ID   COBD_CLOPE              Reviewed;         315 AA.
AC   Q8XLK2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-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=CPE1039;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB80745.1; -; Genomic_DNA.
DR   RefSeq; WP_011010194.1; NC_003366.1.
DR   AlphaFoldDB; Q8XLK2; -.
DR   STRING; 195102.gene:10490302; -.
DR   EnsemblBacteria; BAB80745; BAB80745; BAB80745.
DR   KEGG; cpe:CPE1039; -.
DR   HOGENOM; CLU_054212_0_0_9; -.
DR   OMA; NSGYTMA; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000818; 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..315
FT                   /note="Cobalamin biosynthesis protein CobD"
FT                   /id="PRO_0000150925"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   315 AA;  35048 MW;  409A461A1C476D3B CRC64;
     MIKIIIGYVL DLIIGDPNNP YHPIRYIGKL ASNMEKLWRK VFKKNLKIAG FFAWLFIVFI
     TFGVTLGIVH IANKINPILG TVVSGILIYF CISAKGLKVE GLKVIKILKE GDIVKARKQL
     SYIVGRDTEN LDEEAIVRAV VETVAENMSD GIIAPLFFAG IGGAPLAFLY KAVNTCDSMF
     GYKNEKYKDF GFFSAKLDDV FNYIPARLTA YLIVISSFIL RLNCKNIFKI YKRDRYNHSS
     PNSAHPEAAV AGALGIRLGG ANYYFGKLVE KPTIGDAKKK IEISDVYKTN NILGMVSFLG
     MVVALIIRCI LEVII