ID   HEM6_TOBAC              Reviewed;         397 AA.
AC   Q42946;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 98.
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   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. SR1; 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}.
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DR   EMBL; X82831; CAA58038.1; -; mRNA.
DR   PIR; T02929; T02929.
DR   RefSeq; NP_001312882.1; NM_001325953.1.
DR   AlphaFoldDB; Q42946; -.
DR   SMR; Q42946; -.
DR   STRING; 4097.Q42946; -.
DR   GeneID; 107815524; -.
DR   KEGG; nta:107815524; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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-KW.
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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..397
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase,
FT                   chloroplastic"
FT                   /id="PRO_0000006034"
FT   REGION          76..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..144
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          337..372
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        199
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         355..360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            272
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  44936 MW;  CF48884871E7EEA2 CRC64;
     MLTPILSSAS CSWTPTSQFP HSWHSSPSFL TKPLNLPFTE SYKTAKRPTP NYSFKVQAMI
     EKEVAVSHKP DAFLRESDMG SNVTSNSSSV RGRFEKMRRE AQDSVCLAIE KADGGAKFKE
     DVWSRPGGGG GHSSVLQDGA VFEKAGVNVS VVYGVMPPEA YRAARPTDNG NVKPGPIPFF
     AAGVSSVLHP KNPFAPTLHF NYRYFETDAP KDAPGAPRQW WFGGGTDFTP AYIFEEDVKH
     FHSVQKAACD KFDASFYPRF KKWCVDYFYI KHRDERRGLG GIFFDDFNDY DQEMLLSFST
     ECANSVIPAY IPIVEKRKDT PFTDKHKAWQ QLRRGRYVEF NLVYDRGTTF GLKTGGRIES
     ILVSLPLTAR WEYDHKPEEG TEEWKLLDAC INPKEWI