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Database: UniProt
Entry: Q6NHA4_CORDI
LinkDB: Q6NHA4_CORDI
Original site: Q6NHA4_CORDI 
ID   Q6NHA4_CORDI            Unreviewed;       415 AA.
AC   Q6NHA4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Precorrin-6Y C5,15-methyltransferase {ECO:0000313|EMBL:CAE49765.1};
GN   OrderedLocusNames=DIP1236 {ECO:0000313|EMBL:CAE49765.1};
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=257309 {ECO:0000313|EMBL:CAE49765.1, ECO:0000313|Proteomes:UP000002198};
RN   [1] {ECO:0000313|EMBL:CAE49765.1, ECO:0000313|Proteomes:UP000002198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis
RC   {ECO:0000313|Proteomes:UP000002198};
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.,
RA   Bentley S.D., Besra G.S., Churcher C., James K.D., De Zoysa A.,
RA   Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Moule S., Quail M.A., Rabbinowitsch E., Rutherford K.,
RA   Thomson N.R., Unwin L., Whitehead S., Barrell B.G.Parkhill.J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
RN   [2] {ECO:0007829|PDB:3HM2}
RP   X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 236-410 IN COMPLEX WITH CALCIUM
RP   AND MAGNESIUM.
RA   Kim Y., Bigelow L., Keigher L., Joachimiak A.;
RT   "Crystal Structure of Putative Precorrin-6Y C5,15-Methyltransferase
RT   Targeted Domain from Corynebacterium diphtheriae.";
RL   Submitted (MAY-2009) to the PDB data bank.
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; BX248357; CAE49765.1; -; Genomic_DNA.
DR   PDB; 3HM2; X-ray; 2.21 A; A/B/C/D/E/F/G/H=236-410.
DR   PDBsum; 3HM2; -.
DR   AlphaFoldDB; Q6NHA4; -.
DR   SMR; Q6NHA4; -.
DR   STRING; 257309.DIP1236; -.
DR   DNASU; 2649791; -.
DR   KEGG; cdi:DIP1236; -.
DR   HOGENOM; CLU_031955_0_0_11; -.
DR   UniPathway; UPA00148; -.
DR   EvolutionaryTrace; Q6NHA4; -.
DR   Proteomes; UP000002198; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR012818; CbiE.
DR   InterPro; IPR006365; Cbl_synth_CobL.
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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3HM2}; Calcium {ECO:0007829|PDB:3HM2};
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573};
KW   Metal-binding {ECO:0007829|PDB:3HM2};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002198};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..200
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
FT   BINDING         291
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:3HM2"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3HM2"
FT   BINDING         295
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:3HM2"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:3HM2"
SQ   SEQUENCE   415 AA;  44123 MW;  AC77FBA3129BF9A9 CRC64;
     MGRSKNDDGQ AHTGSITVVG IGAGGVEELG AQARTALRQA TIIIGSKRQL GLLPEDFQGD
     RIAWPSPLVP AIPALFAEFI DKEVVVLGSG DPMFHGIGST LHRLLPNHSM TVIPQPSSAS
     LACARLGWAL DTTSVYSLVT HPIAHLTLAI EQGDRFLVLG RNHESPHEIC EHLISLGQST
     AEVTVLSDIG SVSETITSGA ATDYPSNDSA LNVIAIRPLA ATRSRVPGLP DSEYVTDGQL
     TKQHVRALAI SALAPKPHET LWDIGGGSGS IAIEWLRSTP QTTAVCFEIS EERRERILSN
     AINLGVSDRI AVQQGAPRAF DDVPDNPDVI FIGGGLTAPG VFAAAWKRLP VGGRLVANAV
     TVESEQMLWA LRKQFGGTIS SFAISHEHTV GSFITMKPAL PVHQWTVVKA LTKEL
//
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