ID R5VB49_9BACT Unreviewed; 605 AA.
AC R5VB49;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 33.
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 ORFNames=BN709_02763 {ECO:0000313|EMBL:CCZ80711.1};
OS Odoribacter laneus CAG:561.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=1263089 {ECO:0000313|EMBL:CCZ80711.1, ECO:0000313|Proteomes:UP000017974};
RN [1] {ECO:0000313|EMBL:CCZ80711.1, ECO:0000313|Proteomes:UP000017974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:561 {ECO:0000313|Proteomes:UP000017974};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCZ80711.1}.
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DR EMBL; CBAQ010000031; CCZ80711.1; -; Genomic_DNA.
DR AlphaFoldDB; R5VB49; -.
DR UniPathway; UPA00148; UER00227.
DR Proteomes; UP000017974; Unassembled WGS sequence.
DR GO; GO:0043780; F:cobalt-precorrin-5B C1-methyltransferase activity; IEA:RHEA.
DR GO; GO:0016994; F:precorrin-6A reductase activity; IEA:InterPro.
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 InterPro; IPR003723; Precorrin-6x_reduct.
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 Pfam; PF02571; CbiJ; 1.
DR SUPFAM; SSF111342; CbiD-like; 1.
DR PROSITE; PS51014; COBK_CBIJ; 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:UP000017974};
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 605 AA; 67549 MW; 322E3F8E92713B30 CRC64;
MILVFGGTTE GRKVVQLLDG AGKKYYYSTK GDRQRLESNY AERLSGGMDV AGIVAFCREK
GVGLLVDAAH PFAVQLRENI KQAAVELGIP VIRYERTYPA RDTAFIWCES WEEIVDYLCE
QNIRNLLALT GVQTIPRLKS YWCRYNCWFR VLDREQSLPL AEKYGFPREK LLYYKEGEGV
EKLIERIRPD AIVTKESGTS GYFEEKVKAA VEKRIRVIVL KRPPVPEAFY TVRGENGFRH
QLERLLPGFF PLRTGYTTGS CACAAAKAAF ITLVTGTVLR NCRFVLPCGE EMELPVGLVS
REEGRVTYSV VKDAGDDPDI TNGCEIRATV NFNTTHELRF LPGEGVGVVT LPGLGLEIGA
PAINPVPRRM MEEEFRKLQS FYKISQGIDI MLTVPGGKEL ALKTFNPKLG IEGGISIIGT
SGVVKPFSAE AFVATIRKEI QVAGALGYKH IVINSGAKSE RIVRERFSEL SPQAFVHYGN
YIGETLKIAE EEGISRITMG IMIGKAVKLA EGHQDTHSRH VLMNRDFIVT LMQESGVEEA
VWEKVKQITL ARELWSLLPQ NHPFFELLVR KCQEVCAPVF KNGSLEIILI PETSEGLLSP
DSLFP
//
