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HEM6_FRAT1
ID   HEM6_FRAT1              Reviewed;         308 AA.
AC   Q14HF0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=CPO {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=Coprogen oxidase {ECO:0000255|HAMAP-Rule:MF_00333};
DE            Short=Coproporphyrinogenase {ECO:0000255|HAMAP-Rule:MF_00333};
DE            EC=1.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00333};
GN   Name=hemF {ECO:0000255|HAMAP-Rule:MF_00333}; OrderedLocusNames=FTF1063;
OS   Francisella tularensis subsp. tularensis (strain FSC 198).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC 198;
RX   PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA   Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA   Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA   Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT   "Genome sequencing shows that European isolates of Francisella tularensis
RT   subspecies tularensis are almost identical to US laboratory strain Schu
RT   S4.";
RL   PLoS ONE 2:E352-E352(2007).
CC   -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic
CC       oxidative decarboxylation of propionate groups of rings A and B of
CC       coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-
CC       IX. {ECO:0000255|HAMAP-Rule:MF_00333}.
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
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; AM286280; CAL09079.1; -; Genomic_DNA.
DR   RefSeq; WP_003023689.1; NC_008245.1.
DR   AlphaFoldDB; Q14HF0; -.
DR   SMR; Q14HF0; -.
DR   KEGG; ftf:FTF1063; -.
DR   HOGENOM; CLU_026169_0_1_6; -.
DR   OMA; HDKGTLF; -.
DR   UniPathway; UPA00251; UER00322.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; Heme biosynthesis; Metal-binding; Oxidoreductase;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..308
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT                   /id="PRO_1000133181"
FT   REGION          248..283
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         104
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         114
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         116..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         153
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         183
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         266..268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   SITE            183
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ   SEQUENCE   308 AA;  35854 MW;  492C4954C84C8201 CRC64;
     MQEKISKFED FLTQLQQNIT TALEQHETNA AKFISDKWQK PDTHDQKLKG YGNSMIIEGG
     EIFEKGVVAF SRVHGSELPP SATAKRQELA GKSFIATGLS LVIHPRNPFV PTSHANFRIF
     IAGADTDNPI WWFGGGFDLT PYYPFEEDAI HWHQTAKNIC DKHDKTYYPK FKKWCDEYFY
     LKHRDECRGV GGLFFDDLND KSFDECFNFV TDCANSYLDA YIPIVAQRKN IEYSQKHKDF
     QLYRRGRYVE FNLVFDRGTI FGLQSGGRTE SILSSMPPIA TWKYNWQPEL GSEEEKVYQY
     IKPRDWIK
 
 
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