ID CYSG_NEIM0 Reviewed; 480 AA. AC A9LZ77; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 25-NOV-2008, entry version 11. 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=NMCC_1074; OS Neisseria meningitidis serogroup C (strain 053442). OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; OC Neisseriaceae; Neisseria. OX NCBI_TaxID=374833; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004; RA Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., RA Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., RA Shao Z., Liang X., Xu J., Jin Q.; RT "Characterization of ST-4821 complex, a unique Neisseria meningitidis RT clone."; RL Genomics 91:78-87(2008). 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; CP000381; ABX73254.1; -; Genomic_DNA. DR RefSeq; YP_001599210.1; -. DR GeneID; 5795216; -. DR GenomeReviews; CP000381_GR; NMCC_1074. DR KEGG; nmn:NMCC_1074; -. 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; 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 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 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 1 480 Siroheme synthase. FT /FTId=PRO_0000330523. FT REGION 216 456 Uroporphyrinogen-III C-methyltransferase. SQ SEQUENCE 480 AA; 51867 MW; EAD97FA6BA13CBAF CRC64; MNYFPIFANL AGRPVLVVGG GSVAARKISL LLDAGAQVRV VANQLNAELS ALAAENKILW LAEEFRAEHI RTVFLIIAAS SDQALNRRVF QLAESCQKPV NVVDDRDYCS FIFPSIINRN PIQIAVSSSG SAPVLARLLR EKLEALLPHS LGDMAEISGR WRDAVKAKLK SVTERRRFWE KQFNGRFAAL VKNQQTAQAE QELAKQLEQN YQGGFVSLVG AGPGDAGLLT LKGLQEIQQA DVVLYDALVS DGILSLVRRD AERIFVGKRA RGDRTPQEDT NALMVRLARE GRRVVRLKGG DPFVFGRGGE ELETLARHQI PFSVVPGITA AVGATAYAGI PLTHRDYAQS AVFVTGHRKA DAPDIEWQTL ARSRQTLVIY MGALKAALIA ERLQQHGRSP DTPAAVISQG TLPAQKTATG TLANLAELAE TAPNPALIVI GEVVGLHEKL AWFGENGEGE NRVGQAYPAL GGLNAGQRAA //