CYSG_PSEFS
ID CYSG_PSEFS Reviewed; 464 AA.
AC C3JY53;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Siroheme synthase {ECO:0000255|HAMAP-Rule:MF_01646};
DE Includes:
DE RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01646};
DE Short=Urogen III methylase {ECO:0000255|HAMAP-Rule:MF_01646};
DE EC=2.1.1.107 {ECO:0000255|HAMAP-Rule:MF_01646};
DE AltName: Full=SUMT {ECO:0000255|HAMAP-Rule:MF_01646};
DE AltName: Full=Uroporphyrinogen III methylase {ECO:0000255|HAMAP-Rule:MF_01646};
DE Short=UROM {ECO:0000255|HAMAP-Rule:MF_01646};
DE Includes:
DE RecName: Full=Precorrin-2 dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01646};
DE EC=1.3.1.76 {ECO:0000255|HAMAP-Rule:MF_01646};
DE Includes:
DE RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000255|HAMAP-Rule:MF_01646};
DE EC=4.99.1.4 {ECO:0000255|HAMAP-Rule:MF_01646};
GN Name=cysG {ECO:0000255|HAMAP-Rule:MF_01646}; OrderedLocusNames=PFLU_3796;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent
CC methylations of uroporphyrinogen III at position C-2 and C-7 to form
CC precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring
CC dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it
CC catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) +
CC precorrin-2 + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32459,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57308, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58827, ChEBI:CHEBI:59789; EC=2.1.1.107;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin;
CC Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01646};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01646};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC precorrin-2 from uroporphyrinogen III: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01646}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01646}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC dehydrogenase / sirohydrochlorin ferrochelatase family.
CC {ECO:0000255|HAMAP-Rule:MF_01646}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the precorrin
CC methyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01646}.
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DR EMBL; AM181176; CAY50097.1; -; Genomic_DNA.
DR RefSeq; WP_012724932.1; NC_012660.1.
DR AlphaFoldDB; C3JY53; -.
DR SMR; C3JY53; -.
DR STRING; 216595.PFLU_3796; -.
DR PRIDE; C3JY53; -.
DR EnsemblBacteria; CAY50097; CAY50097; PFLU_3796.
DR KEGG; pfs:PFLU_3796; -.
DR eggNOG; COG0007; Bacteria.
DR eggNOG; COG1648; Bacteria.
DR HOGENOM; CLU_011276_2_2_6; -.
DR OMA; KMTVVVY; -.
DR OrthoDB; 1185397at2; -.
DR UniPathway; UPA00148; UER00211.
DR UniPathway; UPA00148; UER00222.
DR UniPathway; UPA00262; UER00211.
DR UniPathway; UPA00262; UER00222.
DR UniPathway; UPA00262; UER00376.
DR Proteomes; UP000002332; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd11642; SUMT; 1.
DR Gene3D; 1.10.8.210; -; 1.
DR Gene3D; 3.30.950.10; -; 1.
DR Gene3D; 3.40.1010.10; -; 1.
DR HAMAP; MF_01646; Siroheme_synth; 1.
DR InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR006366; CobA/CysG_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR InterPro; IPR012409; Sirohaem_synth.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR Pfam; PF10414; CysG_dimeriser; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036426; Sirohaem_synth; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
DR TIGRFAMs; TIGR01470; cysG_Nterm; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Lyase; Methyltransferase; Multifunctional enzyme;
KW NAD; Oxidoreductase; Phosphoprotein; Porphyrin biosynthesis;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..464
FT /note="Siroheme synthase"
FT /id="PRO_1000215847"
FT REGION 1..203
FT /note="Precorrin-2 dehydrogenase /sirohydrochlorin
FT ferrochelatase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT REGION 216..464
FT /note="Uroporphyrinogen-III C-methyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT ACT_SITE 270
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 22..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 43..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 225
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 301..303
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 306
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 331..332
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 383
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT BINDING 412
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01646"
SQ SEQUENCE 464 AA; 50290 MW; D046EA912A23E815 CRC64;
MEFLPLFHNL RGSRVLVVGG GEIALRKSRL LADAGAVLRV VAPQIEDQLR ELVQGSGGEL
MLRGYQEADL DGCTLIIAAT DDEPLNAQVS SDAKRRCVPV NVVDAPALCS VIFPAIVDRS
PLVIAVSSGG DAPVLARLIR AKLETWIPST YGQLAGLAAR FRAQVKGLYP DVQQRRAFWE
EVFQGPIADR QLAGQGDEAE RLLIEKVNGA PPYAPGEVYL VGAGPGDPDL LTFRALRLMQ
QADVVLYDRL VAPAILELCR RDAERIYVGK RRADHAVPQD QINQQLVDLA KQGKRVLRLK
GGDPFIFGRG GEEIEELAAH GIPFQVVPGI TAASGCAAYA GIPLTHRDYA QSVRFITGHL
KNGTSDLPWQ DLVGPSQTLV FYMGLIGLPI ICEQLIKHGR AADTPAALIQ QGTTSNQRVF
TGTLADLPRM VAEHEVHAPT LVIVGEVVVL REKLKWFEGA QSQV
