ID A0A1I4F1D4_9BACL Unreviewed; 662 AA.
AC A0A1I4F1D4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Precorrin-3B C17-methyltransferase {ECO:0000313|EMBL:SFL11120.1};
GN ORFNames=SAMN03159341_103273 {ECO:0000313|EMBL:SFL11120.1};
OS Paenibacillus sp. 1_12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFL11120.1, ECO:0000313|Proteomes:UP000198699};
RN [1] {ECO:0000313|EMBL:SFL11120.1, ECO:0000313|Proteomes:UP000198699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_12 {ECO:0000313|EMBL:SFL11120.1,
RC ECO:0000313|Proteomes:UP000198699};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953}.
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DR EMBL; FOTE01000003; SFL11120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4F1D4; -.
DR STRING; 1566278.SAMN03159341_103273; -.
DR OrthoDB; 9772960at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000198699; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase 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; cd11646; Precorrin_3B_C17_MT; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 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; IPR006363; Cbl_synth_CobJ/CibH_dom.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR NCBIfam; TIGR01466; cobJ_cbiH; 1.
DR PANTHER; PTHR47036; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR47036:SF1; COBALT-FACTOR III C(17)-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 4: Predicted;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:SFL11120.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SFL11120.1}.
FT DOMAIN 4..215
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 536..639
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 271..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 71634 MW; C21272D0801314C3 CRC64;
MAGKLLIVGF GPGSFEHITK RAREALQESD VIIGYNTYVD LISGLLSDQQ IVRTGMTEEV
SRAQEAVRQA EAGKKVAVIS SGDAGVYGMA GLVYEVLIEK GWHPEDGVEV EIIPGISAIN
SSASLLGAPI MHDSCTISLS DHLTPWELIE RRVEAAGQAD FVIALYNPRS GRRTRQIVET
QRILLKYRSP ETPVGIVKSA YRDREHIVLT NLRDMLDHDI GMLTTVIIGN SSTMVYDGLM
ITPRGYQRKY TLGADVQPLR PHQRLRQEAE PWALEQLPED PNDEHDDEEW ESNDEGDSLI
EDIDDEEWDD EEDEVLAKNG GSLSAVSAVS PSSGAAGKPS LNYNEGIAAK AEAGKPYEGA
LGKAKAVEYL GISTAAEPSA VAVAERHVSA DPLLLAMEAL QLVERRNGVA SVSINTTAPA
VSVSGASVTA SAPAASSTAV TAGLFRQQSI FELAVSPGVA NKQFTAKQML TLAAVVGDKG
SMEYTPHHQL IVRVPTDNPA EITQRLSMEG FLLAPIGDVA QVKACDFCNG EKGESIAYAE
ELQAKLGGLG VPKEMRIGFN GCGMACYGAV NEDIGIVYRR GKFDLFLGGK TVGRNVHPAQ
PVAEGIKPED LVATIERIMQ RYVTEGHPNE RFHKFFKRVK ELEGYRHQDL PVFTIENAIC
GD
//