AC   MF_01646;
DC   Protein; auto
TR   HAMAP; MF_01646; -; 1; level=0
XX
Names: Siroheme_synth
XX
ID   CYSG
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;
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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   -!- 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   -!- 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   -!- 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   -!- 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-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
CC       dehydrogenase / sirohydrochlorin ferrochelatase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the precorrin
CC       methyltransferase family.
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DR   PROSITE; PS00839; SUMT_1; 1; trigger=no
DR   PROSITE; PS00840; SUMT_2; 1; trigger=no
DR   Pfam; PF00590; TP_methylase; 1; trigger=no
DR   NCBIfam; TIGR01469; CobA_cysG_Cterm; 1; trigger=no
DR   NCBIfam; TIGR01470; CysG_Nterm; 1; trigger=no
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KW   Cobalamin biosynthesis
KW   Lyase
KW   Methyltransferase
KW   Multifunctional enzyme
KW   NAD
KW   Oxidoreductase
case <FT:13>
KW   Phosphoprotein
end case
KW   Porphyrin biosynthesis
KW   S-adenosyl-L-methionine
KW   Transferase
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GO   GO:0004325; F:ferrochelatase activity
GO   GO:0004851; F:uroporphyrin-III C-methyltransferase activity
GO   GO:0043115; F:precorrin-2 dehydrogenase activity
GO   GO:0006779; P:porphyrin-containing compound biosynthetic process
GO   GO:0009236; P:cobalamin biosynthetic process
GO   GO:0019354; P:siroheme biosynthetic process
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FT   From: CYSG_SALTY (P25924)
FT   BINDING         22..23
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   BINDING         43..44
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   REGION          Nter..204
FT                   /note="Precorrin-2 dehydrogenase / sirohydrochlorin
FT                   ferrochelatase"
FT   REGION          216..Cter
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT   BINDING         301..303
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: G-G-D
FT   BINDING         331..332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: [TS]-A
FT   ACT_SITE        248
FT                   /note="Proton acceptor"
FT   Condition: D
FT   ACT_SITE        270
FT                   /note="Proton donor"
FT   Condition: K
FT   BINDING         225
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: P
FT   BINDING         306
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: [IVL]
FT   BINDING         382
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: M
FT   BINDING         411
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT   Condition: [GA]
FT   MOD_RES         128
FT                   /note="Phosphoserine"
FT   Condition: S
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Size: 457-549;
Related: None;
Template: P0AEA8; P25924;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: in AERHH, AERS4, CROS8, PECAS, HALHL, KLEP7, SERP5, YERE8, YERP3,
 YERPN, YERPP, YERPS
Plasmid: None
Comments: None
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# Revision 1.22 2023/06/01
//