Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family N-succinylamino acid racemase 1

  ⌊ FunctionalDomain N-succinylamino acid racemase (ID 271)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Deinococcus radiodurans R1 Taxon ID: 243230 10957399 NP_051613.1 (RefSeq) PRP URP
Deinococcus radiodurans Taxon ID: 1299 499186410 WP_010883950.1 (RefSeq)
Deinococcus radiodurans R1 Taxon ID: 243230 6460828 AAF12532.1 (Genbank) PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a Q9RZP3 Q9RZP3_DEIRA (TrEMBL)

Sequence

Length of Enzyme (full-length): 395 | Length of Functional Domain: 371

1       10        20        30        40        50        60

MTPFSPAGLTLESAELRLLEMPLKFDFETSFGVMRRRYVPLLTLRSGGLEGYAEGVMDFL
PLYREETVAGAVAFVEGQLLPRLLGQRFATPEALALELAPYRGNRMARAMVEMAFWDLWA
KALRLPLWQVLGGVRHKVPVGVSLGIQPGAEQTADLAARHAAEGYRRIKLKIKPGWDEQP
VAAVRAALPDTQLTVDANSAYTLADASALQRLDGYGLKYIEQPLAFDDLLDHAALQKNLR
TPLCLDESITSARDTRQALSIGAGRVINLKVARVGGHLEARRIHDLTLAFDASLWCGGMV
ETGIGRAHNIHLSTLENFTLPGDTSSASRYWERDIIQEPLEVERGEMPVPPGPGIGVSLD
PQALAGVTRWTREIQAGQTPFIDALPHQPPADEVY
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
196 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
221 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
246 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
171 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
196 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
221 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
246 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
171 Lys (K) side chain base (abstracts alpha proton), acid (donates proton to leaving group) proton relay -- reactant ICS PubMed:16650857
196 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
221 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
246 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:16650857
270 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: |

Curation History
Time Change Annotation Old Value New Value
Nov. 3, 2014, 2:33 a.m. update curation agent sbrown setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.