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Entry: A0A1H8NLA6_9BURK
LinkDB: A0A1H8NLA6_9BURK
Original site: A0A1H8NLA6_9BURK 
ID   A0A1H8NLA6_9BURK        Unreviewed;       495 AA.
AC   A0A1H8NLA6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Coproporphyrinogen-III oxidase {ECO:0000256|PIRNR:PIRNR000167};
DE            EC=1.3.98.3 {ECO:0000256|PIRNR:PIRNR000167};
GN   ORFNames=SAMN05428959_106181 {ECO:0000313|EMBL:SEO30163.1};
OS   Duganella sp. CF517.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1881038 {ECO:0000313|EMBL:SEO30163.1, ECO:0000313|Proteomes:UP000198691};
RN   [1] {ECO:0000313|Proteomes:UP000198691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF517 {ECO:0000313|Proteomes:UP000198691};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FODC01000006; SEO30163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8NLA6; -.
DR   STRING; 1881038.SAMN05428959_106181; -.
DR   OrthoDB; 9808022at2; -.
DR   UniPathway; UPA00251; UER00323.
DR   Proteomes; UP000198691; Unassembled WGS sequence.
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   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:UP000198691};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000167,
KW   ECO:0000256|PIRSR:PIRSR000167-1}.
FT   DOMAIN          78..314
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
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         93
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         97
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         99..101
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         100
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         144
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         145..146
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         179
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         206
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         243
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         277
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         363
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   495 AA;  54941 MW;  C21741E4F9A41026 CRC64;
     MHTSPSAPRS PSQGPTHSAG PSHAGVGAAF PAVEFDAAII GKLSQSGPRY TSYPTADRFT
     PEFGYGQFLE AVAGLRMRRS QRPLSLYIHI PFCDTVCYYC GCNKIVTKDH GKAATYLGYL
     KQELDMQGRL FAGIGQLEQL HFGGGTPTYL SDRQMGDLMA HLRANFDFAP DAQGEYSIEI
     DPRTVSVERV HSLRAQGFNR ISLGVQDFDA DVQKAVNRIQ PEAETRAVID AARDAGFRSV
     SIDLIYGLPK QTIASMERTM EKVIAASPDR IALYNYAHLP HLFKPQRRIL DADLPSAAVK
     LDLLALCIER LCAAGYVYIG MDHFAKPDDE LAVAQRQGRL QRNFQGYSTR AETDLIACGV
     SAISAVGATY SQNEKTLDAY YEKLDGGVLP ITRGIKLDTD DLLRRIVIQK LMCNFELSIS
     SLEQAYPIRF PLYFADELEK LKAFEDDGLL TVDAHWISVT PKGRLLIRNI CMVFDRHLTL
     ARADTTQPLR YSKTI
//
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