha-trehalose
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
Acetyl-CoA + phosphate = CoA + acetyl phosphate
L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O
ATP + adenosine = ADP + AMP
ATP + H(2)O = ADP + phosphate
A glutathione-S-conjugate + H(2)O = an (L-cysteinylglycine)-S-conjugate + L-glutamate
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
A beta-lactam + H(2)O = a substituted beta-amino acid
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
Thiosulfate + cyanide = sulfite + thiocyanate
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rv1827 pThr 22 Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 17.31 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WJA9 (Residues: 1-162; Coverage: 100%)
Gene names: MTCY1A11.16c, Rv1827, garA
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 89%
Refinement method: simulated annealing
Chemical shifts: BMR16248  
Expression system: Escherichia coli