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Database: UniProt
Entry: C7R1A7_JONDD
LinkDB: C7R1A7_JONDD
Original site: C7R1A7_JONDD 
ID   C7R1A7_JONDD            Unreviewed;       447 AA.
AC   C7R1A7;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=Uroporphyrin-III C-methyltransferase {ECO:0000313|EMBL:ACV08322.1};
GN   OrderedLocusNames=Jden_0658 {ECO:0000313|EMBL:ACV08322.1};
OS   Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP
OS   55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria
OS   denitrificans).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC   Jonesia.
OX   NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV08322.1, ECO:0000313|Proteomes:UP000000628};
RN   [1] {ECO:0000313|EMBL:ACV08322.1, ECO:0000313|Proteomes:UP000000628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 /
RC   NBRC 15587 / NCTC 10816 / Prevot 55134
RC   {ECO:0000313|Proteomes:UP000000628};
RX   PubMed=21304666; DOI=10.4056/sigs.41646;
RA   Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T.,
RA   Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A.,
RA   Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Han C.;
RT   "Complete genome sequence of Jonesia denitrificans type strain (Prevot
RT   55134).";
RL   Stand. Genomic Sci. 1:262-269(2009).
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; CP001706; ACV08322.1; -; Genomic_DNA.
DR   RefSeq; WP_015770950.1; NC_013174.1.
DR   AlphaFoldDB; C7R1A7; -.
DR   STRING; 471856.Jden_0658; -.
DR   KEGG; jde:Jden_0658; -.
DR   eggNOG; COG0007; Bacteria.
DR   eggNOG; COG1648; Bacteria.
DR   HOGENOM; CLU_011276_2_1_11; -.
DR   UniPathway; UPA00262; UER00222.
DR   Proteomes; UP000000628; Chromosome.
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:ACV08322.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000000628};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACV08322.1}.
FT   DOMAIN          190..393
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   REGION          426..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
FT   ACT_SITE        242
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036426-1"
SQ   SEQUENCE   447 AA;  46977 MW;  AFE7794F59B7C137 CRC64;
     MSDVLPLGVR LTGRPVLVVG GGAVAARRAR MLHRSGARVT VISPQLCPDM EELIATSQYA
     ADQAHGYRVV VHHRTYRDGD VHGMWLVATA TSHREVDDAV AQAAEDNRVF CLKGGDPHSA
     TAWAPALTTH GDSTIAVLSQ GHSPNPRRSI RLRDKIAAFL TTHPEEPRLA RGRIGTPQQQ
     PTHTPPVGHV TLVGGGPGAL GLLTIAGKQA IEHADVLVMD RLAPQEARRY APAHAEIIDV
     GKTGGRHPVS QAEIHDILID RATAGLHVVR LKGGDPYVFG RGGEEYEACT RHNIPVTVLP
     GVTSAVSVPA AAGIPVTHRG VSRGFTVLTG HCDLDKAPLA QDHTVVLLMG VSRLEELTAQ
     LIAQGNSANT PCAIIEDGYG PRQRTTTGTL ASIAQTARQV GVQSPAITVV GDVAAFAHSP
     FSAALPGSIG QQSPARHEGH AQAGLTQ
//
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