UniProtKB - P00183 (CPXA_PSEPU)

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History
Entry version 150 (23 May 2018)
Sequence version 2 (23 Jan 2007)
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Protein

Camphor 5-monooxygenase

Gene

camC

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Involved in a camphor oxidation system.

Catalytic activityⁱ

⁺-camphor + reduced putidaredoxin + O₂ = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H₂O.

Cofactorⁱ

heme

Pathwayⁱ: (R)-camphor degradation

This protein is involved in the pathway (R)-camphor degradation, which is part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the pathway (R)-camphor degradation and in Terpene metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Metal bindingⁱ	358	Iron (heme axial ligand)		1

GO - Molecular functionⁱ

camphor 5-monooxygenase activity Source: UniProtKB-EC
heme binding Source: InterPro
iron ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

(+)-camphor catabolic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Monooxygenase, Oxidoreductase
Ligand	Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-3021
BRENDAⁱ	1.14.15.1 5092
UniPathwayⁱ	UPA00719

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Camphor 5-monooxygenase (EC:1.14.15.1) Alternative name(s): Cytochrome P450-cam Short name: Cytochrome P450cam
Gene namesⁱ	Name:camC Synonyms:cyp101
Organismⁱ	Pseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifierⁱ	303 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas putida group

Subcellular locationⁱ

Cytoplasm By similarity

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL5594
Drug and drug target database More...DrugBankⁱ	DB02817 5-Exo-Hydroxycamphor DB03627 Adamantane DB04032 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Butyl-Amide DB03031 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Octyl-Amide DB02125 Adamantanone DB04501 Camphane DB01744 Camphor DB01011 Metyrapone DB01703 N-(2-Ferrocenylethyl)Maleimide DB01826 N-Butyl Isocyanide DB03540 Norcamphor DB02851 Thiocamphor

ChEMBLⁱ

CHEMBL5594

DrugBankⁱ

DB02817 5-Exo-Hydroxycamphor
DB03627 Adamantane
DB04032 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Butyl-Amide
DB03031 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Octyl-Amide
DB02125 Adamantanone
DB04501 Camphane
DB01744 Camphor
DB01011 Metyrapone
DB01703 N-(2-Ferrocenylethyl)Maleimide
DB01826 N-Butyl Isocyanide
DB03540 Norcamphor
DB02851 Thiocamphor

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000052204	2 – 415	Camphor 5-monooxygenaseAdd BLAST		414

Proteomic databases

PRIDEⁱ	P00183

PRIDEⁱ

P00183

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
camB	P00259	3	EBI-15706256,EBI-15706395

With

Entry

#Exp.

IntAct

Notes

camB

P00259

EBI-15706256,EBI-15706395

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-29809N
IntActⁱ	P00183, 1 interactor

