Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family 4R-hydroxyproline betaine 2-epimerase

  ⌊ FunctionalDomain 4R-hydroxyproline betaine 2-epimerase (ID 6121)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES PubMed:24056934
This entry was last updated onNov. 22, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Paracoccus denitrificans Taxon ID: 266 500071499 WP_011747512.1 (RefSeq)
Paracoccus denitrificans PD1222 Taxon ID: 318586 119373699 ABL69292.1 (Genbank) URP
Paracoccus denitrificans PD1222 Taxon ID: 318586 586908170 URP

Uniprot

Protein NameAccessionEC Number Identifier
4-hydroxyproline betaine 2-epimerase A1B198 HPBD_PARDP (Swiss-Prot)

Sequence

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

1       10        20        30        40        50        60

MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETCPVGPTYAPSH
ALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYAKAAIDIAAYDLMGKHYGVRV
ADLLGGVAAERVPSYYATGIGQPDEIARIAAEKVAEGFPRLQIKIGGRPVEIDIETVRKV
WERIRGTGTRLAVDGNRSLPSRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIY
LDESGEDLSTVIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDI
IAAACTHIGATVQPRLNEGVWVAQPYIAQPYDEENGIRIAGGHIDLPKGPGLGITPDESL
FGPPVASFS
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
194 Asp (D) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
219 Glu (E) side chain metal binding ligand metal ligand -- binding ISS PubMed:8987982
242 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
164 Lys (K) side chain abstracts alpha proton (base) proton relay -- reactant ICS PubMed:11747448
194 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
219 Glu (E) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
242 Asp (D) side chain metal binding ligand metal ligand -- binding ICS PubMed:11747448
Family CAR This EFD conserves 7/7 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
164 Lys (K) side chain None -- ISS PubMed:24056934
194 Asp (D) side chain Metal binding ligand metal ligand -- binding ICS PubMed:24056934
219 Glu (E) side chain Metal binding ligand metal ligand -- binding ICS PubMed:24056934
242 Asp (D) side chain Metal binding ligand metal ligand -- binding ICS PubMed:24056934
266 Lys (K) side chain None -- ISS PubMed:24056934
293 Asp (D) side chain Interacts with betaine substrate binding -- binding ICS PubMed:24056934
321 Trp (W) side chain Forms pi-cation interaction with betaine electrostatic stabiliser -- spectator ICS PubMed:24056934

Catalyzed Reaction

4R-hydroxyproline betaine 2-epimerase

trans-4-hydroxy-L-proline betaine
85533		 cis-4-hydroxy-D-proline betaine
85534

EC: 5.1.1.22 | IntEnz: 5.1.1.22 | Kegg: 5.1.1.22 | BioCyc: 5.1.1.22 | BRENDA: 5.1.1.22

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
4E8G Crystal Structure Of An Enolase (Mandelate Racemase Subgroup) From Paracococus Denitrificans Pd1222 (Target Nysgrc-012907) With Bound Mg Mandelate Racemase/Muconate Lactonizing Enzyme, N-Terminaldomain Protein 4 2.0 Selenomethionine
(2 more ⇓) 		CSA • PDB • PDBSum
4IZG Crystal Structure Of An Enolase (Mandelate Racemase Subgroup) From Paracococus Denitrificans Pd1222 (Target Nysgrc-012907) With Bound Cis-4Oh-D-Proline Betaine (Product) Mandelate Racemase/Muconate Lactonizing Enzyme, N-Terminaldomain Protein 4 1.7 Iodide Ion
(2 more ⇓) 		CSA • PDB • PDBSum
4J1O Crystal Structure Of An Enolase (Mandelate Racemase Subgroup) From Paracococus Denitrificans Pd1222 (Target Nysgrc-012907) With Bound L-Proline Betaine (Substrate) Mandelate Racemase/Muconate Lactonizing Enzyme, N-Terminaldomain Protein 4 1.6 Magnesium Ion
(3 more ⇓) 		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 updateSFLDGIs.py setDomainBoundaries.py
Aug. 10, 2015, 3:03 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
update domain end position 365 369
update family assignment evidence code IEA IES
update name uncharacterized muconate cycloisomerase subgroup sequence, enolase superfamily 4R-hydroxyproline betaine 2-epimerase
update superfamily assignment evidence code IEA ISS
EC number assigned by UniProtKB accession ID.