ID   E1R8J8_SEDSS            Unreviewed;       379 AA.
AC   E1R8J8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
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   OrderedLocusNames=Spirs_0185 {ECO:0000313|EMBL:ADK79342.1};
OS   Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS   (Spirochaeta smaragdinae).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Sediminispirochaeta.
OX   NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK79342.1, ECO:0000313|Proteomes:UP000002318};
RN   [1] {ECO:0000313|EMBL:ADK79342.1, ECO:0000313|Proteomes:UP000002318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC   {ECO:0000313|Proteomes:UP000002318};
RX   PubMed=21304743; DOI=10.4056/sigs.1143106;
RA   Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA   Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA   Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA   Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT   4228).";
RL   Stand. Genomic Sci. 3:136-144(2010).
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}.
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DR   EMBL; CP002116; ADK79342.1; -; Genomic_DNA.
DR   RefSeq; WP_013252806.1; NC_014364.1.
DR   AlphaFoldDB; E1R8J8; -.
DR   STRING; 573413.Spirs_0185; -.
DR   KEGG; ssm:Spirs_0185; -.
DR   eggNOG; COG1903; Bacteria.
DR   HOGENOM; CLU_041273_1_0_12; -.
DR   OrthoDB; 6439987at2; -.
DR   UniPathway; UPA00148; UER00227.
DR   Proteomes; UP000002318; Chromosome.
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:UP000002318};
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   379 AA;  40496 MW;  4A6508D904DD48AB CRC64;
     MAQWYDQELG KVSGMRLGIT TGSCAQAAAR AALEFLLGIF ADKRVEITLP KGHRRYSGRQ
     ILVPVESIGA TSDGTGAEAL VRKDSGDDPD ITDGILIGAR VRLKEGNGVE IDGAEGVGRI
     TRPGLAGKVG EAAINPIPRR MIREELLPLL PEGKGCRVEI FVPEGIALAE KTWNPRIGIL
     GGISIIGTKG VVEPKSEEAY KASINRVIHS YLKSGMSRLI ITPGYVGEAF LSSRGIALDR
     VVTVGDHVGH ALLRGADHGA KELLLVGHIG KLTKIAVAMF NTHWSSGDAR LEVIAAYAGA
     AGASAEKVRR LLSLSLAEEA VALIHDWGLD EIWNAIARRA AERTEKLVEG RCTIGVVLLD
     LKGHSLGSWP KERVEGWLK
//