ID   HEMN_THEVL              Reviewed;         325 AA.
AC   O31067;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Oxygen-independent coproporphyrinogen-III oxidase;
DE            Short=Coproporphyrinogenase;
DE            Short=Coprogen oxidase;
DE            EC=1.3.99.22;
DE   Flags: Fragment;
GN   Name=hemN;
OS   Thermosynechococcus vulcanus (Synechococcus vulcanus).
OC   Bacteria; Cyanobacteria; Chroococcales; Thermosynechococcus.
OX   NCBI_TaxID=32053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Los D.A.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
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; AF027176; AAB84028.1; -; Genomic_DNA.
DR   BRENDA; 1.3.99.22; 276791.
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; Cytoplasm; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW   Porphyrin biosynthesis; S-adenosyl-L-methionine.
FT   CHAIN        <1    325       Oxygen-independent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_0000109953.
FT   BINDING      13     13       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING      40     40       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING      52     52       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   BINDING      77     77       S-adenosyl-L-methionine 2 (By
FT                                similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   325 AA;  36817 MW;  A4011FB51C67732B CRC64;
     AFLMTKDAEI SIEVSPRYIN GDYFLRGRKL GFNRISFGVQ DFDPQVQLAV NRVQRETMFF
     QVMEWIRAAE FESVNIDLIY GLPYQTVQSF EATIAKTLRL DPDRIAVFNF AYLPNLKPIQ
     KRIDPTTLPD SATKLTILQR VIERLTSQGY RYIGMDHFAK PTDELAIAQR SGDLKRNFQG
     YTTLPTADLI GFGLTSISML QAAYAQNQKH LATYFSDVAA GHHGPQECGF NCTVEDLLRR
     TIIMELMCQF SLDKGAIARQ FNLDFDAYFA SELAALRELA ADGLLHLGRD RLEVTPVGRL
     LIRNITAVFD AYLQQKSGRT FSKAI
//