UniProtKB - O32141 (PUCL_BACSU)
Protein
Uric acid degradation bifunctional protein PucL
Gene
pucL
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Catalyzes two steps in the degradation of uric acid, i.e. the oxidation of uric acid to 5-hydroxyisourate (HIU) and the stereoselective decarboxylation of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) to (S)-allantoin.3 Publications
Miscellaneous
HIU and OHCU are unstable, they spontaneously decompose to form a racemic mixture of allantoin.
Catalytic activityi
pH dependencei
Optimum pH is 8.1 Publication
Temperature dependencei
Optimum temperature is 37 degrees Celsius. Retains 90% of its activity after 72 hours of incubation at 20 degrees Celsius or -4 degrees Celsius, but loses 50% of its activity after 12 hours of incubation at 37 degrees Celsius.1 Publication
: urate degradation Pathwayi
This protein is involved in step 1 and 3 of the subpathway that synthesizes (S)-allantoin from urate.Proteins known to be involved in the 3 steps of the subpathway in this organism are:
- Uric acid degradation bifunctional protein PucL (pucL)
- 5-hydroxyisourate hydrolase (pucM)
- Urate oxidase (pucL), Uric acid degradation bifunctional protein PucL (pucL)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-allantoin from urate, the pathway urate degradation and in Purine metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 68 | Proton donor; for OHCU decarboxylase activity1 Publication | 1 | |
Binding sitei | 69 | OHCU; via carbonyl oxygenBy similarity | 1 | |
Active sitei | 179 | Charge relay system; for urate oxidase activityBy similarity | 1 | |
Active sitei | 239 | Charge relay system; for urate oxidase activityBy similarity | 1 | |
Binding sitei | 349 | UrateBy similarity | 1 | |
Binding sitei | 366 | UrateBy similarity | 1 |
GO - Molecular functioni
- carboxy-lyase activity Source: GO_Central
- urate oxidase activity Source: UniProtKB-EC
GO - Biological processi
- allantoin biosynthetic process Source: InterPro
- purine nucleobase metabolic process Source: UniProtKB-KW
- urate catabolic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Decarboxylase, Lyase, Multifunctional enzyme, Oxidoreductase |
Biological process | Purine metabolism |
Enzyme and pathway databases
BioCyci | BSUB:BSU32450-MONOMER |
SABIO-RKi | O32141 |
UniPathwayi | UPA00394;UER00650 UPA00394;UER00652 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:pucL Synonyms:yunL Ordered Locus Names:BSU32450 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 68 | H → A: Loss of OHCU decarboxylase activity. 1 Publication | 1 | |
Mutagenesisi | 84 | E → A: Loss of OHCU decarboxylase activity. 1 Publication | 1 | |
Mutagenesisi | 158 | R → A: Loss of OHCU decarboxylase activity. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000166006 | 1 – 494 | Uric acid degradation bifunctional protein PucLAdd BLAST | 494 |
Proteomic databases
PaxDbi | O32141 |
PRIDEi | O32141 |
Expressioni
Inductioni
Expression is very low in excess nitrogen (glutamate plus ammonia) and is induced by TnrA during imiting-nitrogen conditions (glutamate). Expression is further induced when allantoin or uric acid are added during limiting-nitrogen conditions.2 Publications
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | O32141 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 174 | OHCU decarboxylaseAdd BLAST | 174 | |
Regioni | 81 – 85 | OHCU binding1 Publication | 5 | |
Regioni | 116 – 120 | OHCU bindingBy similarity | 5 | |
Regioni | 175 – 494 | Urate oxidaseAdd BLAST | 320 | |
Regioni | 239 – 240 | Urate bindingBy similarity | 2 | |
Regioni | 414 – 415 | Urate bindingBy similarity | 2 |
Sequence similaritiesi
In the N-terminal section; belongs to the OHCU decarboxylase family.Curated
In the C-terminal section; belongs to the uricase family.Curated
Phylogenomic databases
eggNOGi | COG3195, Bacteria COG3648, Bacteria |
InParanoidi | O32141 |
OMAi | QQTLYQM |
PhylomeDBi | O32141 |
Family and domain databases
Gene3Di | 1.10.3330.10, 1 hit |
InterProi | View protein in InterPro IPR018020, OHCU_decarboxylase IPR017580, OHCU_decarboxylase-1 IPR036778, OHCU_decarboxylase_sf IPR002042, Uricase IPR019842, Uricase_CS |
Pfami | View protein in Pfam PF09349, OHCU_decarbox, 1 hit PF01014, Uricase, 2 hits |
PRINTSi | PR00093, URICASE |
SUPFAMi | SSF158694, SSF158694, 1 hit |
TIGRFAMsi | TIGR03164, UHCUDC, 1 hit TIGR03383, urate_oxi, 1 hit |
PROSITEi | View protein in PROSITE PS00366, URICASE, 1 hit |
i Sequence
Sequence statusi: Complete.
