Top Level Name

  ⌊ Superfamily (core) Enolase

    ⌊ Subgroup muconate cycloisomerase

     ⌊ Family 4R-hydroxyproline betaine 2-epimerase

  ⌊ FunctionalDomain 4R-hydroxyproline betaine 2-epimerase (ID 13983)

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
Pelagibaca bermudensis Taxon ID: 344736 495076664 WP_007801489.1 (RefSeq)
Pelagibaca bermudensis HTCC2601 Taxon ID: 314265 114543141 EAU46159.1 (Genbank) URP
Pelagibaca bermudensis HTCC2601 Taxon ID: 314265 122344006 URP

Uniprot

Protein NameAccessionEC Number Identifier
4-hydroxyproline betaine 2-epimerase Q0FPQ4 HPBD_PELBH (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 367 | Length of Functional Domain: 367

1       10        20        30        40        50        60

MKIAEIQLFQHDLPVVNGPYRIASGDVWSLTTTIVKIIAEDGTIGWGETCPVGPTYAEAH
AGGALAALEVLASGLAGAEALPLPLHTRMDSLLCGHNYAKSALDIAVHDLWGKRLGVPVH
ELLGGALTDSVSSYYSLGVMEPDEAARQALEKQREGYSRLQVKLGARPIEIDIEAIRKVW
EAVRGTGIALAADGNRGWTTRDALRFSRECPDIPFVMEQPCNSFEDLEAIRPLCHHALYM
DEDGTSLNTVITAAATSLVDGFGMKVSRIGGLQHMRAFRDFCAARNLPHTCDDAWGGDIV
SAACTHIASTVLPRLMEGAWLAQPYVAEHYDAENGVRIEGGRIRVPQGPGLGLTIDPERF
GPPLFSA
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
193 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
241 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
193 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
241 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
163 Lys (K) side chain None -- ISS PubMed:24056934
193 Asp (D) side chain Metal binding ligand metal ligand -- binding ICS PubMed:24056934
218 Glu (E) side chain Metal binding ligand metal ligand -- binding ICS PubMed:24056934
241 Asp (D) side chain Metal binding ligand metal ligand -- binding ICS PubMed:24056934
265 Lys (K) side chain None -- ISS PubMed:24056934
292 Asp (D) side chain Interacts with betaine substrate binding -- binding ICS PubMed:24056934
320 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
2PMQ Crystal Structure Of A Mandelate Racemase/Muconate Lactonizing Enzyme From Roseovarius Sp. Htcc2601 Mandelate Racemase/Muconate Lactonizing Enzyme 3 1.72 Selenomethionine • Magnesium Ion CSA • PDB • PDBSum
4H2H Crystal Structure Of An Enolase (Mandalate Racemase Subgroup, Target Efi-502101) From Pelagibaca Bermudensis Htcc2601, With Bound Mg And L-4-Hydroxyproline Betaine (Betonicine) Mandelate Racemase/Muconate Lactonizing Enzyme 3 1.7 Magnesium Ion
(4 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, 2:56 a.m. update curation agent updateSFLD2.py setDomainBoundaries.py
Aug. 10, 2015, 3:27 a.m. update curation agent setDomainBoundaries.py sbrown
update curation agent sbrown setDomainBoundaries.py
update domain end position 362 367
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.