Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family N-succinylamino acid racemase 1

  ⌊ FunctionalDomain N-succinylamino acid racemase (ID 5849)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IGS PubMed:16584181
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermus thermophilus Taxon ID: 274 499547476 WP_011228259.1 (RefSeq)
Thermus thermophilus HB8 Taxon ID: 300852 55980843 YP_144140.1 (RefSeq) URP
Thermus thermophilus HB8 Taxon ID: 300852 168988853 URP
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Uniprot

Protein NameAccessionEC Number Identifier
n/a Q5SJX8 Q5SJX8_THET8 (TrEMBL)

Sequence

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

1       10        20        30        40        50        60

MRIEAAELRILELPLKFRFETSFGVQTKRTILLLRLFGEGLEGLGEGVMERLPLYREETV
AGARYLLEEVFLPRVLGRDLPNPEALREALAPFRGNPMAKAVLEMAFFDLWAKALGRPLW
QVLGGVRQAVEVGVSLGIQPSVEDTLRVVERHLEEGYRRIKLKIKPGWDYEVLKAVREAF
PEATLTADANSAYSLANLAQLKRLDELRLDYIEQPLAYDDLLDHAKLQRELSTPICLDES
LTGAEKARKAIELGAGRVFNVKPARLGGHGESLRVHALAESAGIPLWMGGMLEAGVGRAH
NLHLATLPGFTKPGDVSSASRYWEEDIVEEALEAKDGLMPVPEGVGIGVHLKLPFVERVT
LWQRYMSAS
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
188 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
213 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
238 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
188 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
213 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
238 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
163 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS PubMed:16650857
188 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
213 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
238 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
262 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS PubMed:16650857

Catalyzed Reaction

N-succinylamino acid racemase

N-succinyl-L-amino acid residue
85535		 N-succinyl-D-amino acid
85536

EC: | IntEnz: | Kegg: | BioCyc: | BRENDA: |

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
2ZC8 Crystal Structure Of N-Acylamino Acid Racemase From Thermus Thermophilus Hb8 N-Acylamino Acid Racemase 6 1.95 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.