HEMF_CERS4
ID HEMF_CERS4 Reviewed; 452 AA.
AC P33770; Q3J141;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Coproporphyrinogen III oxidase, anaerobic 1;
DE Short=Coprogen oxidase;
DE Short=Coproporphyrinogenase;
DE EC=1.3.98.3 {ECO:0000250|UniProtKB:P32131};
GN Name=hemN; OrderedLocusNames=RHOS4_19250; ORFNames=RSP_0317;
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].
RX PubMed=1333567; DOI=10.1111/j.1365-2958.1992.tb01772.x;
RA Coomber S.A., Jones R.M., Jordan P.M., Hunter C.N.;
RT "A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter
RT sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence
RT analysis of the gene.";
RL Mol. Microbiol. 6:3159-3169(1992).
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: Anaerobic transformation of coproporphyrinogen III into
CC protoporphyrinogen IX. Dedicated to bacteriochlorophyll biosynthesis.
CC {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.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB24393.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S50573; AAB24393.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP000143; ABA79493.1; -; Genomic_DNA.
DR PIR; S28440; S28440.
DR RefSeq; WP_011338144.1; NZ_CP030271.1.
DR RefSeq; YP_353394.1; NC_007493.2.
DR AlphaFoldDB; P33770; -.
DR SMR; P33770; -.
DR STRING; 272943.RSP_0317; -.
DR PRIDE; P33770; -.
DR EnsemblBacteria; ABA79493; ABA79493; RSP_0317.
DR KEGG; rsp:RSP_0317; -.
DR PATRIC; fig|272943.9.peg.2264; -.
DR eggNOG; COG0635; Bacteria.
DR OMA; CERLCWF; -.
DR PhylomeDB; P33770; -.
DR BioCyc; MetaCyc:MON-19721; -.
DR UniPathway; UPA00251; UER00323.
DR Proteomes; UP000002703; Chromosome 1.
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:0030494; P:bacteriochlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
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..452
FT /note="Coproporphyrinogen III oxidase, anaerobic 1"
FT /id="PRO_0000109948"
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"
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"
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"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 112..113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT CONFLICT 195..197
FT /note="ETL -> QSV (in Ref. 1; AAB24393)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="D -> E (in Ref. 1; AAB24393)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..409
FT /note="PRIAEAAEKF -> LAHRRSGREV (in Ref. 1; AAB24393)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50054 MW; 36E1430A36C0D6C9 CRC64;
MTNIALLQSL GLFDARVPRY TSYPAAPVFS GAVGADFQAQ AIEALDPAVP ISVYVHVPFC
ERLCWFCACR TQGTQTLAPV EAYVGTLLQE LELVKQHLPA GVKAGRLHWG GGTPTILSPE
LIHKLAQAIK AVIPFAEDYE FSVEIDPMMV DEPKIRALSE EGMNRASIGI QDFTDIVQNA
IGREQPFENT KACVETLRRY GVHSLNTDLV YGLPHQNRES LAATIDKVLS LRPDRVAIFG
YAHVPWMAKR QKLIDETVLP PDIERHELAN LAARLFTEGG FERIGIDHFA LPDDSMAVAA
RSRKLRRNFQ GYTDDTCPTL LGIGASSISK FEQGYLQNTA ATAAYIKSIE EGRLPGYRGH
RMTEEDYLHG RAIEMIMCDF FLDLPALRAR FGEPAETMVP RIAEAAEKFT PFVTVDADGS
MSIAKEGRAL ARMIARLFDA YETPEARYSQ AS
