Q9LR75 (HEM6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coproporphyrinogen-III oxidase, chloroplastic
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3

Alternative name(s):
Protein LESION INITIATION 2

Gene names

Name:	CPX
Synonyms:	CPO, HEMF, LIN2
Ordered Locus Names:	At1g03475
ORF Names:	F21B7.10

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	386 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III By similarity.
Catalytic activity	Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › chloroplast Probable.
Sequence similarities	Belongs to the aerobic coproporphyrinogen-III oxidase family.
Sequence caution	The sequence AAK53008.1 differs from that shown. Reason: Erroneous initiation. The sequence AAM47469.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR
Molecular function	coproporphyrinogen oxidase activity Inferred from electronic annotation. Source: EC protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 48	48	Chloroplast Potential
	Chain	49 – 386	338	Coproporphyrinogen-III oxidase, chloroplastic		PRO_0000006031
Regions
	Region	125 – 134	10	Important for dimerization By similarity
	Region	190 – 192	3	Substrate binding By similarity
	Region	326 – 361	36	Important for dimerization By similarity
	Region	344 – 349	6	Substrate binding By similarity
Sites
	Active site	188	1	Proton donor By similarity
	Binding site	174	1	Substrate By similarity
	Site	261	1	Important for dimerization By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9LR75 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B82BD6787643D0B8	FASTA	386	43,796
	10 20 30 40 50 60 MASHSSTLLS SPTFAPFSSH RLHYSPNPST LRFSRPIRNK PNLALRCSVS IEKEVPETER 70 80 90 100 110 120 PFTFLRDSDD VTPSSSSSSV RARFETMIRA AQDSVCDAIE AIEGGPKFKE DVWSRPGGGG 130 140 150 160 170 180 GISRVLQDGN VFEKAGVNVS VVYGVMPPEA YRAAKGSASD QKPGPVPFFA AGVSSVLHPK 190 200 210 220 230 240 NPFAPTLHFN YRYFETDAPK DVPGAPRQWW FGGGTDFTPA YIFEEDVKHF HSIQKQACDK 250 260 270 280 290 300 FDPSFYPRFK KWCDDYFYIK HRDERRGLGG IFFDDLNDYD QEMLLSFATE CANSVVPAYI 310 320 330 340 350 360 PIVEKRKDME FTEQHKAWQQ LRRGRYVEFN LVYDRGTTFG LKTGGRIESI LVSLPLSARW 370 380 EYDHKPEEGT EEWKLLDACI NPKEWI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A deficiency of coproporphyrinogen III oxidase causes lesion formation in Arabidopsis." Ishikawa A., Okamoto H., Iwasaki Y., Asahi T. Plant J. 27:89-99(2001) [PubMed: 11489187] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation of genes and subcellular localization of tetrapyrrole biosynthetic enzymes from Arabidopsis." Tan F.C. Thesis (2001), University of Cambridge, United Kingdom Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[3]	"Molecular characterisation of coproporphyrinogen oxidase from Glycine max and Arabidopsis thaliana." Santana M.A., Tan F.C., Smith A.G. Plant Physiol. Biochem. 40:289-298(2002) Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Landsberg erecta.
[4]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[6]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-386. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB044394 mRNA. Translation: BAB61876.1. AJ420796 mRNA. Translation: CAD12661.1. AC002560 Genomic DNA. Translation: AAF86536.1. CP002684 Genomic DNA. Translation: AEE27577.1. AF375424 mRNA. Translation: AAK53008.1. Different initiation. AY113166 mRNA. Translation: AAM47469.1. Different initiation.
IPI	IPI00519439.
PIR	C86166.
RefSeq	NP_171847.4. NM_100230.6.
UniGene	At.19140.
3D structure databases
ProteinModelPortal	Q9LR75.
SMR	Q9LR75. Positions 76-386.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9LR75.
Proteomic databases
PRIDE	Q9LR75.
ProMEX	Q9LR75.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G03475.1; AT1G03475.1; AT1G03475.
GeneID	839489.
GenomeReviews	Gene locus AT1G03475 in contig CT485782_GR.
KEGG	ath:AT1G03475.
Organism-specific databases
TAIR	At1g03475.
Phylogenomic databases
eggNOG	KOG1518.
GeneTree	EPGT00050000012010.
HOGENOM	HBG631180.
InParanoid	Q9LR75.
PhylomeDB	Q9LR75.
ProtClustDB	PLN02873.
Enzyme and pathway databases
BioCyc	ARA:AT1G03475-MONOMER. MetaCyc:AT1G03475-MONOMER.
Gene expression databases
Genevestigator	Q9LR75.
GermOnline	AT1G03475. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001260. Coprogen_oxidase_aer. IPR018375. Coprogen_oxidase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
KO	K00228.
PANTHER	PTHR10755. Coprogen_oxidas. 1 hit.
Pfam	PF01218. Coprogen_oxidas. 1 hit. [Graphical view]
PIRSF	PIRSF000166. Coproporphyri_ox. 1 hit.
PRINTS	PR00073. COPRGNOXDASE.
SUPFAM	SSF102886. Coprogen_oxidas. 1 hit.
PROSITE	PS01021. COPROGEN_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM6_ARATH

Accession

Primary (citable) accession number: Q9LR75
Secondary accession number(s): Q546I5, Q94JR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 1, 2000
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program