UniProtKB - A0A031WDE4 (HYPD_CLODI)
Protein
Trans-4-hydroxy-L-proline dehydratase
Gene
pflD
Organism
Clostridioides difficile (Peptoclostridium difficile)
Status
Functioni
Glycine radical enzyme that catalyzes the dehydration of the non-proteinogenic amino acid trans-4-hydroxy-L-proline (Hyp) to produce delta1-pyrroline-5-carboxylate (P5C). Is involved in the anaerobic degradation of 4-hydroxyproline.1 Publication
Catalytic activityi
- EC:4.2.1.1721 Publication
Kineticsi
Kcat is 45 sec(-1) for trans-4-hydroxy-L-proline as substrate.1 Publication
- KM=1.2 mM for trans-4-hydroxy-L-proline1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 434 | Cysteine radical intermediateBy similarity | 1 | |
Active sitei | 436 | Proton acceptorBy similarity | 1 |
GO - Molecular functioni
- carbon-oxygen lyase activity Source: UniProtKB
GO - Biological processi
- proline salvage Source: UniProtKB
Keywordsi
Molecular function | Lyase |
Names & Taxonomyi
Protein namesi | Recommended name: Trans-4-hydroxy-L-proline dehydratase1 Publication (EC:4.2.1.1721 Publication)Alternative name(s): Glycyl radical enzymeCurated Hyp dehydratase1 Publication |
Gene namesi | Name:pflD1 Publication Synonyms:csdB_2Imported ORF Names:BGU81_07860Imported, BN1095_640054Imported, BN1096_740112Imported, BN1097_360077Imported, SAMEA3375004_02654Imported |
Organismi | Clostridioides difficile (Peptoclostridium difficile) |
Taxonomic identifieri | 1496 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae › Clostridioides |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000445027 | 1 – 789 | Trans-4-hydroxy-L-proline dehydrataseAdd BLAST | 789 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 765 | Glycine radicalPROSITE-ProRule annotation1 Publication | 1 |
Post-translational modificationi
Requires the activating protein PflE to generate the key active site glycyl radical on Gly-765 that is involved in catalysis.1 Publication
Keywords - PTMi
Organic radicalStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | A0A031WDE4 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 7 – 663 | PFLPROSITE-ProRule annotationAdd BLAST | 657 | |
Domaini | 670 – 789 | Glycine radicalPROSITE-ProRule annotationAdd BLAST | 120 |
Sequence similaritiesi
Family and domain databases
InterProi | View protein in InterPro IPR001150, Gly_radical IPR004184, PFL_dom |
Pfami | View protein in Pfam PF01228, Gly_radical, 1 hit PF02901, PFL-like, 1 hit |
PROSITEi | View protein in PROSITE PS51149, GLY_RADICAL_2, 1 hit PS51554, PFL, 1 hit |
i Sequence
Sequence statusi: Complete.
A0A031WDE4-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARGTFERTK KLREESINAE PHISIERAVL MTEAYKKYEG SVEIPVLRAL
60 70 80 90 100
SFKHYIENRT LSINDGELIV GEKGDSPNGA PTYPEICCHT MEDLEVMHNR
110 120 130 140 150
DIINFSVSEE ARKIHKEEII PFWKKRQTRD KIINAMTPEW LAAYEAGMFT
160 170 180 190 200
EFMEQRAPGH TVCGDTIYKK GFLDLKKDIE ARLKELDFLN DLDAYNKKAD
210 220 230 240 250
LEAMAIACDA MVILGKRYAE KARQMAEEET DEAKKKDLLL IAETCDVVPA
260 270 280 290 300
HKPETYHQAI QMYWFVHIGV TTELNIWDAF TPGRLDQHLN PFYERDVENG
310 320 330 340 350
ILDRDRAQEL LECLWVKFNN QPAPPKVGIT LKESSTYTDF ANINTGGINP
360 370 380 390 400
DGQDGVNEVS YIILDVMDEM KLIQPSSNVQ ISKKTPQKFL KRACEISRKG
410 420 430 440 450
WGQPAFYNTE AIVQELMEAG KTIEDARLGG TSGCVETGCF GKEAYVLTGY
460 470 480 490 500
MNIPKILELT LNNGYDPISK KQIGIETGDP RNFQSYEELF EAFKKQLHYM
510 520 530 540 550
IDIKIEGNAV IENICAKHMP CPLMSTIVDD CIEKGKDYQR GGARYNTRYI
560 570 580 590 600
QGVGIGTITD SLTAIKYNVF DKKKFDMDTL LKALDANFEG YEAILNLVSN
610 620 630 640 650
KTPKYGNDDD YADEIMQEIF NAYYNEVTGR PTVCGGEYRV DMLPTTCHIY
660 670 680 690 700
FGEIMGASPN GRLCAKPVSE GISPEKGGDT NGPTAVIKSC AKMDHIKTGG
710 720 730 740 750
TLLNQRFAPS VVQGEKGLDN MANLVRAYFN MDGHHIQFNV FDKNVLLEAQ
760 770 780
KNPQDYKDLI VRVAGYSDHF NNLSRTLQDE IIGRTEQTF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | LK932372 Genomic DNA Translation: CDS85123.1 LK932529 Genomic DNA Translation: CDS89454.1 LK933338 Genomic DNA Translation: CDT68933.1 MPEQ01000010 Genomic DNA Translation: PBG28510.1 FURH01000003 Genomic DNA Translation: SJT80202.1 |
RefSeqi | WP_021363977.1, NZ_VINA01000003.1 |
Genome annotation databases
EnsemblBacteriai | PBG28510; PBG28510; BGU81_07860 |
GeneIDi | 57296828 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | LK932372 Genomic DNA Translation: CDS85123.1 LK932529 Genomic DNA Translation: CDS89454.1 LK933338 Genomic DNA Translation: CDT68933.1 MPEQ01000010 Genomic DNA Translation: PBG28510.1 FURH01000003 Genomic DNA Translation: SJT80202.1 |
RefSeqi | WP_021363977.1, NZ_VINA01000003.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6VXC | X-ray | 2.05 | A/B/C/D/E/F/G/H | 1-789 | [»] | |
6VXE | X-ray | 2.46 | A/B/C/D/E/F/G/H | 1-789 | [»] | |
SMRi | A0A031WDE4 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Genome annotation databases
EnsemblBacteriai | PBG28510; PBG28510; BGU81_07860 |
GeneIDi | 57296828 |
Family and domain databases
InterProi | View protein in InterPro IPR001150, Gly_radical IPR004184, PFL_dom |
Pfami | View protein in Pfam PF01228, Gly_radical, 1 hit PF02901, PFL-like, 1 hit |
PROSITEi | View protein in PROSITE PS51149, GLY_RADICAL_2, 1 hit PS51554, PFL, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HYPD_CLODI | |
Accessioni | A0A031WDE4Primary (citable) accession number: A0A031WDE4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 12, 2018 |
Last sequence update: | July 9, 2014 | |
Last modified: | April 7, 2021 | |
This is version 40 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families