ID   HEM62_NOSS1             Reviewed;         347 AA.
AC   Q8YX58;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Coproporphyrinogen-III oxidase, aerobic 2;
DE            Short=Coprogen oxidase 2 {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=Coproporphyrinogenase 2 {ECO:0000255|HAMAP-Rule:MF_00333};
DE            EC=1.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00333};
GN   Name=hemF2 {ECO:0000255|HAMAP-Rule:MF_00333}; OrderedLocusNames=all1357;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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 (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         Evidence={ECO:0000255|HAMAP-Rule:MF_00333};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC       route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00333}.
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DR   EMBL; BA000019; BAB73314.1; -; Genomic_DNA.
DR   PIR; AB1976; AB1976.
DR   RefSeq; WP_010995529.1; NC_003272.1.
DR   AlphaFoldDB; Q8YX58; -.
DR   SMR; Q8YX58; -.
DR   STRING; 103690.17130704; -.
DR   EnsemblBacteria; BAB73314; BAB73314; BAB73314.
DR   KEGG; ana:all1357; -.
DR   eggNOG; COG0408; Bacteria.
DR   OMA; WFGGITD; -.
DR   OrthoDB; 1086432at2; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1500.10; -; 1.
DR   HAMAP; MF_00333; Coprogen_oxidas; 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   3: Inferred from homology;
KW   Cytoplasm; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..347
FT                   /note="Coproporphyrinogen-III oxidase, aerobic 2"
FT                   /id="PRO_0000109881"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..84
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   REGION          287..322
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   ACT_SITE        133
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         135..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         305..310
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   SITE            197
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ   SEQUENCE   347 AA;  40031 MW;  402D8DFB7BB51D29 CRC64;
     MGRHSDNSLQ ESANHTVLLT SPTNTIPKDS RQRSQQFMQN LQDEICTALE QLDGKASFHQ
     DHWERAEGGE GRTRVIREGR VFEQGGVNFS AVWGNSLPAS ILAQRPEAAG HEFFATGTSM
     VLHPRNPYVP TVHLNYRYFE AGPIWWFGGG ADLTPYYAFK EDAVHFHQTL KNACDVHNPE
     YYPTFKRWCD EYFYLRHREE QRGIGGIFFD YQDASGKLYV ESQTDSSVAI YSQKVGNVAR
     NWEDIFAFVQ SCGQAFLPAY LPIVERRQGI EYGDRQRNFQ LYRRGRYVEF NLVYDRGTVF
     GLQTKGRTES ILMSLPPLAR WEYCYEPEAG SPEAELTEVF LQPRDWV