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Protein

Oxalate decarboxylase OxdC

Gene

oxdC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts oxalate to formate and CO2 in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H2O2, and oxalate-dependent, H2O(2)-independent dye oxidations.3 Publications

Catalytic activityi

Oxalate = formate + CO2.3 Publications

Cofactori

Mn2+2 PublicationsNote: Binds 2 manganese ions per subunit.1 Publication

pH dependencei

Optimum pH is 5.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi95Manganese 11 Publication1
Metal bindingi97Manganese 11 Publication1
Metal bindingi101Manganese 11 Publication1
Metal bindingi140Manganese 11 Publication1
Metal bindingi273Manganese 21 Publication1
Metal bindingi275Manganese 21 Publication1
Metal bindingi280Manganese 21 Publication1
Metal bindingi319Manganese 21 Publication1
Active sitei333Proton donor1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU33240-MONOMER.
MetaCyc:BSU33240-MONOMER.
BRENDAi4.1.1.2. 658.
SABIO-RKO34714.

Names & Taxonomyi

Protein namesi
Recommended name:
Oxalate decarboxylase OxdC1 Publication (EC:4.1.1.23 Publications)
Gene namesi
Name:oxdC1 Publication
Synonyms:yvrK1 Publication
Ordered Locus Names:BSU33240
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi270R → E: Leads to a 20-fold reduction of CO(2) production. 1 Publication1
Mutagenesisi333E → A: Leads to a 25-fold reduction of activity and a 4-fold reduction of CO(2) production. 1 Publication1
Mutagenesisi340Y → F: Leads to a 13-fold reduction of CO(2) production. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000581061 – 385Oxalate decarboxylase OxdCAdd BLAST385

Proteomic databases

PaxDbiO34714.
PRIDEiO34714.

Expressioni

Inductioni

Induced by acid pH but not by oxalate (PubMed:10960116). Positively regulated by SigO and its coactivator RsoA (PubMed:18573182).2 Publications

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018051.

Structurei

Secondary structure

1385
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Helixi25 – 30Combined sources6
Helixi32 – 35Combined sources4
Beta strandi49 – 51Combined sources3
Helixi52 – 54Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi63 – 68Combined sources6
Turni70 – 72Combined sources3
Beta strandi80 – 86Combined sources7
Beta strandi91 – 99Combined sources9
Beta strandi101 – 115Combined sources15
Beta strandi121 – 127Combined sources7
Beta strandi130 – 134Combined sources5
Beta strandi140 – 156Combined sources17
Helixi162 – 164Combined sources3
Beta strandi165 – 167Combined sources3
Helixi168 – 173Combined sources6
Helixi177 – 184Combined sources8
Helixi189 – 191Combined sources3
Beta strandi200 – 202Combined sources3
Helixi210 – 213Combined sources4
Beta strandi226 – 229Combined sources4
Helixi230 – 232Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi239 – 247Combined sources9
Turni248 – 250Combined sources3
Beta strandi258 – 264Combined sources7
Beta strandi269 – 274Combined sources6
Beta strandi276 – 278Combined sources3
Beta strandi280 – 296Combined sources17
Beta strandi299 – 308Combined sources10
Beta strandi310 – 313Combined sources4
Beta strandi318 – 323Combined sources6
Beta strandi325 – 327Combined sources3
Beta strandi329 – 339Combined sources11
Helixi345 – 350Combined sources6
Helixi354 – 361Combined sources8
Helixi365 – 368Combined sources4
Beta strandi377 – 379Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J58X-ray1.75A1-385[»]
1L3JX-ray1.90A1-385[»]
1UW8X-ray2.00A1-385[»]
2UY8X-ray2.80A1-385[»]
2UY9X-ray3.10A1-385[»]
2UYAX-ray2.00A1-385[»]
2UYBX-ray2.10A1-385[»]
2V09X-ray1.80A1-385[»]
3S0MX-ray2.31A6-382[»]
4METX-ray2.10A/B/C/D1-382[»]
5HI0X-ray2.60A1-385[»]
ProteinModelPortaliO34714.
SMRiO34714.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34714.

