ID   CYSG_PSYA2              Reviewed;         549 AA.
AC   Q4FSU1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   16-JUN-2009, entry version 28.
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=Psyc_1065;
OS   Psychrobacter arcticus (strain DSM 17307 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   NASA Astrobiology Institute;
RA   Ayala-del-Rio H.L., Chain P., Ponder M.A., Di Bartolo G., Ivanova N.,
RA   Bergholz P.W., Hauser L., Land M., Bakermans C., Rodrigues D.,
RA   Klappenbach J.A., Zarka D., Larimer F., Richardson P., Thomashow M.F.,
RA   Tiedje J.M.;
RT   "Complete sequence of Psychrobacter arcticum 273-4.";
RL   Submitted (JUL-2005) 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.
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; CP000082; AAZ18917.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_264351.1; -.
DR   GeneID; 3514951; -.
DR   GenomeReviews; CP000082_GR; Psyc_1065.
DR   KEGG; par:Psyc_1065; -.
DR   NMPDR; fig|259536.4.peg.646; -.
DR   HOGENOM; Q4FSU1; -.
DR   OMA; Q4FSU1; DKLVPQQ.
DR   BioCyc; PARC259536:PSYC_1065-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; 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    549       Siroheme synthase.
FT                                /FTId=PRO_0000330546.
FT   REGION      249    491       Uroporphyrinogen-III C-methyltransferase.
SQ   SEQUENCE   549 AA;  59727 MW;  019AACCDA20937C4 CRC64;
     MNTFPLFFKL EDRKVLIVGG GDVALRKADL LSRAGACITV LAPSINHEIQ ALLSSSKHEL
     IYEHYNKTYM TNSRVIIAAT DDERLNHQIH ADATALNIPV NVVDTPHLCD FIFPAIVDRN
     PIVIGISSNG KAPVLARLLR ARLETLIPQG YGKLAKLAGE FRGDVKAKIP TLTGRRQFWE
     RAFEGKVSQL MFAGNENEAL AQLQADLDNT AASITAKDAT DDNGLSTAST SAPAIANEFT
     AARNTMGEVY IVGAGPGDPE LLTFKALRLM QQADIVYYDA LVSPQVLDLC RRDADKVFVG
     KKRRNHAVAQ LGINELLVNS AKEGRRVVRL KGGDPFIFGR GGEEIESLRA HNIPYQVVPG
     ITAANAAASY AGIPLTHRDH SQSVRFVTGF LKAGAPNNNF KNFLDTDETV VFYMGLHSLP
     RLTEGLIDAG RSAETPIAIV SNASMPNQQV LTGTLASIVE LQEKNQLPTP ALLIMGDVVS
     LHHDLAWYNL HNQQHNQNTS ETDNNWLRGG TATTPKSNAQ FNAHQQAHAL SMITNLATED
     GDLEQLIIG
//