O32141-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MFTMDDLNQM DTQTLTDTLG SIFEHSSWIA ERSAALRPFS SLSDLHRKMT
60 70 80 90 100
GIVKAADRET QLDLIKKHPR LGTKKTMSDD SVREQQNAGL GKLEQQEYEE
110 120 130 140 150
FLMLNEHYYD RFGFPFILAV KGKTKQDIHQ ALLARLESER ETEFQQALIE
160 170 180 190 200
IYRIARFRLA DIITEKGETQ MKRTMSYGKG NVFAYRTYLK PLTGVKQIPE
210 220 230 240 250
SSFAGRDNTV VGVDVTCEIG GEAFLPSFTD GDNTLVVATD SMKNFIQRHL
260 270 280 290 300
ASYEGTTTEG FLHYVAHRFL DTYSHMDTIT LTGEDIPFEA MPAYEEKELS
310 320 330 340 350
TSRLVFRRSR NERSRSVLKA ERSGNTITIT EQYSEIMDLQ LVKVSGNSFV
360 370 380 390 400
GFIRDEYTTL PEDGNRPLFV YLNISWQYEN TNDSYASDPA RYVAAEQVRD
410 420 430 440 450
LASTVFHELE TPSIQNLIYH IGCRILARFP QLTDVSFQSQ NHTWDTVVEE
460 470 480 490
IPGSKGKVYT EPRPPYGFQH FTVTREDAEK EKQKAAEKCR SLKA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB15235.1 |
PIRi | G70016 |
RefSeqi | NP_391125.1, NC_000964.3 WP_003242600.1, NZ_JNCM01000033.1 |
Genome annotation databases
EnsemblBacteriai | CAB15235; CAB15235; BSU32450 |
GeneIDi | 936669 |
KEGGi | bsu:BSU32450 |
PATRICi | fig|224308.179.peg.3512 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB15235.1 |
PIRi | G70016 |
RefSeqi | NP_391125.1, NC_000964.3 WP_003242600.1, NZ_JNCM01000033.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6A4M | X-ray | 2.60 | A | 175-479 | [»] | |
SMRi | O32141 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU32450 |
Proteomic databases
PaxDbi | O32141 |
PRIDEi | O32141 |
Genome annotation databases
EnsemblBacteriai | CAB15235; CAB15235; BSU32450 |
GeneIDi | 936669 |
KEGGi | bsu:BSU32450 |
PATRICi | fig|224308.179.peg.3512 |
Phylogenomic databases
eggNOGi | COG3195, Bacteria COG3648, Bacteria |
InParanoidi | O32141 |
OMAi | QQTLYQM |
PhylomeDBi | O32141 |
Enzyme and pathway databases
UniPathwayi | UPA00394;UER00650 UPA00394;UER00652 |
BioCyci | BSUB:BSU32450-MONOMER |
SABIO-RKi | O32141 |
Family and domain databases
Gene3Di | 1.10.3330.10, 1 hit |
InterProi | View protein in InterPro IPR018020, OHCU_decarboxylase IPR017580, OHCU_decarboxylase-1 IPR036778, OHCU_decarboxylase_sf IPR002042, Uricase IPR019842, Uricase_CS |
Pfami | View protein in Pfam PF09349, OHCU_decarbox, 1 hit PF01014, Uricase, 2 hits |
PRINTSi | PR00093, URICASE |
SUPFAMi | SSF158694, SSF158694, 1 hit |
TIGRFAMsi | TIGR03164, UHCUDC, 1 hit TIGR03383, urate_oxi, 1 hit |
PROSITEi | View protein in PROSITE PS00366, URICASE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PUCL_BACSU | |
Accessioni | O32141Primary (citable) accession number: O32141 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1999 |
Last sequence update: | January 1, 1998 | |
Last modified: | December 2, 2020 | |
This is version 133 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-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families