Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family N-succinylamino acid racemase 1

  ⌊ FunctionalDomain N-succinylamino acid racemase (ID 5855)

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
n/a 284827163 ADB99285.1 (Genbank)
Deinococcus radiodurans Taxon ID: 1299 56554698
Deinococcus radiodurans Taxon ID: 1299 56554697
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Sequence

Length of Enzyme (full-length): 375 | Length of Functional Domain: 370

1       10        20        30        40        50        60

MAHTGRMFKIEAAEIVVARLPLKFRFETSFGVQTHKVVPLLILHGEGVQGVAEGTMEARP
MYREETIAGALDLLRGTFLPAILGQTFANPEAVSDALGSYRGNRMARAMVEMAAWDLWAR
TLGVPLGTLLGGHKEQVEVGVSLGIQADEQATVDLVRRHVEQGYRRIKLKIKPGWDVQPV
RATREAFPDIRLTVDANSAYTLADAGRLRQLDEYDLTYIEQPLAWDDLVDHAELARRIRT
PLCLDESVASASDARKALALGAGGVINLKVARVGGHAESRRVHDVAQSFGAPVWCGGMLE
SGIGRAHNIHLSTLSNFRLPGDTSSASRYWERDLIQEPLEAVDGLMPVPQGPGTGVTLDR
EFLATVTEAQEEHRA
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
195 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
220 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
245 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
170 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
195 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
220 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
245 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
170 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS PubMed:16650857
195 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
220 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
245 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
269 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS PubMed:16650857

Catalyzed Reaction

N-acylamino acid racemase

N-acetyl-D-methionine(1-)
85220		 N-acetyl-L-methionine(1-)
71670

EC: 5.1.1.- | IntEnz: 5.1.1.- | Kegg: 5.1.1.- | BioCyc: 5.1.1.- | BRENDA: 5.1.1.- |

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1R0M Structure Of Deinococcus Radiodurans N-Acylamino Acid Racemase At 1.3 : Insights Into A Flexible Binding Pocket And Evolution Of Enzymatic Activity N-Acylamino Acid Racemase 7 1.3 CSA • PDB • PDBSum
1XS2 Structural Basis For Catalytic Racemization And Substrate Specificity Of An N-Acylamino Acid Racemase Homologue From Deinococcus Radiodurans N-Acylamino Acid Racemase 7 2.3 Magnesium Ion CSA • PDB • PDBSum
1XPY Structural Basis For Catalytic Racemization And Substrate Specificity Of An N-Acylamino Acid Racemase Homologue From Deinococcus Radiodurans N-Acylamino Acid Racemase 7 2.3 Magnesium Ion • N~2~-Acetyl-L-Glutamine CSA • PDB • PDBSum
2GGJ The Mutant Y218C Of Deinococcus Radiodurans N-Acylamino Acid Racemase N-Acylamino Acid Racemase 7 2.5 Yes CSA • PDB • PDBSum
2FKP The Mutant G127C-T313C Of Deinococcus Radiodurans N-Acylamino Acid Racemase N-Acylamino Acid Racemase 7 2.0 Yes CSA • PDB • PDBSum
2GGI The Mutant E149C-A182C Of Deinococcus Radiodurans N-Acylamino Acid Racemase N-Acylamino Acid Racemase 7 2.2 Yes CSA • PDB • PDBSum
2GGH The Mutant A68C-D72C-Nlq Of Deinococcus Radiodurans Nacylamino Acid Racemase N-Acylamino Acid Racemase 7 2.2 Yes Magnesium Ion • N~2~-Acetyl-L-Glutamine CSA • PDB • PDBSum
2GGG The Mutant A68C-D72C Of Deinococcus Radiodurans N-Acylamino Acid Racemase N-Acylamino Acid Racemase 7 2.4 Yes 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.