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Database: UniProt
Entry: A0A1F1E5M9_9PORP
LinkDB: A0A1F1E5M9_9PORP
Original site: A0A1F1E5M9_9PORP 
ID   A0A1F1E5M9_9PORP        Unreviewed;       614 AA.
AC   A0A1F1E5M9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=HMPREF2890_03305 {ECO:0000313|EMBL:OFR37764.1};
OS   Porphyromonas sp. HMSC065F10.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1739394 {ECO:0000313|EMBL:OFR37764.1, ECO:0000313|Proteomes:UP000177035};
RN   [1] {ECO:0000313|EMBL:OFR37764.1, ECO:0000313|Proteomes:UP000177035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC065F10 {ECO:0000313|EMBL:OFR37764.1,
RC   ECO:0000313|Proteomes:UP000177035};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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:OFR37764.1}.
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DR   EMBL; LTXH01000107; OFR37764.1; -; Genomic_DNA.
DR   RefSeq; WP_070465306.1; NZ_KV793774.1.
DR   AlphaFoldDB; A0A1F1E5M9; -.
DR   STRING; 1739394.HMPREF2890_03305; -.
DR   OrthoDB; 6439987at2; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000177035; 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:UP000177035};
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   614 AA;  67188 MW;  B3E3B03101E50143 CRC64;
     MGKILIIGGT TEGRAAVEVC EEAGKPFLYS TLGTSQEIAL HHGTRLEGPL DADAMTSLCR
     REEVSVLVDA AHPFATIVHR NVAKAASEVA LPTVRYERAF PPLPEGALSV SSFPEAMKEL
     ERLAPRRLLA LTGVKSIAAM GDYPLRHEVW LRVMPIPETE RIISESDFPR NRLIYYDREQ
     DDRALMERLR PDLLLLKESG ESSGFEEKVK AATALGIPIL VIRRPTLGYR PTETVLGPVG
     LRRALERLDP DFFPLRIGFT TGTTATAATT AALLALLNDE TYAEVPVRLL TGEEIRFPIS
     ETCIESEECA TATAIKYSGD DPDVTSGTTI LSTVRLTDSH TGVTFYGGKG VGRITLPGIG
     LPIGDPAINP GPRQMMTEAV GRLVDLSRVG IDITITVPEG ETLAPHTFNP RLGVVDGISI
     LGTTGVLRPF STEAWVDSIR REMGVSRSVF GEHLVINSGG KSERWLRAHF PDLPPNAFVQ
     YGNFIGRCLE MARSMDFAHI TLGIMIGKAV KLAEGQLDTH SKKSVMSKPF IRSLGRESGL
     DEATLDRIDG ITMAGEIWEI LPDHAHPFYH ILLDRCYAVC KPLVPGIRLD LILIDKEGGL
     IERNAEDKNK RNHV
//
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