ID   CYSG_PHOLL              Reviewed;         470 AA.
AC   Q7N8L2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   04-NOV-2008, entry version 33.
DE   RecName: Full=Siroheme synthase;
DE   Includes:
DE     RecName: Full=Uroporphyrinogen-III C-methyltransferase;
DE              Short=Urogen III methylase;
DE              EC=2.1.1.107;
DE     AltName: Full=SUMT;
DE     AltName: Full=Uroporphyrinogen III methylase;
DE              Short=UROM;
DE   Includes:
DE     RecName: Full=Precorrin-2 dehydrogenase;
DE              EC=1.3.1.76;
DE   Includes:
DE     RecName: Full=Sirohydrochlorin ferrochelatase;
DE              EC=4.99.1.4;
GN   Name=cysG; OrderedLocusNames=plu0708;
OS   Photorhabdus luminescens subsp. laumondii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=141679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TT01;
RX   MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S.,
RA   Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V.,
RA   Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: Multifunctional enzyme that catalyze the SAM-dependent
CC       methylation of uroporphyrinogen III at position C-2 and C-7 to
CC       form precorrin-2 and then position C-12 or C-18 to form
CC       trimethylpyrrocorphin 2. It also catalyzes the conversion of
CC       precorrin-2 into siroheme. This reaction consist of the NAD-
CC       dependent oxidation of precorrin-2 into sirohydrochlorin and its
CC       subsequent ferrochelation into siroheme (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uroporphyrinogen III
CC       = S-adenosyl-L-homocysteine + precorrin-1.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S-
CC       adenosyl-L-homocysteine + precorrin-2.
CC   -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin +
CC       NADH.
CC   -!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       precorrin-2 from uroporphyrinogen III: step 1/1.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       sirohydrochlorin from precorrin-2: step 1/1.
CC   -!- PATHWAY: Porphyrin metabolism; siroheme biosynthesis; precorrin-2
CC       from uroporphyrinogen III: step 1/1.
CC   -!- PATHWAY: Porphyrin metabolism; siroheme biosynthesis; siroheme
CC       from sirohydrochlorin: step 1/1.
CC   -!- PATHWAY: Porphyrin metabolism; siroheme biosynthesis;
CC       sirohydrochlorin from precorrin-2: step 1/1.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase 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; BX571861; CAE13003.1; -; Genomic_DNA.
DR   RefSeq; NP_928053.1; -.
DR   HSSP; P25924; 1PJT.
DR   GeneID; 2800671; -.
DR   GenomeReviews; BX470251_GR; plu0708.
DR   KEGG; plu:plu0708; -.
DR   NMPDR; fig|243265.1.peg.677; -.
DR   PhotoList; plu0708; -.
DR   HOGENOM; Q7N8L2; -.
DR   BioCyc; PLUM243265:PLU0708-MON; -.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:HAMAP.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:EC.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:HAMAP.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01646; -; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA_cysG_C.
DR   InterPro; IPR006367; CysG_synth_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   Gene3D; G3DSA:3.40.1010.10; 4pyrrole_Mease_sub1; 1.
DR   Gene3D; G3DSA:3.30.950.10; 4pyrrole_Mease_sub2; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
DR   TIGRFAMs; TIGR01470; cysG_Nterm; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Cobalamin biosynthesis; Complete proteome; Lyase; Methyltransferase;
KW   Multifunctional enzyme; NAD; Oxidoreductase; Porphyrin biosynthesis;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    470       Siroheme synthase.
FT                                /FTId=PRO_0000330530.
FT   REGION      216    456       Uroporphyrinogen-III C-methyltransferase.
SQ   SEQUENCE   470 AA;  51343 MW;  343EAAB8BF73706F CRC64;
     MDYLPIFVEL KGRLVLLVGG GEVAARKATL LLRAGALLQV VAPELCSELQ QRYQAGELEW
     YQGEFQPEYL DGIFLVIAAT DDRILNHQVF SEADKRSILV NVVDDQVHCS FIFPSIIDRS
     PVLVAISSAG KAPVLARLIR EKLEALLPSS LGTMAKIAGK WRERVKQRLT SMRQRRSFWE
     QAFNGRFAML VANGQIQQAE KQLEQQLEQS DLQGELALVG AGPGDPGLLT LKGLQVIQQA
     DVVLYDHLVS SDVLDLIRRD ADKICVGKRA GNHSVSQEET NRLIVKFARQ GKKVVRLKGG
     DPFIFGRGGE ELQVAASAGI PFQVVPGITA AIGATAYAGI PLTHREHSQS ITFITGHCRE
     KGNELDWPAL ARGHQTLVIY MGTVKAALIS HQLILHGRAE DTPVAVIGCG TRLEQQVLTG
     TLLELEQLAQ QAPSPALLVV GEVAQLHHQI AWFGQQSIAK ISRPAVVDFA
//