ID HEMN_CERS5 Reviewed; 452 AA. AC P95651; A4WR64; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 27-MAR-2024, entry version 132. DE RecName: Full=Oxygen-independent coproporphyrinogen III oxidase; DE Short=CPO; DE EC=1.3.98.3 {ECO:0000250|UniProtKB:P32131}; DE AltName: Full=Coproporphyrinogen III dehydrogenase; DE Short=CPDH; GN Name=hemN; OrderedLocusNames=Rsph17025_0977; OS Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter OS sphaeroides). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales; OC Paracoccaceae; Cereibacter. OX NCBI_TaxID=349102; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Shi J., Bartnikas T.B., Shapleigh J.P.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17025 / ATH 2.4.3; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M., RA Donohue T.J., Kaplan S.; RT "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the heme and chlorophyll biosynthesis. Catalyzes CC the anaerobic oxidative decarboxylation of propionate groups of rings A CC and B of coproporphyrinogen III to yield the vinyl groups in CC protoporphyrinogen IX. {ECO:0000250|UniProtKB:P32131}. 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:0000250|UniProtKB:P32131}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P32131}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:P32131}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet CC route): step 1/1. CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P32131}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32131}. CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U80081; AAB38508.1; -; Genomic_DNA. DR EMBL; CP000661; ABP69878.1; -; Genomic_DNA. DR PIR; T10882; T10882. DR AlphaFoldDB; P95651; -. DR SMR; P95651; -. DR STRING; 349102.Rsph17025_0977; -. DR KEGG; rsq:Rsph17025_0977; -. DR eggNOG; COG0635; Bacteria. DR HOGENOM; CLU_027579_3_0_5; -. DR BioCyc; RSPH349102:G1G8M-1002-MONOMER; -. DR UniPathway; UPA00251; UER00323. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0051989; F:coproporphyrinogen dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISS:UniProtKB. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; ISS:UniProtKB. DR Gene3D; 1.10.10.920; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004558; Coprogen_oxidase_HemN. DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. 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; 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; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; KW Porphyrin biosynthesis; S-adenosyl-L-methionine. FT CHAIN 1..452 FT /note="Oxygen-independent coproporphyrinogen III oxidase" FT /id="PRO_0000109949" FT DOMAIN 45..278 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 54 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 60 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 64 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 66 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 67 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 111 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 112..113 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 144 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 171 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 183 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 208 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 242 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 328 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT CONFLICT 22 FT /note="S -> C (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 70 FT /note="R -> P (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 197..198 FT /note="LR -> CA (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 302 FT /note="S -> T (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 306 FT /note="R -> G (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="G -> A (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="I -> L (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" FT CONFLICT 443 FT /note="T -> S (in Ref. 1; AAB38508)" FT /evidence="ECO:0000305" SQ SEQUENCE 452 AA; 49947 MW; 814AFC17EE710CDA CRC64; MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYIHVPFC ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKKHLPA GVKAGRLHWG GGTPTILSPE LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV DEPKIRALSE EGMNRASIGI QDFTDIVQSA IGREQPFENT RACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLQ LGPDRVAIFG YAHVPWMAKR QKLIDENVLP NDMERHELAN LAAKMFTEGG FERIGIDHFA RPDDSMAVAA RSGKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKAIE EGRLPGYRGH RMTDEDYLHG RAIEMIMCEF RLDLPALRAR FGEAAETMVP RITEAAAKFA PFITVDEAGS MSIEAEGRAL TRMIARVFDA YETPEARYSQ AS //