Chemistry databases

BindingDBⁱ	P00183

BindingDBⁱ

P00183

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	6 – 8	Combined sources	3
Helixⁱ	21 – 23	Combined sources	3
Beta strandⁱ	29 – 31	Combined sources	3
Helixⁱ	35 – 37	Combined sources	3
Helixⁱ	39 – 43	Combined sources	5
Helixⁱ	44 – 47	Combined sources	4
Beta strandⁱ	48 – 51	Combined sources	4
Beta strandⁱ	53 – 57	Combined sources	5
Helixⁱ	59 – 61	Combined sources	3
Beta strandⁱ	63 – 66	Combined sources	4
Helixⁱ	69 – 77	Combined sources	9
Turnⁱ	79 – 81	Combined sources	3
Beta strandⁱ	82 – 86	Combined sources	5
Beta strandⁱ	88 – 90	Combined sources	3
Helixⁱ	91 – 96	Combined sources	6
Turnⁱ	100 – 103	Combined sources	4
Turnⁱ	106 – 108	Combined sources	3
Helixⁱ	109 – 120	Combined sources	12
Helixⁱ	122 – 143	Combined sources	22
Helixⁱ	144 – 146	Combined sources	3
Beta strandⁱ	147 – 150	Combined sources	4
Helixⁱ	151 – 154	Combined sources	4
Turnⁱ	155 – 157	Combined sources	3
Helixⁱ	158 – 168	Combined sources	11
Helixⁱ	172 – 174	Combined sources	3
Helixⁱ	175 – 186	Combined sources	12
Beta strandⁱ	190 – 192	Combined sources	3
Helixⁱ	194 – 214	Combined sources	21
Helixⁱ	220 – 225	Combined sources	6
Beta strandⁱ	230 – 233	Combined sources	4
Helixⁱ	236 – 251	Combined sources	16
Helixⁱ	253 – 266	Combined sources	14
Helixⁱ	269 – 277	Combined sources	9
Helixⁱ	279 – 281	Combined sources	3
Helixⁱ	282 – 292	Combined sources	11
Beta strandⁱ	298 – 304	Combined sources	7
Beta strandⁱ	306 – 308	Combined sources	3
Beta strandⁱ	311 – 313	Combined sources	3
Beta strandⁱ	318 – 321	Combined sources	4
Helixⁱ	323 – 328	Combined sources	6
Turnⁱ	330 – 332	Combined sources	3
Beta strandⁱ	333 – 335	Combined sources	3
Helixⁱ	354 – 356	Combined sources	3
Helixⁱ	361 – 378	Combined sources	18
Beta strandⁱ	382 – 384	Combined sources	3
Beta strandⁱ	395 – 397	Combined sources	3
Beta strandⁱ	399 – 401	Combined sources	3
Beta strandⁱ	404 – 406	Combined sources	3
Helixⁱ	409 – 411	Combined sources	3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1AKD	X-ray	1.80	A	2-415	[»]
	1C8J	X-ray	2.10	A/B	2-415	[»]
	1CP4	X-ray	1.90	A	2-415	[»]
	1DZ4	X-ray	1.60	A/B	2-415	[»]
	1DZ6	X-ray	1.90	A/B	2-415	[»]
	1DZ8	X-ray	1.90	A/B	2-415	[»]
	1DZ9	X-ray	1.90	A/B	2-415	[»]
	1GEB	X-ray	2.03	A	1-415	[»]
	1GEK	X-ray	1.70	A	1-415	[»]
	1GEM	X-ray	2.00	A	1-415	[»]
	1GJM	X-ray	2.20	A	2-415	[»]
	1IWI	X-ray	2.00	A	1-415	[»]
	1IWJ	X-ray	2.00	A	1-415	[»]
	1IWK	X-ray	2.00	A	1-415	[»]
	1J51	X-ray	2.20	A/B/C/D	2-415	[»]
	1K2O	X-ray	1.65	A/B	2-415	[»]
	1LWL	X-ray	2.20	A	1-415	[»]
	1MPW	X-ray	2.34	A/B	2-415	[»]
	1NOO	X-ray	2.20	A	2-415	[»]
	1O76	X-ray	1.80	A/B	2-415	[»]
	1P2Y	X-ray	2.30	A	2-415	[»]
	1P7R	X-ray	2.85	A	2-415	[»]
	1PHA	X-ray	1.63	A	2-415	[»]
	1PHB	X-ray	1.60	A	2-415	[»]
	1PHC	X-ray	1.60	A	2-415	[»]
	1PHD	X-ray	1.60	A	2-415	[»]
	1PHE	X-ray	1.60	A	2-415	[»]
	1PHF	X-ray	1.60	A	2-415	[»]
	1PHG	X-ray	1.60	A	2-415	[»]
