Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family N-succinylamino acid racemase 2

  ⌊ FunctionalDomain N-succinylamino acid racemase 2 (ID 4304)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code ISS
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Bacillus thuringiensis Taxon ID: 1428 446627119 WP_000704465.1 (RefSeq) URP
Bacillus thuringiensis serovar konkukian str. 97-27 Taxon ID: 281309 49480074 YP_034658.1 (RefSeq) URP
Bacillus thuringiensis Taxon ID: 1428 753742448 AJI32438.1 (Genbank) URP
Show All

Uniprot

Protein NameAccessionEC Number Identifier
n/a A0A0U0G932 A0A0U0G932_STREE (TrEMBL)
n/a Q6HP62 Q6HP62_BACHK (TrEMBL)

Sequence

Length of Enzyme (full-length): 369 | Length of Functional Domain: 369

1       10        20        30        40        50        60

MKITAIHLYAIRLPLRDPFVISYGSYSDMPSIIVKMETDEGIIGYGEGVADDHVTGESWE
STFHTLKHTLAPALIGQNPMNIEKIHDMMDNTIYGVPTAKAAIDIACFDIMGKKLNQPVY
QLIGGRYHEEFPITHVLSIADPEEMAEEAASMIQKGYQSFKMKVGTNVKEDVKRIEAVRE
RVGNDIAIRVDVNQGWKNSANTLTALRSLGHVNIDWIEQPVIADDIDAMAHIRSKTDLPL
MIDEGLKGSREMRQIIKVDAADKVNIKLMKCGGIYPAVKLAHQAEMAGIECQVGSMVESS
VASSAGFHVAFSKKIITSVELTGPLKFTKDIGNLHYDVPFIRLNEKPGLGIEINEDTLRE
LTVFQGSVR
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
191 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
218 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
243 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
Subgroup CAR This EFD conserves 4/4 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
163 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
191 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
218 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
243 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
Family CAR This EFD conserves 8/8 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
51 Asp (D) side chain interacts with lysine/arginine side chains of substrate substrate binding -- binding ICS PubMed:17603539
163 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS
191 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
218 Glu (E) side chain metal binding ligand metal ligand -- binding ICS
243 Asp (D) side chain metal binding ligand metal ligand -- binding ICS
267 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS
322 Thr (T) main chain Interacts with N-succinyl moiety of substrate substrate binding -- binding ICS PubMed:17603539
326 Lys (K) main chain Interacts with N-succinyl moiety of substrate substrate binding -- binding ICS PubMed:17603539

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2P8B Crystal Structure Of N-Succinyl Arg/Lys Racemase From Bacillus Cereus Atcc 14579 Complexed With N-Succinyl Lys. Mandelate Racemase/Muconate Lactonizing Enzymefamily Protein 115 1.7 Magnesium Ion • N-Succinyl Lysine CSA • PDB • PDBSum
2P8C Crystal Structure Of N-Succinyl Arg/Lys Racemase From Bacillus Cereus Atcc 14579 Complexed With N-Succinyl Arg. Mandelate Racemase/Muconate Lactonizing Enzymefamily Protein 115 2.0 Magnesium Ion • N~2~-(3-Carboxypropanoyl)-L-Arginine CSA • PDB • PDBSum
2P88 Crystal Structure Of N-Succinyl Arg/Lys Racemase From Bacillus Cereus Atcc 14579 Mandelate Racemase/Muconate Lactonizing Enzymefamily Protein 115 2.4 Magnesium Ion CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:34 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.