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Entry: I0IQ78_LEPFC
LinkDB: I0IQ78_LEPFC
Original site: I0IQ78_LEPFC 
ID   I0IQ78_LEPFC            Unreviewed;       466 AA.
AC   I0IQ78;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE            EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN   OrderedLocusNames=LFE_1748 {ECO:0000313|EMBL:BAM07427.1};
OS   Leptospirillum ferrooxidans (strain C2-3).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM07427.1, ECO:0000313|Proteomes:UP000007382};
RN   [1] {ECO:0000313|EMBL:BAM07427.1, ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|EMBL:BAM07427.1,
RC   ECO:0000313|Proteomes:UP000007382};
RX   PubMed=22815442; DOI=10.1128/JB.00696-12;
RA   Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT   Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT   Japan.";
RL   J. Bacteriol. 194:4122-4123(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA   Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA   Kamijo T., Ohta H.;
RT   "The complete genome sequence of the pioneer microbe on fresh volcanic
RT   deposit, Leptospirillum ferrooxidans strain C2-3.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-
CC         deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX;
CC         Xref=Rhea:RHEA:15425, ChEBI:CHEBI:16526, ChEBI:CHEBI:17319,
CC         ChEBI:CHEBI:57307, ChEBI:CHEBI:57309, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:59789; EC=1.3.98.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001496,
CC         ECO:0000256|PIRNR:PIRNR000167};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000167,
CC         ECO:0000256|PIRSR:PIRSR000167-2};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet
CC       route): step 1/1. {ECO:0000256|ARBA:ARBA00004785,
CC       ECO:0000256|PIRNR:PIRNR000167}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR000167}.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC       family. {ECO:0000256|ARBA:ARBA00005493, ECO:0000256|PIRNR:PIRNR000167}.
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DR   EMBL; AP012342; BAM07427.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0IQ78; -.
DR   STRING; 1162668.LFE_1748; -.
DR   KEGG; lfc:LFE_1748; -.
DR   PATRIC; fig|1162668.3.peg.2077; -.
DR   eggNOG; COG0635; Bacteria.
DR   HOGENOM; CLU_027579_3_0_0; -.
DR   OMA; HILNLMC; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000007382; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 1.10.10.920; -; 1.
DR   Gene3D; 3.30.750.200; -; 1.
DR   InterPro; IPR004558; Coprogen_oxidase_HemN.
DR   InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR   InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR007197; rSAM.
DR   NCBIfam; TIGR00538; hemN; 1.
DR   PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1.
DR   PANTHER; PTHR13932:SF6; OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE; 1.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF000167; HemN; 1.
DR   SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR000167};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000167};
KW   Iron {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-2};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR000167, ECO:0000256|PIRSR:PIRSR000167-
KW   2};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR000167};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW   ECO:0000256|PIRNR:PIRNR000167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007382};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-1}.
FT   DOMAIN          54..289
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   BINDING         63
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-2"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-2"
FT   BINDING         75..77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         76
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-2"
FT   BINDING         120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         154
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         193
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         252
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000167-1"
SQ   SEQUENCE   466 AA;  52790 MW;  3A99A217880BBE89 CRC64;
     MTPNMMAGTQ VSRELLKKYD VAGPRYTSYP TAPVWTTDFT AENYRDAINR GQSKKPDKPL
     SLYFHLPFCD SLCYFCGCSV IISRDRGKTA DYIDLLATEM ALVGPLYSKK RKVVQLHFGG
     GSPSNLTPPQ NRLLFSHINK WFNVDYSQGE ISVEIDPRHA SNDYLASIRD LGVNRISMGV
     QDFDPKVQAA VNRIQPVALT EGVFNECRKL NFNGINIDLI YGLPFQTVEG FAQTLDQVIR
     MSPDRIAVFN YAHVPWLKKH MVLIKEKDLP SPEVKFALMS MILDRLTGAG YVVIGMDHFA
     KPDDELTKAQ KEHSLYRNFQ GYTTKAEADL VGMGVTAISM VGDVYSQNLK SLPDYQKAVM
     AGDLPVHRGY KLSLDDEMRR LVITRIMCDL EINRQNVLDP FGKNFDQVFT KEIEELDRFQ
     QDGLLIITPE KITLTTTGRI FMRNIAMTFD RYLNVSAKGP LFSRTL
//
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