ID A0A1H1P0E6_9ACTN Unreviewed; 255 AA.
AC A0A1H1P0E6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Precorrin-4 C11-methyltransferase {ECO:0000313|EMBL:SDS04663.1};
GN ORFNames=SAMN04488570_1013 {ECO:0000313|EMBL:SDS04663.1};
OS Nocardioides scoriae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=642780 {ECO:0000313|EMBL:SDS04663.1, ECO:0000313|Proteomes:UP000198859};
RN [1] {ECO:0000313|Proteomes:UP000198859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005879, ECO:0000256|RuleBase:RU003960}.
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DR EMBL; LT629757; SDS04663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1P0E6; -.
DR STRING; 642780.SAMN04488570_1013; -.
DR OrthoDB; 9815856at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000198859; Chromosome i.
DR GO; GO:0046026; F:precorrin-4 C11-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; cd11641; Precorrin-4_C11-MT; 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 NCBIfam; TIGR01465; cobM_cbiF; 1.
DR PANTHER; PTHR45790:SF4; COBALT-PRECORRIN-4 C(11)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00839; SUMT_1; 1.
DR PROSITE; PS00840; SUMT_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU003960};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 2..208
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT REGION 235..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 255 AA; 26823 MW; C6C0433DB7744BCE CRC64;
MTVHFVGAGP GAADLLTLRA ASLLARADVV LYPGTYLDAE VLGHARPDAR LVDTQDLDLD
QILAELVAAD GAGRDVVRLV SGDPSLYSAV AEQTRRLDAA GVGWDVTPGV PAYAAAAALV
GRELTVPLVA QSVVLTRAQA RSTAMPETES LARFAATRAT LALHLAVTRT RELMAELEPD
YGADCPVVVV HRASQPDELV LRGTVADVAD AVERAGLRQA AVILVGRALD PHDGGESYLY
DPARDRAAKR RPAQP
//
