ID   HEM6_HORVU              Reviewed;         391 AA.
AC   Q42840;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase, chloroplastic;
DE            Short=Coprogen oxidase;
DE            Short=Coproporphyrinogenase;
DE            EC=1.3.3.3;
DE   Flags: Precursor;
GN   Name=CPX;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Svalofs Bonus; TISSUE=Leaf;
RX   PubMed=7580857; DOI=10.1007/bf01106776;
RA   Kruse E., Mock H.-P., Grimm B.;
RT   "Coproporphyrinogen III oxidase from barley and tobacco -- sequence
RT   analysis and initial expression studies.";
RL   Planta 196:796-803(1995).
CC   -!- FUNCTION: Involved in the heme and chlorophyll biosynthesis. Catalyzes
CC       the aerobic oxidative decarboxylation of propionate groups of rings A
CC       and B of coproporphyrinogen-III to yield the vinyl groups in
CC       protoporphyrinogen-IX (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82830; CAA58037.1; -; mRNA.
DR   PIR; T04486; T04486.
DR   AlphaFoldDB; Q42840; -.
DR   SMR; Q42840; -.
DR   ChEMBL; CHEMBL2366495; -.
DR   PRIDE; Q42840; -.
DR   UniPathway; UPA00251; UER00322.
DR   ExpressionAtlas; Q42840; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..391
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase,
FT                   chloroplastic"
FT                   /id="PRO_0000006032"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..134
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          331..366
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         349..354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            266
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  43556 MW;  BD3549559F2EB2CB CRC64;
     MASSLLTTPS QTLAPNPAAA RARRSSPAAA QVSFSSPLLP GRRALRCARP VAIEKEVPEK
     EAPTTFLRED GSGAGSGSVR ERFEGMIRRV QGEICAALEE ADGSGKRFVE DVWSRPGGVC
     VHSRVLQDGN VFEKAGVNVS AVIGVCPRSA YRAAKGAAKN GAADGHKAGP VPFFSAGISS
     VLHPKNPFAP TLHFNYRYFE TDAPKDVPGA PRSWWFGGGT DLTPSYLIEE DVKHFHSVQK
     QTCDKFDPSF YPRFKKWCDD YFYIKHRNER RGLGGIFFDD LNDYDQDMLL NFATECAGSV
     IPAYIPIIER RKDTPFNEEQ KAWQQVRRGR YVEFNLVYDR GTTFGLKTGG RIESILVSLP
     LTARWEYDHK PEEGSEEWKL LDACINPKEW L