HEM61_ARATH
ID HEM61_ARATH Reviewed; 386 AA.
AC Q9LR75; Q546I5; Q94JR5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Coproporphyrinogen-III oxidase 1, chloroplastic;
DE Short=AtCPO-I;
DE Short=Coprogen oxidase;
DE Short=Coproporphyrinogenase;
DE EC=1.3.3.3;
DE AltName: Full=Protein LESION INITIATION 2;
DE Flags: Precursor;
GN Name=CPX1; Synonyms=CPO, HEMF, HEMF1, LIN2; OrderedLocusNames=At1g03475;
GN ORFNames=F21B7.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11489187; DOI=10.1046/j.1365-313x.2001.01058.x;
RA Ishikawa A., Okamoto H., Iwasaki Y., Asahi T.;
RT "A deficiency of coproporphyrinogen III oxidase causes lesion formation in
RT Arabidopsis.";
RL Plant J. 27:89-99(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RA Santana M.A., Tan F.C., Smith A.G.;
RT "Molecular characterisation of coproporphyrinogen oxidase from Glycine max
RT and Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 40:289-298(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-386.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Key enzyme in heme biosynthesis. Catalyzes the oxidative
CC decarboxylation of propionic acid side chains of rings A and B of
CC coproporphyrinogen III. {ECO:0000269|PubMed:11489187,
CC ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC route): step 1/1.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|Ref.2}. Plastid
CC {ECO:0000269|Ref.2}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledons, leaves and roots.
CC {ECO:0000269|Ref.2}.
CC -!- DISRUPTION PHENOTYPE: Spontaneous formation of necrotic leaf lesions.
CC {ECO:0000269|PubMed:11489187}.
CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK53008.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAM47469.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB044394; BAB61876.1; -; mRNA.
DR EMBL; AJ420796; CAD12661.1; -; mRNA.
DR EMBL; AC002560; AAF86536.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27577.1; -; Genomic_DNA.
DR EMBL; AF375424; AAK53008.1; ALT_INIT; mRNA.
DR EMBL; AY113166; AAM47469.1; ALT_INIT; mRNA.
DR PIR; C86166; C86166.
DR RefSeq; NP_171847.4; NM_100230.7.
DR AlphaFoldDB; Q9LR75; -.
DR SMR; Q9LR75; -.
DR BioGRID; 24724; 17.
DR STRING; 3702.AT1G03475.1; -.
DR iPTMnet; Q9LR75; -.
DR MetOSite; Q9LR75; -.
DR PaxDb; Q9LR75; -.
DR PRIDE; Q9LR75; -.
DR ProteomicsDB; 230318; -.
DR EnsemblPlants; AT1G03475.1; AT1G03475.1; AT1G03475.
DR GeneID; 839489; -.
DR Gramene; AT1G03475.1; AT1G03475.1; AT1G03475.
DR KEGG; ath:AT1G03475; -.
DR Araport; AT1G03475; -.
DR TAIR; locus:2825062; AT1G03475.
DR eggNOG; KOG1518; Eukaryota.
DR HOGENOM; CLU_026169_0_1_1; -.
DR InParanoid; Q9LR75; -.
DR OMA; HDKGTLF; -.
DR OrthoDB; 1080991at2759; -.
DR PhylomeDB; Q9LR75; -.
DR BioCyc; ARA:AT1G03475-MON; -.
DR BioCyc; MetaCyc:AT1G03475-MON; -.
DR BRENDA; 1.3.3.3; 399.
DR UniPathway; UPA00251; UER00322.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9LR75; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LR75; baseline and differential.
DR Genevisible; Q9LR75; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.1500.10; -; 1.
DR InterPro; IPR001260; Coprogen_oxidase_aer.
DR InterPro; IPR036406; Coprogen_oxidase_aer_sf.
DR InterPro; IPR018375; Coprogen_oxidase_CS.
DR PANTHER; PTHR10755; PTHR10755; 1.
DR Pfam; PF01218; Coprogen_oxidas; 1.
DR PIRSF; PIRSF000166; Coproporphyri_ox; 1.
DR PRINTS; PR00073; COPRGNOXDASE.
DR SUPFAM; SSF102886; SSF102886; 1.
DR PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE 2: Evidence at transcript level;
KW Chlorophyll biosynthesis; Chloroplast; Heme biosynthesis; Oxidoreductase;
KW Plastid; Porphyrin biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..386
FT /note="Coproporphyrinogen-III oxidase 1, chloroplastic"
FT /id="PRO_0000006031"
FT REGION 125..134
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT REGION 326..361
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190..192
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 344..349
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
SQ SEQUENCE 386 AA; 43796 MW; B82BD6787643D0B8 CRC64;
MASHSSTLLS SPTFAPFSSH RLHYSPNPST LRFSRPIRNK PNLALRCSVS IEKEVPETER
PFTFLRDSDD VTPSSSSSSV RARFETMIRA AQDSVCDAIE AIEGGPKFKE DVWSRPGGGG
GISRVLQDGN VFEKAGVNVS VVYGVMPPEA YRAAKGSASD QKPGPVPFFA AGVSSVLHPK
NPFAPTLHFN YRYFETDAPK DVPGAPRQWW FGGGTDFTPA YIFEEDVKHF HSIQKQACDK
FDPSFYPRFK KWCDDYFYIK HRDERRGLGG IFFDDLNDYD QEMLLSFATE CANSVVPAYI
PIVEKRKDME FTEQHKAWQQ LRRGRYVEFN LVYDRGTTFG LKTGGRIESI LVSLPLSARW
EYDHKPEEGT EEWKLLDACI NPKEWI