	1QMQ	X-ray	1.55	A	2-415	[»]
	1RE9	X-ray	1.45	A	2-415	[»]
	1RF9	X-ray	1.80	A	1-415	[»]
	1T85	X-ray	1.80	A	2-415	[»]
	1T86	X-ray	1.90	A/B	2-415	[»]
	1T87	X-ray	1.80	A/B	2-415	[»]
	1T88	X-ray	1.90	A/B	2-415	[»]
	1UYU	X-ray	2.00	A/B	2-415	[»]
	1YRC	X-ray	1.40	A	2-415	[»]
	1YRD	X-ray	1.70	A	2-415	[»]
	2A1M	X-ray	2.10	A/B	1-415	[»]
	2A1N	X-ray	1.90	A/B	1-415	[»]
	2A1O	X-ray	1.55	A/B	1-415	[»]
	2CP4	X-ray	2.10	A	2-415	[»]
	2CPP	X-ray	1.63	A	2-415	[»]
	2FE6	X-ray	1.50	A	1-415	[»]
	2FER	X-ray	1.70	A	11-415	[»]
	2FEU	X-ray	1.70	A/B	11-415	[»]
	2FRZ	X-ray	2.10	A/B	2-415	[»]
	2GQX	X-ray	2.10	A/B	11-415	[»]
	2GR6	X-ray	2.30	A/B	11-415	[»]
	2H7Q	X-ray	1.50	A	2-415	[»]
	2H7R	X-ray	2.10	A	2-415	[»]
	2H7S	X-ray	2.15	A/C	2-415	[»]
	2L8M	NMR	-	A	1-415	[»]
	2LQD	NMR	-	A	3-415	[»]
	2M56	NMR	-	A	12-415	[»]
	2QBL	X-ray	1.80	A	1-415	[»]
	2QBM	X-ray	1.80	A	1-415	[»]
	2QBN	X-ray	1.75	A	1-415	[»]
	2QBO	X-ray	1.90	A	1-415	[»]
	2Z97	X-ray	1.80	A	1-415	[»]
	2ZAW	X-ray	1.55	A	1-415	[»]
	2ZAX	X-ray	1.60	A	1-415	[»]
2ZUH	X-ray	1.55	A	1-415	[»]
2ZUI	X-ray	1.50	A	1-415	[»]
2ZUJ	X-ray	1.60	A	1-415	[»]
2ZWT	X-ray	1.35	A	1-415	[»]
2ZWU	X-ray	1.30	A	1-415	[»]
3CP4	X-ray	2.30	A	2-415	[»]
3CPP	X-ray	1.90	A	2-415	[»]
3FWF	X-ray	1.83	A/B	11-415	[»]
3FWG	X-ray	1.55	A/B	11-415	[»]
3FWI	X-ray	2.40	A	11-415	[»]
3FWJ	X-ray	1.90	A	11-415	[»]
3L61	X-ray	1.50	A	2-415	[»]
3L62	X-ray	1.70	A	2-415	[»]
3L63	X-ray	1.50	A	2-415	[»]
3OIA	X-ray	1.65	A	2-415	[»]
3OL5	X-ray	1.75	A	2-415	[»]
3P6M	X-ray	2.00	A	2-415	[»]
3P6N	X-ray	1.70	A	2-415	[»]
3P6O	X-ray	2.00	A	2-415	[»]
3P6P	X-ray	1.90	A	2-415	[»]
3P6Q	X-ray	1.95	A	2-415	[»]
3P6R	X-ray	2.10	A	2-415	[»]
3P6S	X-ray	2.00	A	2-415	[»]
3P6T	X-ray	1.90	A	2-415	[»]
3P6U	X-ray	1.70	A	2-415	[»]
3P6V	X-ray	2.00	A	2-415	[»]
3P6W	X-ray	2.10	A	2-415	[»]
3P6X	X-ray	1.65	A	2-415	[»]
3W9C	X-ray	2.50	A	2-415	[»]
3WRH	X-ray	1.62	A/E	1-415	[»]
3WRI	X-ray	2.90	A/B	1-415	[»]
3WRJ	X-ray	1.85	A/E	1-415	[»]
3WRK	X-ray	2.61	A/D	1-415	[»]
3WRL	X-ray	1.65	A/E	1-415	[»]
3WRM	X-ray	1.95	A/F	1-415	[»]
4CP4	X-ray	2.10	A	2-415	[»]
4CPP	X-ray	2.11	A	2-415	[»]
4EK1	X-ray	1.97	A/B	2-415	[»]
4G3R	X-ray	2.20	A/B	2-415	[»]
4JWS	X-ray	2.15	A/B	1-415	[»]
4JWU	X-ray	2.20	A/B	1-415	[»]
4JX1	X-ray	2.09	A/B/E/F	1-415	[»]
4KKY	X-ray	2.00	X	2-414	[»]
4L49	X-ray	2.13	A	1-415	[»]
4L4A	X-ray	2.10	A	1-415	[»]
4L4B	X-ray	2.10	A	1-415	[»]
4L4C	X-ray	2.20	A/B	1-415	[»]
4L4D	X-ray	2.10	A	1-415	[»]
4L4E	X-ray	1.26	A	1-415	[»]
4L4F	X-ray	1.29	A	1-415	[»]
4L4G	X-ray	1.55	A	1-415	[»]
5CP4	X-ray	1.75	A	2-415	[»]
5CPP	X-ray	2.08	A	2-415	[»]
5GXG	X-ray	1.70	A	2-415	[»]
5IK1	X-ray	1.53	A	10-415	[»]
5WK7	X-ray	1.98	A	1-415	[»]
5WK9	X-ray	1.98	A	1-415	[»]
6CP4	X-ray	1.90	A	2-415	[»]
6CPP	X-ray	1.90	A	2-415	[»]
7CPP	X-ray	2.00	A	2-415	[»]
8CPP	X-ray	2.10	A	2-415	[»]
ProteinModelPortalⁱ	P00183
SMRⁱ	P00183
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P00183

