ID   HEMN_RALEH              Reviewed;         494 AA.
AC   O34162; Q0K5P9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 60.
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=H16_A3615;
OS   Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
OS   (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier
OS   337)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98060717; PubMed=9396835; DOI=10.1007/s002030050540;
RA   Lieb C., Siddiqui R.A., Hippler B., Jahn D., Friedrich B.;
RT   "The Alcaligenes eutrophus hemN gene encoding the oxygen-independent
RT   coproporphyrinogen III oxidase, is required for heme biosynthesis
RT   during anaerobic growth.";
RL   Arch. Microbiol. 169:52-60(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
RA   Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E.,
RA   Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
RA   Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium
RT   Ralstonia eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
CC   -!- FUNCTION: Anaerobic transformation of coproporphyrinogen-III into
CC       protoporphyrinogen-IX.
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; U94742; AAB66374.1; -; Genomic_DNA.
DR   EMBL; AM260479; CAJ94672.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_728040.1; -.
DR   GeneID; 4247051; -.
DR   GenomeReviews; AM260479_GR; H16_A3615.
DR   KEGG; reh:H16_A3615; -.
DR   HOGENOM; O34162; -.
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    494       Oxygen-independent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_0000109937.
FT   REGION      127    128       S-adenosyl-L-methionine 2 binding (By
FT                                similarity).
FT   METAL        75     75       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        79     79       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        82     82       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   BINDING      69     69       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING      81     81       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     126    126       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   BINDING     159    159       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING     186    186       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     198    198       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     223    223       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   CONFLICT     63     65       Missing (in Ref. 1; AAB66374).
FT   CONFLICT    480    481       QP -> HA (in Ref. 1; AAB66374).
SQ   SEQUENCE   494 AA;  54499 MW;  CEDE1267B17A069F CRC64;
     MIPSAITSPA PDRRALSDFR ALAGRIDGNG PRYTSYPTAD RFHNGPDLSL YHDALAACRA
     DAPAPLSLYL HIPFCENICY YCGCNKIITR DHGRSARYVN YLGREMALVA DRLGPRRQVL
     QSHWGGGTPT FLDPGEMRRV MALLHEHFEL AAEGEHSIEI DPRRVDHARM ALLAELGFNR
     VSLGVQDFDP EVQQAIHRIQ PFEETRAVVD AARTLGFRSV SLDLIYGLPH QTAARFGRTI
     DQVLALRPDR LSVYSYAHLP HVFKPQRRID ENALPPAGEK LDILVSTIER LSAEGYVYIG
     MDHFALPDDD LAVAQREGRL QRNFQGYSTH AGYDQVGLGI SAIGAIAGRY VQNARTLDEY
     YGALDHGRLP LARGVAMSAD DHLRREIIGA LMCNGVLDIP ALEARHGIRF GTAFAPELAD
     LAALGADGLV QCAPDRITVT PLGRLLVRRV AMVFDRYLRE DAARPASTGA QAVAANDGAQ
     PVRFVPRARY SRVV
//