UniProtKB - P32397 (CGOX_BACSU)
Coproporphyrinogen III oxidase
cgoX
Functioni
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:7928957, PubMed:9217019).
Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III (PubMed:8288631, PubMed:7928957, PubMed:9217019, PubMed:9784236).
Can also oxidize protoporphyrinogen IX to protoporphyrin-IX (PubMed:8288631, PubMed:7928957, PubMed:9217019, PubMed:9784236, PubMed:19944166).
The specific activity for the oxidation of coproporphyrinogen III is much higher than that for the oxidation of protoporphyrinogen IX (PubMed:7928957, PubMed:9217019).
Can also oxidize mesoporphyrinogen IX, but not uroporphyrinogen III (PubMed:8288631, PubMed:9784236, PubMed:7928957).
5 PublicationsCatalytic activityi
Cofactori
Activity regulationi
Kineticsi
- KM=0.56 µM for coproporphyrinogen III1 Publication
- KM=5.29 µM for coproporphyrinogen III1 Publication
- KM=0.95 µM for protoporphyrinogen IX1 Publication
- KM=10.4 µM for protoporphyrinogen IX1 Publication
- KM=1.0 µM for protoporphyrinogen IX1 Publication
- KM=21.1 µM for mesoporphyrinogen IX1 Publication
- KM=4.92 µM for mesoporphyrinogen IX1 Publication
- Vmax=7.0 nmol/min/mg enzyme with coproporphyrinogen III as substrate1 Publication
- Vmax=0.98 nmol/min/mg enzyme with coproporphyrinogen III as substrate1 Publication
- Vmax=0.85 nmol/min/mg enzyme with protoporphyrinogen IX as substrate1 Publication
- Vmax=3.7 nmol/min/mg enzyme with protoporphyrinogen IX as substrate1 Publication
- Vmax=45 nmol/min/mg enzyme with mesoporphyrinogen IX as substrate1 Publication
pH dependencei
: protoheme biosynthesis Pathwayi
This protein is involved in the pathway protoheme biosynthesis, which is part of Porphyrin-containing compound metabolism.1 Publication2 PublicationsView all proteins of this organism that are known to be involved in the pathway protoheme biosynthesis and in Porphyrin-containing compound metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 49 | FAD; via amide nitrogen1 Publication | 1 | |
Binding sitei | 256 | FAD; via amide nitrogen and carbonyl oxygenBy similarity | 1 | |
Binding sitei | 409 | FAD1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 12 – 17 | FAD1 Publication | 6 | |
Nucleotide bindingi | 41 – 42 | FAD1 Publication | 2 | |
Nucleotide bindingi | 63 – 66 | FAD1 Publication | 4 | |
Nucleotide bindingi | 448 – 450 | FAD1 Publication | 3 |
GO - Molecular functioni
- oxidoreductase activity Source: GO_Central
- oxygen-dependent protoporphyrinogen oxidase activity Source: InterPro
GO - Biological processi
- heme biosynthetic process Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Heme biosynthesis |
Ligand | FAD, Flavoprotein |
Enzyme and pathway databases
BioCyci | BSUB:BSU10140-MONOMER |
BRENDAi | 1.3.3.15, 658 1.3.3.4, 658 |
SABIO-RKi | P32397 |
UniPathwayi | UPA00252 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:cgoX1 Publication Synonyms:hemG1 Publication, hemY1 Publication Ordered Locus Names:BSU10140 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Cell membrane 1 Publication; Peripheral membrane protein 1 Publication
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, Cytoplasm, MembranePathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 64 | P → A: Decreased affinity for protoporphyrinogen-IX. 1 Publication | 1 | |
Mutagenesisi | 71 | K → A: Strongly decreased catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 176 | I → A: Strongly decreased catalytic activity. 1 Publication | 1 | |
Mutagenesisi | 227 | F → R: Decreased affinity for protoporphyrinogen-IX. 1 Publication | 1 | |
Mutagenesisi | 366 | Y → A or H: Reduces protoporphyrinogen oxidation by 90%. 1 Publication | 1 | |
Mutagenesisi | 366 | Y → E: Reduces protoporphyrinogen oxidation by 99%. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL1075048 |
DrugBanki | DB07338, Acifluorfen |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000135263 | 1 – 470 | Coproporphyrinogen III oxidaseAdd BLAST | 470 |
Proteomic databases
jPOSTi | P32397 |
PaxDbi | P32397 |
PRIDEi | P32397 |
Interactioni
Subunit structurei
Monomer.
