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UniProtKB - P0AFI0 (OXC_ECOLI)
Protein
Oxalyl-CoA decarboxylase
Gene
oxc
Organism
Escherichia coli (strain K12)
Status
Functioni
Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA.
1 PublicationCatalytic activityi
- EC:4.1.1.81 Publication
Cofactori
Protein has several cofactor binding sites:- Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication
- thiamine diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit.1 Publication
Activity regulationi
Activated by ADP.1 Publication
Kineticsi
kcat is 69.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (with 300 µM ADP at pH 6.5 and 30 degrees Celsius). kcat is 60.7 sec(-1) for decarboxylase activity with oxalyl-CoA as substrate (at pH 6.5 and 30 degrees Celsius).
- KM=3.17 µM for oxalyl-CoA (with 300 µM ADP at pH 6.5 and 30 degrees Celsius)1 Publication
- KM=4.8 µM for oxalyl-CoA (at pH 6.5 and 30 degrees Celsius)1 Publication
pH dependencei
Optimum pH is between 5.5 and 7.1 Publication
: oxalate degradation Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes CO(2) and formate from oxalate. This subpathway is part of the pathway oxalate degradation, which is itself part of Metabolic intermediate degradation.View all proteins of this organism that are known to be involved in the subpathway that synthesizes CO(2) and formate from oxalate, the pathway oxalate degradation and in Metabolic intermediate degradation.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 32 | Substrate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 118 | SubstrateBy similarity | 1 | |
Binding sitei | 158 | ADP1 Publication | 1 | |
Binding sitei | 220 | ADP1 Publication | 1 | |
Binding sitei | 280 | ADP1 Publication | 1 | |
Binding sitei | 302 | ADP1 Publication | 1 | |
Binding sitei | 322 | ADP; via amide nitrogen1 Publication | 1 | |
Binding sitei | 355 | Substrate | 1 | |
Binding sitei | 372 | Thiamine pyrophosphate1 Publication | 1 | |
Metal bindingi | 447 | Magnesium1 Publication | 1 | |
Metal bindingi | 474 | Magnesium1 Publication | 1 | |
Metal bindingi | 476 | Magnesium; via carbonyl oxygen1 Publication | 1 | |
Binding sitei | 478 | Thiamine pyrophosphate; via amide nitrogen1 Publication | 1 |
GO - Molecular functioni
- ADP binding Source: EcoCyc
- identical protein binding Source: IntAct
- magnesium ion binding Source: UniProtKB
- oxalyl-CoA decarboxylase activity Source: EcoCyc
- thiamine pyrophosphate binding Source: EcoCyc
GO - Biological processi
- cellular response to acidic pH Source: EcoCyc
- fatty acid alpha-oxidation Source: GO_Central
- oxalate catabolic process Source: UniProtKB
Keywordsi
Molecular function | Decarboxylase, Lyase |
Ligand | Magnesium, Metal-binding, Nucleotide-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyci | EcoCyc:G7236-MONOMER |
BRENDAi | 4.1.1.8, 2026 |
UniPathwayi | UPA00540;UER00599 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:oxc Synonyms:yfdU Ordered Locus Names:b2373, JW2370 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000090824 | 1 – 564 | Oxalyl-CoA decarboxylaseAdd BLAST | 564 |
Proteomic databases
PaxDbi | P0AFI0 |
PRIDEi | P0AFI0 |
Expressioni
Inductioni
By the acid response regulator EvgA.1 Publication
Interactioni
Subunit structurei
Homotetramer; dimer of dimers.
1 PublicationBinary interactionsi
P0AFI0
With | #Exp. | IntAct |
---|---|---|
itself | 4 | EBI-557143,EBI-557143 |
GO - Molecular functioni
- identical protein binding Source: IntAct
Protein-protein interaction databases
BioGRIDi | 4260862, 15 interactors 851186, 1 interactor |
DIPi | DIP-48075N |
IntActi | P0AFI0, 6 interactors |
MINTi | P0AFI0 |
STRINGi | 511145.b2373 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P0AFI0 |
SMRi | P0AFI0 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0AFI0 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 261 – 265 | Substrate bindingCurated | 5 | |
Regioni | 396 – 398 | Thiamine pyrophosphate binding | 3 | |
Regioni | 403 – 404 | Substrate binding | 2 | |
Regioni | 421 – 423 | Thiamine pyrophosphate binding | 3 | |
Regioni | 448 – 449 | Thiamine pyrophosphate binding | 2 | |
Regioni | 550 – 552 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Belongs to the TPP enzyme family.Curated
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
InParanoidi | P0AFI0 |
OMAi | PGPYGCL |
PhylomeDBi | P0AFI0 |
Family and domain databases
InterProi | View protein in InterPro IPR029035, DHS-like_NAD/FAD-binding_dom IPR045025, HACL1-like IPR017660, Oxalyl-CoA_decarboxylase IPR029061, THDP-binding IPR012000, Thiamin_PyroP_enz_cen_dom IPR012001, Thiamin_PyroP_enz_TPP-bd_dom IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR43710, PTHR43710, 1 hit |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF00205, TPP_enzyme_M, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR03254, oxalate_oxc, 1 hit |
i Sequence
Sequence statusi: Complete.
