ID   COBD_METM7              Reviewed;         306 AA.
AC   A6VFP2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Probable cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=MmarC7_0198;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. {ECO:0000255|HAMAP-
CC       Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00024};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00024}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00024}.
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DR   EMBL; CP000745; ABR65268.1; -; Genomic_DNA.
DR   RefSeq; WP_011976605.1; NC_009637.1.
DR   AlphaFoldDB; A6VFP2; -.
DR   STRING; 426368.MmarC7_0198; -.
DR   EnsemblBacteria; ABR65268; ABR65268; MmarC7_0198.
DR   GeneID; 5329103; -.
DR   KEGG; mmz:MmarC7_0198; -.
DR   eggNOG; arCOG04274; Archaea.
DR   HOGENOM; CLU_054212_0_2_2; -.
DR   OMA; NSGYTMA; -.
DR   OrthoDB; 101304at2157; -.
DR   UniPathway; UPA00148; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00024; CobD_CbiB; 1.
DR   InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR   PANTHER; PTHR34308; PTHR34308; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
DR   TIGRFAMs; TIGR00380; cobD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cobalamin biosynthesis; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..306
FT                   /note="Probable cobalamin biosynthesis protein CobD"
FT                   /id="PRO_1000074381"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   306 AA;  34234 MW;  FFD396B7E6CC8A0B CRC64;
     MTNPIYLILA DFFDRYIGEP PEKIHPVVFI GKLICFFENV FKSTNSVNKT RDLLFGFLNV
     ILVLAIVFFM TYEIEQIINS ISNSYIKISI YSIILSFSIG HKSLIEFSKA PIKFIVNNDL
     EGAKKSVQCI VSRNTSELDK KHILSASIES ASENITDSII APLIYAAIFG LPGAFLYRAV
     NTFDAMIGYK SEKYQYYGKT AAYLDDILNF IPSRIAGMLL IISAPFYGGN IKSAIYGYFN
     EGNKTPSPNS GYTMATLANS LNMELEKIGY YKLGKGEITI EKALNSLKAV DYSVLLFLII
     YTVLLM