HEMN_CERS5
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 03-AUG-2022, entry version 126.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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}.
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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 EnsemblBacteria; ABP69878; ABP69878; Rsph17025_0977.
DR KEGG; rsq:Rsph17025_0977; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_3_0_5; -.
DR OMA; CERLCWF; -.
DR OrthoDB; 1130951at2; -.
DR BioCyc; RSPH349102:G1G8M-1002-MON; -.
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; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR004558; Coprogen_oxidase_HemN.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000167; HemN; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00538; hemN; 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
