HEMN_BRADU
ID HEMN_BRADU Reviewed; 450 AA.
AC O31381;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=bll7086;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=11157943; DOI=10.1128/jb.183.4.1300-1311.2001;
RA Fischer H.-M., Velasco L., Delgado M.J., Bedmar E.J., Schaeren S.,
RA Zingg D., Goettfert M., Hennecke H.;
RT "One of two hemN genes in Bradyrhizobium japonicum is functional during
RT anaerobic growth and in symbiosis.";
RL J. Bacteriol. 183:1300-1311(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
CC -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the anaerobic
CC oxidative decarboxylation of propionate groups of rings A and B of
CC coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen
CC 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; AJ002517; CAA05507.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC52351.1; -; Genomic_DNA.
DR RefSeq; NP_773726.1; NC_004463.1.
DR RefSeq; WP_011089823.1; NZ_CP011360.1.
DR AlphaFoldDB; O31381; -.
DR SMR; O31381; -.
DR STRING; 224911.27355368; -.
DR EnsemblBacteria; BAC52351; BAC52351; BAC52351.
DR GeneID; 64026845; -.
DR KEGG; bja:bll7086; -.
DR PATRIC; fig|224911.44.peg.7144; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_3_0_5; -.
DR InParanoid; O31381; -.
DR OMA; VPFCRSM; -.
DR PhylomeDB; O31381; -.
DR UniPathway; UPA00251; UER00323.
DR Proteomes; UP000002526; Chromosome.
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; 3.80.30.20; -; 1.
DR InterPro; IPR004558; Coprogen_oxidase_HemN.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
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; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..450
FT /note="Oxygen-independent coproporphyrinogen III oxidase"
FT /id="PRO_0000109940"
FT DOMAIN 42..276
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 57
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 61
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 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
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 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 109..110
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 180
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 205
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 239
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT CONFLICT 307
FT /note="Q -> H (in Ref. 1; CAA05507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 49327 MW; EEAC485931754EE9 CRC64;
MRADLAVSYG EERLPRYTSY PTAPHFSPVI DAGTYARWLS ELPAGASASL YLHVPFCREM
CWYCGCHTQI VRRDDLIAAY QRTLRSEIAL VAETIGRRIK VEHIHFGGGT PTIMAPEAFA
ELMAAMRQAF FVLPSAEIAV EIDPRTLTAD MVEAMRLSGV NRASLGVQSF DPIVQRAINR
IQSFEQTAAV VDMLRHAGIA GINFDLIYGL PHQTVASCLD TVRRSLLLAP DRFSVFGYAH
VPDFKKHQRM INQGALPDGP ARHDQACAIA NALKEAGYVQ IGLDHFARPD DSMAVAFEER
TLRRNFQGYT TDQGEVLLGF GASAIGHLPQ GYVQNEVQIG AYAQSIGASR LATAKGYGLT
DDDRLRADII ERIMCEFSAD LGDICARHGA EPEAMLKSAS RLKPLISDGV VRLDGDRLAV
ANDSRFLVRS VAAAFDAHLD PGKQLHSRAV
