ID   CYSG_PSE14              Reviewed;         464 AA.
AC   Q48H75;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=PSPPH_3088;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ35170.1; -; Genomic_DNA.
DR   RefSeq; YP_275258.1; -.
DR   GeneID; 3557746; -.
DR   GenomeReviews; CP000058_GR; PSPPH_3088.
DR   KEGG; psp:PSPPH_3088; -.
DR   NMPDR; fig|264730.3.peg.3461; -.
DR   HOGENOM; Q48H75; -.
DR   OMA; Q48H75; TTVVYMP.
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    464       Siroheme synthase.
FT                                /FTId=PRO_0000330543.
FT   REGION      218    460       Uroporphyrinogen-III C-methyltransferase.
SQ   SEQUENCE   464 AA;  50022 MW;  40D2232C497E6EDA CRC64;
     MEFLPLFHNL RGSRVLVVGG GEIALRKSRL IADAGAVLRV VAPEIEAQLS ELVVQSGGEM
     ILRGYSESDL DGCVLIIAAT DDEPLNAQVS HDARLRCVPV NVVDAPALCT VIFPAIVDRS
     PLVIAVSSGG DAPVLARLIR AKLETWIPST YGQLAGLAAR FRNQVKGLFP NVQQRRAFWE
     DVFQGAIADR QLAGQGAEAE RLLIAKIAGE PPPETGEVYL VGAGPGDPDL LTFRALRLMQ
     QADVVLYDRL VAPTILDLCR RDAERVYVGK RRAEHAVPQE QINQQLVALA KQGKRVVRLK
     GGDPFIFGRG GEEIEELAVH GIPFQVVPGI TAASGCAAYA GIPLTHRDHA QSVRFITGHL
     KDGTTDLPWS DLVAPAQTLV FYMGLIGLPV ICEELIRHGR SADTPAALVQ QGTTVNQRVF
     TGTLANLPQL VAEHEVHAPT LVIIGEVVKL REKLAWFEGA QATV
//