COBD_DESPS
ID COBD_DESPS Reviewed; 330 AA.
AC Q6ALU7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=DP1949;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG36678.1; -; Genomic_DNA.
DR RefSeq; WP_011189190.1; NC_006138.1.
DR AlphaFoldDB; Q6ALU7; -.
DR STRING; 177439.DP1949; -.
DR EnsemblBacteria; CAG36678; CAG36678; DP1949.
DR KEGG; dps:DP1949; -.
DR eggNOG; COG1270; Bacteria.
DR HOGENOM; CLU_054212_0_0_7; -.
DR OMA; WGYRNER; -.
DR OrthoDB; 2029688at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000602; 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..330
FT /note="Cobalamin biosynthesis protein CobD"
FT /id="PRO_1000201946"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ SEQUENCE 330 AA; 36562 MW; F478E70CFA3C9582 CRC64;
MFSIKILLAI ILDLFLGDPS CYPHPVRCIG LAINRWEKFY RPRVAQPFWA GVLTVCSVLT
LVILTLAVFF TLLAIFPPIV TDFAAVLLLY TTVAIKDLKK ESMAVYRALI QGEDLPKTRK
LLARIVGRDT ENLDRPAIIR ATVETVGENL ADGIIAPLFW AVALSIFAPL LGVKAIVLAS
VGAMSYKAIN TMDSMLGYKN ERYILFGRAA ARLDDWANWL PARCTALGIV AISFMAGYNG
PQAWKIFKRD RYQHTSPNAG HPEAALAGAL NIRLCGPSVY FGNIVEKPYI GNALRAIEPD
DIRQANRIVL FTTFLLSLLF LLFRFVLTGL
