ID   NIRE_PARDP              Reviewed;         287 AA.
AC   Q51701; A1B4Y1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 114.
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;
GN   Name=nirE; OrderedLocusNames=Pden_2488;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7747927; DOI=10.1007/bf00871635;
RA   de Boer A.P.N., Reijnders W.N.M., Kuenen J.G., Stouthamer A.H.,
RA   van Spanning R.J.M.;
RT   "Isolation, sequencing and mutational analysis of a gene cluster involved
RT   in nitrite reduction in Paracoccus denitrificans.";
RL   Antonie Van Leeuwenhoek 66:111-127(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methylation of both C-2 and C-7 of
CC       uroporphyrinogen III leading to precorrin-1 and precorrin-2; their
CC       oxidative esterification gives respectively factor I octamethyl ester
CC       and sirohydrochlorin (By similarity). Inactivation of uroporphyrinogen-
CC       III methyltransferase results in the loss of nitrite and nitric oxide
CC       reductase activities, but not of nitrous oxide reductase activity.
CC       Likely involved in heme D1 biosynthesis. {ECO:0000250}.
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   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U05002; AAA93119.1; -; Genomic_DNA.
DR   EMBL; CP000489; ABL70575.1; -; Genomic_DNA.
DR   RefSeq; WP_011748768.1; NC_008686.1.
DR   AlphaFoldDB; Q51701; -.
DR   SMR; Q51701; -.
DR   STRING; 318586.Pden_2488; -.
DR   PRIDE; Q51701; -.
DR   EnsemblBacteria; ABL70575; ABL70575; Pden_2488.
DR   KEGG; pde:Pden_2488; -.
DR   eggNOG; COG0007; Bacteria.
DR   HOGENOM; CLU_011276_7_0_5; -.
DR   OMA; TRPEQEE; -.
DR   UniPathway; UPA00262; UER00211.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-EC.
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; 3.30.950.10; -; 1.
DR   Gene3D; 3.40.1010.10; -; 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; IPR003043; Uropor_MeTrfase_CS.
DR   Pfam; PF00590; TP_methylase; 1.
DR   SUPFAM; SSF53790; SSF53790; 1.
DR   TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
DR   PROSITE; PS00839; SUMT_1; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Porphyrin biosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..287
FT                   /note="Uroporphyrinogen-III C-methyltransferase"
FT                   /id="PRO_0000150385"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         116..118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         199
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   287 AA;  30029 MW;  AA319E29BAC6C461 CRC64;
     MAGKTVTNGA AQGKAARSGA DGAVRGKAGM GRVDLIGAGP GDPELLTLRA LRLLQQADVV
     VHDRLVSDEV MACIPAHVRR IPVGKAAGFH PVPQEQINAL LVELGLSGLT VARLKGGDPT
     IFGRGGEEFE AVTRAGIPCD YVPGITAAQG AAVSARFPLT HRGLATGLRH VTGHRARDAA
     LDLDWASLAD PQTTLAIYMG AANMAEIARE LIRHGMPADL PVLAVSQAST PQEQRLHATL
     QDIAAALARK PLPAPVLFIV GHVAAMAEDC ALPQELYRPE WRLVAHG