ID   CYSG_ECO57              Reviewed;         457 AA.
AC   P0AEA9; P11098; P76685;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 35.
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=Z4729, ECs4219;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG58476.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37642.1; -; Genomic_DNA.
DR   PIR; C91156; C91156.
DR   PIR; H86001; H86001.
DR   RefSeq; NP_289916.1; -.
DR   RefSeq; NP_312246.1; -.
DR   HSSP; O87696; 1CBF.
DR   SMR; P0AEA9; 1-457.
DR   GeneID; 915926; -.
DR   GeneID; 961541; -.
DR   GenomeReviews; AE005174_GR; Z4729.
DR   GenomeReviews; BA000007_GR; ECs4219.
DR   KEGG; ece:Z4729; -.
DR   KEGG; ecs:ECs4219; -.
DR   HOGENOM; P0AEA9; -.
DR   OMA; P0AEA9; MCRRDAE.
DR   BioCyc; ECOL83334:ECS4219-MON; -.
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; 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    457       Siroheme synthase.
FT                                /FTId=PRO_0000150379.
FT   REGION      218    457       Uroporphyrinogen-III C-methyltransferase.
SQ   SEQUENCE   457 AA;  49951 MW;  DDDE0DC90C5CF2F4 CRC64;
     MDHLPIFCQL RDRDCLIVGG GDVAERKARL LLDAGARLTV NALAFIPQFT AWADAGMLTL
     VEGPFDESLL DTCWLAIAAT DDDALNQRVS EAAEARRIFC NVVDAPKAAS FIMPSIIDRS
     PLMVAVSSGG TSPVLARLLR EKLESLLPLH LGQVAKYAGQ LRGRVKQQFA TMGERRRFWE
     KLFVNDRLAQ SLANNDQKAI TETTEQLINE PLDHRGEVVL VGAGPGDAGL LTLKGLQQIQ
     QADVVVYDRL VSDDIMNLVR RDADRVFVGK RAGYHCVPQE EINQILLREA QKGKRVVRLK
     GGDPFIFGRG GEELETLCNA GIPFSVVPGI TAASGCSAYS GIPLTHRDYA QSVRLITGHL
     KTGGELDWEN LAAEKQTLVF YMGLNQAATI QQKLIEHGMP GEMPVAIVEN GTAVTQRVID
     GTLTQLGELA QQMNSPSLII IGRVVGLRDK LNWFSNH
//