SUMT_PSEAE
ID SUMT_PSEAE Reviewed; 245 AA.
AC Q9I2W4;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Uroporphyrinogen-III C-methyltransferase;
DE Short=Urogen III methylase;
DE EC=2.1.1.107 {ECO:0000250|UniProtKB:P21631};
DE AltName: Full=S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase;
DE Short=SUMT;
DE AltName: Full=Uroporphyrinogen III methylase;
DE Short=UROM;
GN Name=cobA; OrderedLocusNames=PA1778;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Catalyzes the two successive C-2 and C-7 methylation
CC reactions involved in the conversion of uroporphyrinogen III to
CC precorrin-2 via the intermediate formation of precorrin-1. It is a step
CC in the biosynthesis of both cobalamin (vitamin B12) and siroheme.
CC {ECO:0000250|UniProtKB:P21631}.
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 Evidence={ECO:0000250|UniProtKB:P21631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32460;
CC Evidence={ECO:0000250|UniProtKB:P21631};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000250|UniProtKB:P21631}.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
CC {ECO:0000250|UniProtKB:P21631}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05167.1; -; Genomic_DNA.
DR PIR; H83423; H83423.
DR RefSeq; NP_250469.1; NC_002516.2.
DR RefSeq; WP_003087845.1; NZ_QZGE01000003.1.
DR AlphaFoldDB; Q9I2W4; -.
DR SMR; Q9I2W4; -.
DR STRING; 287.DR97_108; -.
DR PaxDb; Q9I2W4; -.
DR EnsemblBacteria; AAG05167; AAG05167; PA1778.
DR GeneID; 877770; -.
DR KEGG; pae:PA1778; -.
DR PATRIC; fig|208964.12.peg.1843; -.
DR PseudoCAP; PA1778; -.
DR HOGENOM; CLU_011276_7_0_6; -.
DR InParanoid; Q9I2W4; -.
DR OMA; FIHRLML; -.
DR PhylomeDB; Q9I2W4; -.
DR BioCyc; PAER208964:G1FZ6-1809-MON; -.
DR UniPathway; UPA00148; UER00211.
DR UniPathway; UPA00262; UER00211.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019354; P:siroheme biosynthetic process; IBA:GO_Central.
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.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Methyltransferase; Porphyrin biosynthesis;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..245
FT /note="Uroporphyrinogen-III C-methyltransferase"
FT /id="PRO_0000287818"
FT BINDING 12
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 87..89
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 168
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 197
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
FT BINDING 225
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000250|UniProtKB:P21631"
SQ SEQUENCE 245 AA; 25925 MW; 7BB11C9942E56F7F CRC64;
MSGKVWLVGA GPGDPELLTL KAVRALQDAD VVMVDDLVNP SILEHCPSAR LVRVGKRGGC
RSTPQDFIQR LMLRHARQGR SVVRLKGGDP CIFGRAGEEA EWLARHGIDS EIVNGITAGL
AGATACGIPL TYRGISRGVT LVTAHTQDDS PLAWEALARS GTTLVVYMGV ARLAEIQAGL
LAGGMAEDTP LAMIENATLG NQRECRSNLG ELLRDAGRFA LKSPAILVIG EVTRDIVSQP
ISLSA