P0AFI0-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSDQLQMTDG MHIIVEALKQ NNIDTIYGVV GIPVTDMARH AQAEGIRYIG
60 70 80 90 100
FRHEQSAGYA AAASGFLTQK PGICLTVSAP GFLNGLTALA NATVNGFPMI
110 120 130 140 150
MISGSSDRAI VDLQQGDYEE LDQMNAAKPY AKAAFRVNQP QDLGIALARA
160 170 180 190 200
IRVSVSGRPG GVYLDLPANV LAATMEKDEA LTTIVKVENP SPALLPCPKS
210 220 230 240 250
VTSAISLLAK AERPLIILGK GAAYSQADEQ LREFIESAQI PFLPMSMAKG
260 270 280 290 300
ILEDTHPLSA AAARSFALAN ADVVMLVGAR LNWLLAHGKK GWAADTQFIQ
310 320 330 340 350
LDIEPQEIDS NRPIAVPVVG DIASSMQGML AELKQNTFTT PLVWRDILNI
360 370 380 390 400
HKQQNAQKMH EKLSTDTQPL NYFNALSAVR DVLRENQDIY LVNEGANTLD
410 420 430 440 450
NARNIIDMYK PRRRLDCGTW GVMGIGMGYA IGASVTSGSP VVAIEGDSAF
460 470 480 490 500
GFSGMEIETI CRYNLPVTIV IFNNGGIYRG DGVDLSGAGA PSPTDLLHHA
510 520 530 540 550
RYDKLMDAFR GVGYNVTTTD ELRHALTTGI QSRKPTIINV VIDPAAGTES
560
GHITKLNPKQ VAGN
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75432.1 AP009048 Genomic DNA Translation: BAA16245.1 |
PIRi | B65011 |
RefSeqi | NP_416874.1, NC_000913.3 WP_001283490.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75432; AAC75432; b2373 BAA16245; BAA16245; BAA16245 |
GeneIDi | 946845 |
KEGGi | ecj:JW2370 eco:b2373 |
PATRICi | fig|1411691.4.peg.4356 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC75432.1 AP009048 Genomic DNA Translation: BAA16245.1 |
PIRi | B65011 |
RefSeqi | NP_416874.1, NC_000913.3 WP_001283490.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2Q27 | X-ray | 2.12 | A/B | 1-564 | [»] | |
2Q28 | X-ray | 1.74 | A/B | 1-564 | [»] | |
2Q29 | X-ray | 1.82 | A/B | 1-564 | [»] | |
AlphaFoldDBi | P0AFI0 | |||||
SMRi | P0AFI0 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260862, 15 interactors 851186, 1 interactor |
DIPi | DIP-48075N |
IntActi | P0AFI0, 6 interactors |
MINTi | P0AFI0 |
STRINGi | 511145.b2373 |
Proteomic databases
PaxDbi | P0AFI0 |
PRIDEi | P0AFI0 |
Genome annotation databases
EnsemblBacteriai | AAC75432; AAC75432; b2373 BAA16245; BAA16245; BAA16245 |
GeneIDi | 946845 |
KEGGi | ecj:JW2370 eco:b2373 |
PATRICi | fig|1411691.4.peg.4356 |
Organism-specific databases
EchoBASEi | EB3895 |
Phylogenomic databases
eggNOGi | COG0028, Bacteria |
InParanoidi | P0AFI0 |
OMAi | PGPYGCL |
PhylomeDBi | P0AFI0 |
Enzyme and pathway databases
UniPathwayi | UPA00540;UER00599 |
BioCyci | EcoCyc:G7236-MONOMER |
BRENDAi | 4.1.1.8, 2026 |
Miscellaneous databases
EvolutionaryTracei | P0AFI0 |
PROi | PR:P0AFI0 |
Family and domain databases
InterProi | View protein in InterPro IPR029035, DHS-like_NAD/FAD-binding_dom IPR045025, HACL1-like IPR017660, Oxalyl-CoA_decarboxylase IPR029061, THDP-binding IPR012000, Thiamin_PyroP_enz_cen_dom IPR012001, Thiamin_PyroP_enz_TPP-bd_dom IPR011766, TPP_enzyme-bd_C |
PANTHERi | PTHR43710, PTHR43710, 1 hit |
Pfami | View protein in Pfam PF02775, TPP_enzyme_C, 1 hit PF00205, TPP_enzyme_M, 1 hit PF02776, TPP_enzyme_N, 1 hit |
SUPFAMi | SSF52467, SSF52467, 1 hit SSF52518, SSF52518, 2 hits |
TIGRFAMsi | TIGR03254, oxalate_oxc, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | OXC_ECOLI | |
Accessioni | P0AFI0Primary (citable) accession number: P0AFI0 Secondary accession number(s): P78093, P78194, P78195 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 20, 2005 |
Last sequence update: | December 20, 2005 | |
Last modified: | May 25, 2022 | |
This is version 119 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