ID   HEMN_SALTY              Reviewed;         457 AA.
AC   P0A1E1; P37129;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=STM4004;
OS   Salmonella typhimurium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   MEDLINE=94252986; PubMed=8195073;
RA   Xu K., Elliott T.;
RT   "Cloning, DNA sequence, and complementation analysis of the Salmonella
RT   typhimurium hemN gene encoding a putative oxygen-independent
RT   coproporphyrinogen III oxidase.";
RL   J. Bacteriol. 176:3196-3203(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
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.
CC   -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III
CC       oxidase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U06779; AAA19690.1; -; Genomic_DNA.
DR   EMBL; AE008887; AAL22843.1; -; Genomic_DNA.
DR   RefSeq; NP_462884.1; -.
DR   SMR; P0A1E1; 4-444.
DR   GeneID; 1255530; -.
DR   GenomeReviews; AE006468_GR; STM4004.
DR   KEGG; stm:STM4004; -.
DR   HOGENOM; P0A1E1; -.
DR   OMA; P0A1E1; HLPSRFA.
DR   BioCyc; STYP99287:STM4004-MON; -.
DR   BRENDA; 1.3.99.22; 2.
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    457       Oxygen-independent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_0000109952.
FT   REGION      113    114       S-adenosyl-L-methionine 2 binding (By
FT                                similarity).
FT   METAL        62     62       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        66     66       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   METAL        69     69       Iron-sulfur (4Fe-4S-S-AdoMet) (By
FT                                similarity).
FT   BINDING      56     56       S-adenosyl-L-methionine 1 (By
FT                                similarity).
FT   BINDING      68     68       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   457 AA;  52828 MW;  5667B4FE76204DAB CRC64;
     MSEQQIDWDL ALIQKYNYSG PRYTSYPTAL EFSEDFEDAA FLQAVARYPE RPLSLYVHIP
     FCHKLCYFCG CNKIVTRQQH KADQYLDALE QEIRHRAPLF ADRHVSQLHW GGGTPTYLNK
     AQISRLMTLL RENFHFNTDA EISIEVDPRE IELDVLDHLR AEGFNRLSMG VQDFNKEVQR
     LVNREQDEEF IFALLNHARD IGFTSTNIDL IYGLPKQTPE SFAFTLKRVT ELNPDRLSVF
     NYAHLPTLFA AQRKIKDADL PSAQQKLDIL QETIVSLTQA GYQFIGMDHF ARPDDELAVA
     QREGVLHRNF QGYTTQGDTD LLGMGVSAIS MIGDGYMQNQ KELKRYYQQV DERGNALWRG
     ITLTRDDCIR RDVIKALICN FRLDFNAVEQ QWGLHFAEYF AEDLQLLSPL AKDGLVDISE
     KGIQVTAKGR LLIRNICMCF DAYLRQKARM QQFSRVI
//