ID   COBD_CLOTE              Reviewed;         317 AA.
AC   Q897L3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=CTC_00721;
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO35323.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE015927; AAO35323.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_035110304.1; NC_004557.1.
DR   AlphaFoldDB; Q897L3; -.
DR   STRING; 212717.CTC_00721; -.
DR   EnsemblBacteria; AAO35323; AAO35323; CTC_00721.
DR   GeneID; 64180508; -.
DR   KEGG; ctc:CTC_00721; -.
DR   HOGENOM; CLU_054212_0_0_9; -.
DR   OMA; WGYRNER; -.
DR   OrthoDB; 2029688at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000001412; Chromosome.
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; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..317
FT                   /note="Cobalamin biosynthesis protein CobD"
FT                   /id="PRO_0000150926"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        152..172
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   317 AA;  35621 MW;  FABB1CA951F4FD65 CRC64;
     MGLIDIIVAV LLDFAIGDPY WFPHPVIYIG KLISYLEEVG RKHFKSNKGL KTLGGLVVLT
     IAITSFGIPF LILWMVKDSF WIFHFLNIIL IWTTLAAKSL KVEGKRVYYA LKNEDIQEAR
     EKLSYIVGRD TRNLTEEEII RADIETIMEN TADGVIAPLF YAMIGGAPFA MMYKGINTMD
     SMLGYMNDKY IHLGFFPAKV DDVFNFIPAR ISGVLICLSA PIVKGNIIRS FKVMLRDRKN
     HKSPNCAYPE GAGAGVMGIQ LGGTNVYFGK AVYKPTIGDR IKDLHHELIN DSVKLMYASE
     TLMVIIYALT VTSYNLR