ID   HEMN_BRAJA              Reviewed;         450 AA.
AC   O31381;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   28-FEB-2003, sequence version 2.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Oxygen-independent coproporphyrinogen-III oxidase;
DE            Short=Coproporphyrinogenase;
DE            Short=Coprogen oxidase;
DE            EC=1.3.99.22;
GN   Name=hemN; OrderedLocusNames=bll7086;
OS   Bradyrhizobium japonicum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=USDA 110;
RX   MEDLINE=21101813; PubMed=11157943;
RX   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
RT   during anaerobic growth and in symbiosis.";
RL   J. Bacteriol. 183:1300-1311(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USDA 110;
RX   MEDLINE=22484998; PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- FUNCTION: Anaerobic transformation of coproporphyrinogen-III into
CC       protoporphyrinogen-IX (By similarity).
CC   -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + 2 S-adenosyl-L-
CC       methionine = protoporphyrinogen-IX + 2 CO(2) + 2 L-methionine + 2
CC       5'-deoxyadenosine.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is coordinated with
CC       3 cysteines and an exchangeable S-adenosyl-L-methionine (By
CC       similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route):
CC       step 1/1.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III
CC       oxidase family.
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DR   EMBL; AJ002517; CAA05507.1; -; Genomic_DNA.
DR   EMBL; BA000040; BAC52351.1; -; Genomic_DNA.
DR   RefSeq; NP_773726.1; -.
DR   GeneID; 1047805; -.
DR   GenomeReviews; BA000040_GR; bll7086.
DR   KEGG; bja:bll7086; -.
DR   HOGENOM; O31381; -.
DR   OMA; O31381; HVPFCRE.
DR   BioCyc; BJAP224911:BLL7086-MON; -.
DR   BRENDA; 1.3.99.22; 280.
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:EC.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR004558; HemN.
DR   InterPro; IPR010723; HemN_C.
DR   InterPro; IPR007197; Radical_SAM.
DR   Pfam; PF06969; HemN_C; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR00538; hemN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Porphyrin biosynthesis;
KW   S-adenosyl-L-methionine.
FT   CHAIN         1    450       Oxygen-independent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_0000109940.
FT   REGION      109    110       S-adenosyl-L-methionine 2 binding (By
FT                                similarity).
FT   METAL        57     57       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        61     61       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        64     64       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   BINDING      51     51       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING      63     63       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     108    108       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   BINDING     141    141       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING     168    168       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     180    180       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     205    205       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   CONFLICT    307    307       Q -> H (in Ref. 1; CAA05507).
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
//