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Database: UniProt
Entry: A0A2D0KQ57_9GAMM
LinkDB: A0A2D0KQ57_9GAMM
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ID   A0A2D0KQ57_9GAMM        Unreviewed;       382 AA.
AC   A0A2D0KQ57;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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:PHM65425.1};
GN   ORFNames=Xsto_02003 {ECO:0000313|EMBL:PHM65425.1};
OS   Xenorhabdus stockiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351614 {ECO:0000313|EMBL:PHM65425.1, ECO:0000313|Proteomes:UP000222366};
RN   [1] {ECO:0000313|EMBL:PHM65425.1, ECO:0000313|Proteomes:UP000222366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17904 {ECO:0000313|EMBL:PHM65425.1,
RC   ECO:0000313|Proteomes:UP000222366};
RX   PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA   Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA   Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA   Ebersberger I., Bode H.B.;
RT   "Natural product diversity associated with the nematode symbionts
RT   Photorhabdus and Xenorhabdus.";
RL   Nat. Microbiol. 2:1676-1685(2017).
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:PHM65425.1}.
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DR   EMBL; NJAJ01000016; PHM65425.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0KQ57; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000222366; 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};
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   382 AA;  41616 MW;  664D0E723FAD2B84 CRC64;
     MNDLIELGTV WHRGKQYRKG YTTGSCATAA AKVAALMILR QQIIHQVSIV TPSGITLALN
     IEQPLIEGDQ AVAAIRKDGG DDVDATHGML IFARVSLNDS GVITLDGGDG IGRVTRVGVG
     LPIGWAAINK TPRQTIEETV REVIGPNRGA DIIIFAPEGE ERAKQTYNDR LGIKGGISII
     GTTGIVTPMS EESWKRSLAL ELETKRASGL DRIIFVPGNH GERFVSQQLG IDASYVVTMS
     NFVGYMLQEA VRLEFRHIVL VGHVGKLVKI AAGIFHTHSH IADGRMETLI ANLALMGAPF
     ELIQAVDQCD TTEAAIELIA GQGWQGVYQQ IAQKICWRID QMLRFAKSKP QCDAILFSFD
     NQVLGCNRSV DQIVRDFMEG GR
//
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