ID A0A2R8AA27_9RHOB Unreviewed; 464 AA.
AC A0A2R8AA27;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Siroheme synthase {ECO:0000313|EMBL:SPF29059.1};
GN Name=cysG_1 {ECO:0000313|EMBL:SPF29059.1};
GN ORFNames=POI8812_01364 {ECO:0000313|EMBL:SPF29059.1};
OS Pontivivens insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pontivivens.
OX NCBI_TaxID=1639689 {ECO:0000313|EMBL:SPF29059.1, ECO:0000313|Proteomes:UP000244932};
RN [1] {ECO:0000313|EMBL:SPF29059.1, ECO:0000313|Proteomes:UP000244932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CeCT 8812 {ECO:0000313|EMBL:SPF29059.1,
RC ECO:0000313|Proteomes:UP000244932};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001156};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000256|ARBA:ARBA00025705}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005010}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879}.
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DR EMBL; OMKW01000002; SPF29059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AA27; -.
DR OrthoDB; 9815856at2; -.
DR UniPathway; UPA00262; UER00211.
DR Proteomes; UP000244932; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:InterPro.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11642; SUMT; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR012409; Sirohaem_synth.
DR InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR NCBIfam; TIGR01470; cysG_Nterm; 1.
DR PANTHER; PTHR45790:SF3; S-ADENOSYL-L-METHIONINE-DEPENDENT UROPORPHYRINOGEN III METHYLTRANSFERASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR Pfam; PF10414; CysG_dimeriser; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036426; Sirohaem_synth; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00839; SUMT_1; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000244932};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 150..202
FT /note="Sirohaem synthase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF10414"
FT DOMAIN 218..427
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT ACT_SITE 248
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT ACT_SITE 270
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ SEQUENCE 464 AA; 49834 MW; 2627A3BCBEAF5C54 CRC64;
MRHFPIFVNL AGRRVVVSGA GECALAKLRL ILKTEANIAV YGAEPHEKLR ELARDGKITL
VERPIEEGDA ICAALLYGAN EDALEDARAA AIGRRAGAMT NIVDNLADSQ FITPAIVDRD
PVTIAIGTEG AAPVLARDIK RRVEEMLPTS LGALARIGQA FRPVADILPM GRIRRAFWSK
FYFERGPRAL AEGEDVARES LDTLLNETLS AEVEAGHVAL IGAGPGDPEL LTLKARRLLH
EADVVITDRL VGAGVLELAR REAEIIEVGK IGFGPSWKQD DINALIVEKA AEGQKVARLK
GGDVAIFARL DEEIEVLEQA GISWEIVPGI TTASAAAASL GQSLTKRGRN KSFRMVTGHD
VDGFAEQDWR DLAKPGATAA IYMGKKASTF LRGRLMMHGA LDNTPVTAIE NVSRADQRIL
PTTLIDLPDM LEREDVTGPV ILMLGLAPRA AVAALPELQA AEAL
//