Family & Domainsi

Sequence similaritiesi

To B.subtilis OxdD.Curated

Phylogenomic databases

eggNOGiENOG4105F0F. Bacteria.
COG2140. LUCA.
HOGENOMiHOG000200624.
InParanoidiO34714.
KOiK01569.
OMAiHARTFNY.
PhylomeDBiO34714.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR017774. Bicupin_oxalate_deCO2ase/Oxase.
IPR006045. Cupin_1.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 2 hits.
[Graphical view]
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR03404. bicupin_oxalic. 1 hit.

Sequencei

Sequence statusi: Complete.

O34714-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKQNDIPQP IRGDKGATVK IPRNIERDRQ NPDMLVPPET DHGTVSNMKF
60 70 80 90 100
SFSDTHNRLE KGGYAREVTV RELPISENLA SVNMRLKPGA IRELHWHKEA
110 120 130 140 150
EWAYMIYGSA RVTIVDEKGR SFIDDVGEGD LWYFPSGLPH SIQALEEGAE
160 170 180 190 200
FLLVFDDGSF SENSTFQLTD WLAHTPKEVI AANFGVTKEE ISNLPGKEKY
210 220 230 240 250
IFENQLPGSL KDDIVEGPNG EVPYPFTYRL LEQEPIESEG GKVYIADSTN
260 270 280 290 300
FKVSKTIASA LVTVEPGAMR ELHWHPNTHE WQYYISGKAR MTVFASDGHA
310 320 330 340 350
RTFNYQAGDV GYVPFAMGHY VENIGDEPLV FLEIFKDDHY ADVSLNQWLA
360 370 380
MLPETFVQAH LDLGKDFTDV LSKEKHPVVK KKCSK
Length:385
Mass (Da):43,566
Last modified:January 1, 1998 - v1
Checksum:iA301F5A75E53F4FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223978 Genomic DNA. Translation: CAA11727.1.
AL009126 Genomic DNA. Translation: CAB15314.1.
PIRiE70047.
RefSeqiNP_391204.1. NC_000964.3.
WP_003243476.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15314; CAB15314; BSU33240.
GeneIDi938620.
KEGGibsu:BSU33240.
PATRICi18978646. VBIBacSub10457_3486.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223978 Genomic DNA. Translation: CAA11727.1.
AL009126 Genomic DNA. Translation: CAB15314.1.
PIRiE70047.
RefSeqiNP_391204.1. NC_000964.3.
WP_003243476.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J58X-ray1.75A1-385[»]
1L3JX-ray1.90A1-385[»]
1UW8X-ray2.00A1-385[»]
2UY8X-ray2.80A1-385[»]
2UY9X-ray3.10A1-385[»]
2UYAX-ray2.00A1-385[»]
2UYBX-ray2.10A1-385[»]
2V09X-ray1.80A1-385[»]
3S0MX-ray2.31A6-382[»]
4METX-ray2.10A/B/C/D1-382[»]
5HI0X-ray2.60A1-385[»]
ProteinModelPortaliO34714.
SMRiO34714.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100018051.

Proteomic databases

PaxDbiO34714.
PRIDEiO34714.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15314; CAB15314; BSU33240.
GeneIDi938620.
KEGGibsu:BSU33240.
PATRICi18978646. VBIBacSub10457_3486.

Phylogenomic databases

eggNOGiENOG4105F0F. Bacteria.
COG2140. LUCA.
HOGENOMiHOG000200624.
InParanoidiO34714.
KOiK01569.
OMAiHARTFNY.
PhylomeDBiO34714.

Enzyme and pathway databases

BioCyciBSUB:BSU33240-MONOMER.
MetaCyc:BSU33240-MONOMER.
BRENDAi4.1.1.2. 658.
SABIO-RKO34714.

Miscellaneous databases

EvolutionaryTraceiO34714.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR017774. Bicupin_oxalate_deCO2ase/Oxase.
IPR006045. Cupin_1.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF00190. Cupin_1. 2 hits.
[Graphical view]
SMARTiSM00835. Cupin_1. 2 hits.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
TIGRFAMsiTIGR03404. bicupin_oxalic. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiOXDC_BACSU
AccessioniPrimary (citable) accession number: O34714
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 1, 1998
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.