EvolutionaryTraceⁱ

P00183

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the cytochrome P450 family.Curated

Phylogenomic databases

KEGG Orthology (KO) More...KOⁱ	K21569

KOⁱ

K21569

Family and domain databases

Gene3Dⁱ	1.10.630.10, 1 hit
InterProⁱ	View protein in InterPro IPR001128 Cyt_P450 IPR002397 Cyt_P450_B IPR017972 Cyt_P450_CS IPR036396 Cyt_P450_sf
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00067 p450, 1 hit
PRINTSⁱ	PR00359 BP450 PR00385 P450
SUPFAMⁱ	SSF48264 SSF48264, 1 hit
PROSITEⁱ	View protein in PROSITE PS00086 CYTOCHROME_P450, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P00183-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTTETIQSNA NLAPLPPHVP EHLVFDFDMY NPSNLSAGVQ EAWAVLQESN 
        60         70         80         90        100
VPDLVWTRCN GGHWIATRGQ LIREAYEDYR HFSSECPFIP REAGEAYDFI 
       110        120        130        140        150
PTSMDPPEQR QFRALANQVV GMPVVDKLEN RIQELACSLI ESLRPQGQCN 
       160        170        180        190        200
FTEDYAEPFP IRIFMLLAGL PEEDIPHLKY LTDQMTRPDG SMTFAEAKEA 
       210        220        230        240        250
LYDYLIPIIE QRRQKPGTDA ISIVANGQVN GRPITSDEAK RMCGLLLVGG 
       260        270        280        290        300
LDTVVNFLSF SMEFLAKSPE HRQELIERPE RIPAACEELL RRFSLVADGR 
       310        320        330        340        350
ILTSDYEFHG VQLKKGDQIL LPQMLSGLDE RENACPMHVD FSRQKVSHTT 
       360        370        380        390        400
FGHGSHLCLG QHLARREIIV TLKEWLTRIP DFSIAPGAQI QHKSGIVSGV 
       410 
QALPLVWDPA TTKAV

Length:415

Mass (Da):46,669

Last modified:January 23, 2007 - v2

Checksum:ⁱE84641B4A65DD2D3

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	56 – 57	Missing AA sequence (PubMed:7130171).Curated	2
Sequence conflictⁱ	277	E → Q AA sequence (PubMed:7130171).Curated	1
Sequence conflictⁱ	362	H → S AA sequence (PubMed:7130171).Curated	1
Sequence conflictⁱ	408	D → N AA sequence (PubMed:7130171).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M12546 Genomic DNA Translation: AAA25760.1 D00528 Genomic DNA Translation: BAA00412.1
PIRⁱ	A25660 O4PSCP

Genome annotation databases

KEGGⁱ	ag:AAA25760

KEGGⁱ

ag:AAA25760

Protein	Similar proteins		Species	Score	Length
P00183	Cytochrome P-450cam		PSEPU		415
UPI00006CA336		PSEPU		421
UPI00001E2D44		PSEPU		420
UPI000003C992		PSEPU		414
UPI0007B176AC		PSEPU		413
+36

Protein	Similar proteins		Species	Score	Length
P00183	Cytochrome P-450cam		PSEPU		415
Cytochrome		Sutterellaceae bacterium		410
Cytochrome P450		Pseudomonas bauzanensis		415
Cytochrome P450		Massilia namucuonensis		419
Uncharacterized protein		Rhodococcus sp. NCIMB 12038		401
+49

BindingDBⁱ	P00183
ChEMBLⁱ	CHEMBL5594
Drug and drug target database More...DrugBankⁱ	DB02817 5-Exo-Hydroxycamphor DB03627 Adamantane DB04032 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Butyl-Amide DB03031 Adamantane-1-Carboxylic Acid-5-Dimethylamino-Naphthalene-1-Sulfonylamino-Octyl-Amide DB02125 Adamantanone DB04501 Camphane DB01744 Camphor DB01011 Metyrapone DB01703 N-(2-Ferrocenylethyl)Maleimide DB01826 N-Butyl Isocyanide DB03540 Norcamphor DB02851 Thiocamphor

PRIDEⁱ	P00183

Structural Biology Knowledgebase	Search...

KEGGⁱ	ag:AAA25760

KEGG Orthology (KO) More...KOⁱ	K21569

UniPathwayⁱ	UPA00719
BioCycⁱ	MetaCyc:MONOMER-3021
BRENDAⁱ	1.14.15.1 5092

EvolutionaryTraceⁱ	P00183

Entry informationⁱ

Entry nameⁱ	CPXA_PSEPU
Accessionⁱ	P00183Primary (citable) accession number: P00183
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	January 23, 2007
	Last modified:	May 23, 2018
	This is version 150 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

UniProtKB

UniParc

Help

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Annotation systems

Supporting data

UniProtKB - P00183 (CPXA_PSEPU)

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Camphor 5-monooxygenase

camC

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: (R)-camphor degradation

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

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Functionⁱ

Pathwayⁱ: (R)-camphor degradation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