ID   CYSG_PSEU5              Reviewed;         465 AA.
AC   A4VLU6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   16-JUN-2009, entry version 20.
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=PST_2288;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W.,
RA   Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D.,
RA   Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Complete genome sequence of the metabolically versatile and root-
RT   associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional enzyme that catalyzes 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 consists 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.
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DR   EMBL; CP000304; ABP79947.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001172789.1; -.
DR   GeneID; 5098368; -.
DR   GenomeReviews; CP000304_GR; PST_2288.
DR   KEGG; psa:PST_2288; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR   InterPro; IPR006367; Sirohaem_synthase_N.
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; PF10414; CysG_dimeriser; 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; FALSE_NEG.
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    465       Siroheme synthase.
FT                                /FTId=PRO_0000330542.
FT   REGION      218    460       Uroporphyrinogen-III C-methyltransferase.
SQ   SEQUENCE   465 AA;  49692 MW;  55ED316A54895278 CRC64;
     MEYLPLFHNL KGRTVLIVGG GEIALRKARL LSEAGARLRV VAPSIEAQLV ELVQAGAGEC
     LDRGYARQDL QGCVLAIAAT DDEPLNATVS QHANALGVPV NVVDSPQLCS VIFPAIVDRS
     PLVVAVSSGG DAPVLARLIR ARIETWIPAA YGQLAGLAKQ FRAQVKARFA NVQQRRVFWE
     EVFQGPIAEQ ALAGRTAEAE RLLAEKLAGV APKALGEVYL VGAGPGDPDL LTFRALRLMQ
     QADVVLYDRL VAPAIIDLCR RDADRIYVGK QRADHAVPQE QINQQLVTLA KQGKRVLRLK
     GGDPFIFGRG GEEIEELAAH GVPFQVVPGI TAASGCAAYA GIPLTHRDHA QSVRFVTGHL
     KDGSCDLPWS ELAAPAQTLV FYMGLVGLPV ICQQLIAHGR SAETPAALVQ QGTTSNQRVF
     TATLGTLAGR IAQEDVQAPT LLIVGEVVQL REKLAWFEGA QAAGR
//