ID   HEMN_AQUAE              Reviewed;         456 AA.
AC   O67886;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
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=aq_2124;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07846.1; -; Genomic_DNA.
DR   PIR; B70482; B70482.
DR   RefSeq; NP_214455.1; -.
DR   GeneID; 1193875; -.
DR   GenomeReviews; AE000657_GR; aq_2124.
DR   KEGG; aae:aq_2124; -.
DR   NMPDR; fig|224324.1.peg.1470; -.
DR   HOGENOM; O67886; -.
DR   OMA; O67886; AFGMTSI.
DR   BioCyc; AAEO224324:AQ_2124-MON; -.
DR   BRENDA; 1.3.99.22; 189781.
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    456       Oxygen-independent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_0000109938.
FT   REGION      113    114       S-adenosyl-L-methionine 2 binding (By
FT                                similarity).
FT   METAL        61     61       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        65     65       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        68     68       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   BINDING      55     55       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING      67     67       S-adenosyl-L-methionine 2; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     112    112       S-adenosyl-L-methionine 1; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   BINDING     145    145       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING     172    172       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     184    184       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING     209    209       S-adenosyl-L-methionine 2 (By
FT                                similarity).
SQ   SEQUENCE   456 AA;  53785 MW;  4E494103B8EF6342 CRC64;
     MKAEFDKELI KKYDRPGPRY TSYPPATEFT EEVKEDEYVK RLIKSNERKT PLSLYFHIPF
     CEQRCLYCGC NVIISHRKGI EEPYLERVCR EMDLVSQYLD KDRKVIQLHW GGGTPNYLSP
     EQIKWFMEEI RKRFEFGDNA EISIELDPRY LTDEQIKAIK DAGFNRISLG VQDLDPKVQQ
     AVNRVQPYEL IKEKMEKLRE AGFESINLDL IYGLPYQTKE SFEKTVEKVI ELNPDRIATY
     SFAYIPQVKP HQQLLPKEAL PSAEEKLRIF EMVINKFQEA GYVYIGMDHF AKPEDELAVA
     QRKGELWRNF QGYTTKKGVE LLGFGATSIG MLYDSYFQNW KTLRDYNKTV DEGKIPVFRG
     YVLNEDDFIR REVIMDIMCN LGVEFSKIEN MFGINFREYF AKELEELKEM EEDGLIKVEE
     DRIKIMPVGR LLIRNVAMVF DAHLRRKKEL NFSRTI
//