COBD_RUEPO
ID COBD_RUEPO Reviewed; 306 AA.
AC Q5LNI0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=SPO3225;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV96460.1; -; Genomic_DNA.
DR RefSeq; WP_011048915.1; NC_003911.12.
DR AlphaFoldDB; Q5LNI0; -.
DR STRING; 246200.SPO3225; -.
DR EnsemblBacteria; AAV96460; AAV96460; SPO3225.
DR KEGG; sil:SPO3225; -.
DR eggNOG; COG1270; Bacteria.
DR HOGENOM; CLU_054212_0_1_5; -.
DR OMA; WGYRNER; -.
DR OrthoDB; 2029688at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001023; 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..306
FT /note="Cobalamin biosynthesis protein CobD"
FT /id="PRO_1000057219"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ SEQUENCE 306 AA; 32958 MW; 17E147EAA97E6188 CRC64;
MSTALLLGFA MLLDAALGEP EWLWSRLRHP AVLIGDIISV LDDELNEGGH RRLKGVAVTA
ILAVGALSVG ALLSLLGPVA EVLICAILLA QKSLAGHVAD VADALRLSLP EARRSVARIV
SRDTATMSEP QVARAAIESA AENLSDGVIA PAFWFLVGGL PGLLLYKTIN TADSMVGYMN
ERYAQFGWAA ARLDDLLNLI PARLTCGMIV LLSNGWRHWR GIVEDAQRHI SPNAGWPEAA
MARALNIALA GPRSYHGEIR HLAWVNEEGR KEIGPREIER AVTLLWQVWA LALGLTLTLV
ALAAIF