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 27-MAR-2024, entry version 107.
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; Bacillota; 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 GeneID; 24254048; -.
DR KEGG; ctc:CTC_00721; -.
DR HOGENOM; CLU_054212_0_0_9; -.
DR OrthoDB; 9811967at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001412; Chromosome.
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 NCBIfam; TIGR00380; cobal_cbiB; 1.
DR PANTHER; PTHR34308; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR PANTHER; PTHR34308:SF1; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR Pfam; PF03186; CobD_Cbib; 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
//
