HEMN_CERS4
ID HEMN_CERS4 Reviewed; 450 AA.
AC P51008; Q3J009;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
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=hemZ; OrderedLocusNames=RHOS4_23070; ORFNames=RSP_0699;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7592416; DOI=10.1128/jb.177.22.6422-6431.1995;
RA Zeilstra-Ryalls J.H., Kaplan S.;
RT "Aerobic and anaerobic regulation in Rhodobacter sphaeroides 2.4.1: the
RT role of the fnrL gene.";
RL J. Bacteriol. 177:6422-6431(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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:0000269|PubMed:7592416}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
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DR EMBL; Z49746; CAA89819.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA79875.1; -; Genomic_DNA.
DR RefSeq; WP_011338424.1; NZ_CP030271.1.
DR RefSeq; YP_353776.1; NC_007493.2.
DR AlphaFoldDB; P51008; -.
DR SMR; P51008; -.
DR STRING; 272943.RSP_0699; -.
DR EnsemblBacteria; ABA79875; ABA79875; RSP_0699.
DR KEGG; rsp:RSP_0699; -.
DR PATRIC; fig|272943.9.peg.2651; -.
DR eggNOG; COG0635; Bacteria.
DR OMA; LMCNLEL; -.
DR PhylomeDB; P51008; -.
DR UniPathway; UPA00251; UER00323.
DR Proteomes; UP000002703; Chromosome 1.
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; IMP: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:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP: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; Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..450
FT /note="Oxygen-independent coproporphyrinogen III oxidase"
FT /id="PRO_0000109950"
FT DOMAIN 45..282
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"
SQ SEQUENCE 450 AA; 49103 MW; CD391AB6F80BBA3E CRC64;
MAAVSHLAKL GLFDARVPRY TSYPTAPNFG VGVTENLHAD WISSIPAGGS ISLYLHVPFC
RRLCWFCACR TQGTSSDAPV RAYAAALKSE LALLRARLAP GVRLARMHWG GGTPTLLPPT
LIHELALAIR DAVPSDAETD FSVEIDPTEI DAARLDALFE AGMTRVSIGV QDFDPLIQQS
IGREQSFELT QRLTEDLRHR GLMGLDADIL YGLPHQTAPG VADSVQKLLS LSPDRVAVLG
YAHVPAVSRR QLMIPTASIP GPEERLDLFE TARTLILWDG YQQVGLDHFA RAGDPLAHAH
ACGRLCRSFQ GYTDDRAEVL IGLGASAISR FPQGFTQNAP STSDHLRAIR SGRFSTARGH
VLSDEDRLRG RMIEQLLCEF RISRAQILAR FAVAPERLET LFRTCAAAFP GVVEITGHGL
EILEEGRPLA RIVARSFDRY DASGKPQGAI
