ID C9Z601_STRSW Unreviewed; 403 AA.
AC C9Z601;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Putative SAM-dependent methyltransferase {ECO:0000313|EMBL:CBG74428.1};
GN OrderedLocusNames=SCAB_74441 {ECO:0000313|EMBL:CBG74428.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG74428.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG74428.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG74428.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879}.
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DR EMBL; FN554889; CBG74428.1; -; Genomic_DNA.
DR RefSeq; WP_013004966.1; NC_013929.1.
DR AlphaFoldDB; C9Z601; -.
DR STRING; 680198.SCAB_74441; -.
DR GeneID; 24307106; -.
DR KEGG; scb:SCAB_74441; -.
DR eggNOG; COG2241; Bacteria.
DR eggNOG; COG2242; Bacteria.
DR HOGENOM; CLU_031955_1_0_11; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001444; 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; cd02440; AdoMet_MTases; 1.
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; IPR006365; Cbl_synth_CobL.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR02467; CbiE; 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; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036428; CobL; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CBG74428.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBG74428.1}.
FT DOMAIN 15..178
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
SQ SEQUENCE 403 AA; 42154 MW; 7C56027202BA58D8 CRC64;
MADRVTVIGW DGSPLTAAAR SALAAATLVA GAAHHLALPE VPPRAERIRL GSVALAARRI
AGHRGTAVVL ADGDPGYFGV VRTLRSPEFG LEVEVVPGVS SVAAAFARAG MPWDDAEVVV
AHRRTLRRAV NVCRAHTKVA VLTSPGAGPA ELGLLLDSVH RTFVVCEELG TERERVTVLS
SDKAVDRTWR DPNLVIVIGG HAGAAAGGGW LAGRDPAAGP RGWALPSAVY GGALGEGESE
LLRSSQLACL GPRVGDLVWD IGSGSGAFAT EAARCGAAVI AVDHDPEACG RTTLAARRFG
VQLQVVHGAA PHVLENLPEP DVVRVGGGGA RVVSAVADRR PRRIVTHALT RPAAERVGRD
LTEHGYEVRC DFVQSVELDT RAWTERERSV AFLLSGTLPE RSV
//
