COBD_PELPD
ID COBD_PELPD Reviewed; 323 AA.
AC A1AMC9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=Ppro_0870;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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; CP000482; ABK98499.1; -; Genomic_DNA.
DR RefSeq; WP_011734810.1; NC_008609.1.
DR AlphaFoldDB; A1AMC9; -.
DR STRING; 338966.Ppro_0870; -.
DR EnsemblBacteria; ABK98499; ABK98499; Ppro_0870.
DR KEGG; ppd:Ppro_0870; -.
DR eggNOG; COG1270; Bacteria.
DR HOGENOM; CLU_054212_0_0_7; -.
DR OMA; WGYRNER; -.
DR OrthoDB; 2029688at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000006732; 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..323
FT /note="Cobalamin biosynthesis protein CobD"
FT /id="PRO_1000090206"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ SEQUENCE 323 AA; 34479 MW; 7DAF106E1BFB5EC6 CRC64;
MIQPDPTVLA LALLLDLCLG DPRWLPHPVV MIGRLITFLE TLLRRCMANE RIAGVLLLAL
TVTSAASVTW LMVWGSARLH ALAGLMVAAL LSSTCLAARS LQRESCLVAD ALDAGDIASA
RVKLSYIVGR DTVDLDEEEI WRALIETVAE NTTDGIIAPL FWLALGGPVA GMAFKAVSTL
DSMVGYKNER YLRLGWASAR MDDLVNYIPA RLTALLMVMV APLIGLSQAN AASIALRDRL
NHPSPNSAHP ESAAAGALGI RLGGPSTYGG LLSVKQFIGD PLRSIDGQAY RGMIRLMYAT
TLAMAVISLA TAALLRGIHV TQL