3 PublicationsProtein-protein interaction databases
STRINGi | 224308.BSU10140 |
Chemistry databases
BindingDBi | P32397 |
Structurei
Secondary structure
3D structure databases
SMRi | P32397 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P32397 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG1232, Bacteria |
InParanoidi | P32397 |
OMAi | WFDQWFG |
PhylomeDBi | P32397 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002937, Amino_oxidase IPR036188, FAD/NAD-bd_sf IPR004572, Protoporphyrinogen_oxidase |
Pfami | View protein in Pfam PF01593, Amino_oxidase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
TIGRFAMsi | TIGR00562, proto_IX_ox, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MSDGKKHVVI IGGGITGLAA AFYMEKEIKE KNLPLELTLV EASPRVGGKI
60 70 80 90 100
QTVKKDGYII ERGPDSFLER KKSAPQLVKD LGLEHLLVNN ATGQSYVLVN
110 120 130 140 150
RTLHPMPKGA VMGIPTKIAP FVSTGLFSLS GKARAAMDFI LPASKTKDDQ
160 170 180 190 200
SLGEFFRRRV GDEVVENLIE PLLSGIYAGD IDKLSLMSTF PQFYQTEQKH
210 220 230 240 250
RSLILGMKKT RPQGSGQQLT AKKQGQFQTL STGLQTLVEE IEKQLKLTKV
260 270 280 290 300
YKGTKVTKLS HSGSCYSLEL DNGVTLDADS VIVTAPHKAA AGMLSELPAI
310 320 330 340 350
SHLKNMHSTS VANVALGFPE GSVQMEHEGT GFVISRNSDF AITACTWTNK
360 370 380 390 400
KWPHAAPEGK TLLRAYVGKA GDESIVDLSD NDIINIVLED LKKVMNINGE
410 420 430 440 450
PEMTCVTRWH ESMPQYHVGH KQRIKELREA LASAYPGVYM TGASFEGVGI
460 470
PDCIDQGKAA VSDALTYLFS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M97208 Genomic DNA Translation: AAA22519.1 Y14083 Genomic DNA Translation: CAA74520.1 AL009126 Genomic DNA Translation: CAB12854.1 |
PIRi | D47045 |
RefSeqi | NP_388895.1, NC_000964.3 WP_003245394.1, NZ_JNCM01000035.1 |
Genome annotation databases
EnsemblBacteriai | CAB12854; CAB12854; BSU_10140 |
GeneIDi | 936311 |
KEGGi | bsu:BSU10140 |
PATRICi | fig|224308.179.peg.1090 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M97208 Genomic DNA Translation: AAA22519.1 Y14083 Genomic DNA Translation: CAA74520.1 AL009126 Genomic DNA Translation: CAB12854.1 |
PIRi | D47045 |
RefSeqi | NP_388895.1, NC_000964.3 WP_003245394.1, NZ_JNCM01000035.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3I6D | X-ray | 2.90 | A/B | 1-470 | [»] | |
SMRi | P32397 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU10140 |
Chemistry databases
BindingDBi | P32397 |
ChEMBLi | CHEMBL1075048 |
DrugBanki | DB07338, Acifluorfen |
Proteomic databases
jPOSTi | P32397 |
PaxDbi | P32397 |
PRIDEi | P32397 |
Protocols and materials databases
DNASUi | 936311 |
Genome annotation databases
EnsemblBacteriai | CAB12854; CAB12854; BSU_10140 |
GeneIDi | 936311 |
KEGGi | bsu:BSU10140 |
PATRICi | fig|224308.179.peg.1090 |
Phylogenomic databases
eggNOGi | COG1232, Bacteria |
InParanoidi | P32397 |
OMAi | WFDQWFG |
PhylomeDBi | P32397 |
Enzyme and pathway databases
UniPathwayi | UPA00252 |
BioCyci | BSUB:BSU10140-MONOMER |
BRENDAi | 1.3.3.15, 658 1.3.3.4, 658 |
SABIO-RKi | P32397 |
Miscellaneous databases
EvolutionaryTracei | P32397 |
PROi | PR:P32397 |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002937, Amino_oxidase IPR036188, FAD/NAD-bd_sf IPR004572, Protoporphyrinogen_oxidase |
Pfami | View protein in Pfam PF01593, Amino_oxidase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
TIGRFAMsi | TIGR00562, proto_IX_ox, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CGOX_BACSU | |
Accessioni | P32397Primary (citable) accession number: P32397 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1993 |
Last sequence update: | October 1, 1993 | |
Last modified: | February 23, 2022 | |
This is version 155 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, Direct protein sequencing, 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