ID F5YLB7_TREPZ Unreviewed; 419 AA.
AC F5YLB7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Precorrin-6y C5,15-methyltransferase (Decarboxylating) {ECO:0000313|EMBL:AEF86059.1};
GN OrderedLocusNames=TREPR_0525 {ECO:0000313|EMBL:AEF86059.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF86059.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF86059.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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DR EMBL; CP001843; AEF86059.1; -; Genomic_DNA.
DR RefSeq; WP_015709495.1; NC_015578.1.
DR AlphaFoldDB; F5YLB7; -.
DR STRING; 545694.TREPR_0525; -.
DR KEGG; tpi:TREPR_0525; -.
DR eggNOG; COG2241; Bacteria.
DR eggNOG; COG2242; Bacteria.
DR HOGENOM; CLU_031955_1_2_12; -.
DR OrthoDB; 9780707at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd11644; Precorrin-6Y-MT; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; IPR012818; CbiE.
DR InterPro; IPR014008; Cbl_synth_MTase_CbiT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR02467; CbiE; 1.
DR NCBIfam; TIGR02469; CbiT; 1.
DR PANTHER; PTHR43182; COBALT-PRECORRIN-6B C(15)-METHYLTRANSFERASE (DECARBOXYLATING); 1.
DR PANTHER; PTHR43182:SF1; COBALT-PRECORRIN-7 C(5)-METHYLTRANSFERASE; 1.
DR Pfam; PF01135; PCMT; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 4: Predicted;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AEF86059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEF86059.1}.
FT DOMAIN 4..188
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 419 AA; 44329 MW; B0FC3DA4B32FCD11 CRC64;
MKQIVIVGTG MGPSSISGEG MKALGDAEVW FGASRLLELL KPFFAEKTVY PIYKPGEILE
AIKNRDENSF AVLVSGDTGF YSAAAGICEA LSDYEPRLIP GVSSIAYFCA RLGIPWQDAA
LLSVHGRDLS ALTGLVRRNH HTFCLTGNNA AALGEALCAT GYGDITVHAG ENLGSAEERI
RTITARELSA SDIARETPLQ NARETPLQVA ERTSLHIAPL SVLLFVNEAP DDRIRFGLPD
EVFVRSEGIP MTKSEIRALS LAKLALRPGD ICWDIGAGTG SVTVEMAMAA YRGKVYAVER
QGNVLGLISQ NCWAFHLGNV EPIAGEAPGG LAELPPPDAV FIGGSGGNLK EILTVILEKN
SRARIVITAI TLETAAAALA LLPGAELTQV SAARAKKAGD SHLFIGQNPV MIISAGGWE
//
