COBM_RHOCB
ID COBM_RHOCB Reviewed; 261 AA.
AC O68100; D5AV02;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Precorrin-4 C(11)-methyltransferase;
DE EC=2.1.1.133;
DE AltName: Full=Precorrin-3 methylase;
GN Name=cobM; OrderedLocusNames=RCAP_rcc02040;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT SB1003.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Catalyzes the methylation of C-11 in precorrin-4 to form
CC precorrin-5.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=precorrin-4 + S-adenosyl-L-methionine = precorrin-5 + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:22012, ChEBI:CHEBI:57769,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:77871;
CC EC=2.1.1.133;
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 4/10.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AF010496; AAC16190.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85784.1; -; Genomic_DNA.
DR PIR; T03537; T03537.
DR RefSeq; WP_013067763.1; NC_014034.1.
DR PDB; 3NDC; X-ray; 2.00 A; A/B=1-261.
DR PDB; 3NEI; X-ray; 2.50 A; A/B=1-261.
DR PDBsum; 3NDC; -.
DR PDBsum; 3NEI; -.
DR AlphaFoldDB; O68100; -.
DR SMR; O68100; -.
DR STRING; 272942.RCAP_rcc02040; -.
DR EnsemblBacteria; ADE85784; ADE85784; RCAP_rcc02040.
DR GeneID; 31490902; -.
DR KEGG; rcp:RCAP_rcc02040; -.
DR eggNOG; COG2875; Bacteria.
DR HOGENOM; CLU_011276_7_1_5; -.
DR OMA; WSAMGEQ; -.
DR OrthoDB; 1185397at2; -.
DR UniPathway; UPA00148; UER00215.
DR EvolutionaryTrace; O68100; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11641; Precorrin-4_C11-MT; 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; IPR006362; Cbl_synth_CobM/CibF.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; SSF53790; 1.
DR TIGRFAMs; TIGR01465; cobM_cbiF; 1.
DR PROSITE; PS00839; SUMT_1; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cobalamin biosynthesis; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..261
FT /note="Precorrin-4 C(11)-methyltransferase"
FT /id="PRO_0000150397"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3NEI"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 59..72
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:3NDC"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:3NDC"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:3NDC"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3NDC"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3NDC"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:3NDC"
SQ SEQUENCE 261 AA; 27704 MW; AAEDA90B8642DCDB CRC64;
MTVHFIGAGP GAADLITIRG RDLIASCPVC LYAGSLVPEA LLAHCPPGAK IVNTAPMSLD
AIIDTIAEAH AAGQDVARLH SGDLSIWSAM GEQLRRLRAL NIPYDVTPGV PSFAAAAATL
GAELTLPGVA QSVILTRTSG RASAMPAGET LENFARTGAV LAIHLSVHVL DEVVQKLVPH
YGEDCPVAIV WRASWPDQRV VRATLATLQT SLGAELERTA LILVGRSLAT EDFDESRLYA
GDYDRRYRPL GTHPRFPEGS E
