ID A0A3E2N9Y7_9CLOT Unreviewed; 390 AA.
AC A0A3E2N9Y7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_00787};
DE EC=2.1.1.195 {ECO:0000256|HAMAP-Rule:MF_00787};
DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000256|HAMAP-Rule:MF_00787};
GN Name=cbiD {ECO:0000256|HAMAP-Rule:MF_00787,
GN ECO:0000313|EMBL:RFZ77792.1};
GN ORFNames=DS742_17035 {ECO:0000313|EMBL:RFZ77792.1};
OS Clostridium indicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=759821 {ECO:0000313|EMBL:RFZ77792.1, ECO:0000313|Proteomes:UP000260680};
RN [1] {ECO:0000313|EMBL:RFZ77792.1, ECO:0000313|Proteomes:UP000260680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PI-S10-A1B {ECO:0000313|EMBL:RFZ77792.1,
RC ECO:0000313|Proteomes:UP000260680};
RA Krishna G., Summeta K., Shikha S., Prabhu P.B., Suresh K.;
RT "New species, Clostridium PI-S10-A1B.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B to
CC form cobalt-precorrin-6A. {ECO:0000256|HAMAP-Rule:MF_00787}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Co-precorrin-5B + S-adenosyl-L-methionine = Co-precorrin-6A +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26285, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:60063, ChEBI:CHEBI:60064;
CC EC=2.1.1.195; Evidence={ECO:0000256|HAMAP-Rule:MF_00787};
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route):
CC step 6/10. {ECO:0000256|HAMAP-Rule:MF_00787}.
CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000256|HAMAP-
CC Rule:MF_00787}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFZ77792.1}.
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DR EMBL; QOHO01000053; RFZ77792.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2N9Y7; -.
DR OrthoDB; 6439987at2; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000260680; Unassembled WGS sequence.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2110.10; CbiD-like; 1.
DR HAMAP; MF_00787; CbiD; 1.
DR InterPro; IPR002748; CbiD.
DR InterPro; IPR036074; CbiD_sf.
DR NCBIfam; TIGR00312; cbiD; 1.
DR PANTHER; PTHR35863; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR35863:SF1; COBALT-PRECORRIN-5B C(1)-METHYLTRANSFERASE; 1.
DR Pfam; PF01888; CbiD; 1.
DR PIRSF; PIRSF026782; CbiD; 1.
DR SUPFAM; SSF111342; CbiD-like; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00787}; Reference proteome {ECO:0000313|Proteomes:UP000260680};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00787};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00787}.
SQ SEQUENCE 390 AA; 42146 MW; A1B6CB4596A1C922 CRC64;
MEKRELRCGF TTGTCAAVAA KAAAAMLLSG NPLQHMKLMT PKGTEADLPL FHVVVKQDKA
SCAVRKDAGD DPDVTDKALI FASVEFLNEA LEDGSAAGCS FVREKTGEFG QLVLTALKGV
GRVTKPGLSS PVGYPAINPV PRSMIFDEVD EVRRMAGYKG ALLISVWIPK GRELAEKTFN
SKLGITGGLS ILGTTGIVKP MSEEALVATI RLELHMKAVA GLKRVILTPG NYGESFIKEE
LNLPEGEGVT VSNFIRESCR MVKEEGFEQI LFVGHIGKLV KVAGGVENTH SRYGDRRMEV
LWDCARAFLG SEEKEAIRSA NTMETAAGIL KELGVLKPVM SEVVKRIKAY MTDWTGGIPV
EVITFSNTLG ILSMTPDAPE MIKKYFTADT
//
