ID A0A1I6Y8I0_9MICC Unreviewed; 423 AA.
AC A0A1I6Y8I0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000313|EMBL:SFT46772.1};
GN ORFNames=SAMN04487915_101493 {ECO:0000313|EMBL:SFT46772.1};
OS Arthrobacter sp. ov118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1761747 {ECO:0000313|EMBL:SFT46772.1, ECO:0000313|Proteomes:UP000199457};
RN [1] {ECO:0000313|EMBL:SFT46772.1, ECO:0000313|Proteomes:UP000199457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV118 {ECO:0000313|EMBL:SFT46772.1,
RC ECO:0000313|Proteomes:UP000199457};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; 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; FPAY01000001; SFT46772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6Y8I0; -.
DR STRING; 1761747.SAMN04487915_101493; -.
DR OrthoDB; 9815856at2; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000199457; 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; IPR006367; Sirohaem_synthase_N.
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; PF13241; NAD_binding_7; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036426; Sirohaem_synth; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 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 ECO:0000313|EMBL:SFT46772.1};
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 S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFT46772.1}.
FT DOMAIN 166..369
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 401..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ SEQUENCE 423 AA; 43645 MW; D677E3B6D49088DF CRC64;
MAIQDIYPTA LRLLGRPVLV VGGGPVAARR AKGLLDAGAR VTVVAPDASP AMAELAGAGL
LSWEPRRYGP SDVDGVWFVQ TATGDPAVDA RVSADAEAQR IWCVNASDHE ASAAWTPAVA
VVDDVKIAVN AGGDPRRAMA LRDAVATALD AGDLPLRRRR ASTGSVALVG GGPGDTGLIT
VRGRRLLGQA DVVVADRLGP RELLGELAPD VRVVEVGKTP GHHPVPQAEI NRILVDEARQ
GHRVVRLKGG DPYVLGRGGE EAEFCRHNGV DVEVVPGVTS ATSVPAAAGI PVTHRGLAKG
FSVVTGHEEL SEVPARADHT VILLMGVGQL RDSAASLAQA GLPAGTPVGI VENGYLPDQR
VTIGTLGTIA DQAEAVGVAN PAVIVIGDVV RVSPFAPSHF KTADYSTTAP NKPRTAKTRV
LTP
//
