ID L0D9B8_SINAD Unreviewed; 325 AA.
AC L0D9B8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN OrderedLocusNames=Sinac_1605 {ECO:0000313|EMBL:AGA25984.1};
OS Singulisphaera acidiphila (strain ATCC BAA-1392 / DSM 18658 / VKM B-2454 /
OS MOB10).
OC Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC Singulisphaera.
OX NCBI_TaxID=886293 {ECO:0000313|EMBL:AGA25984.1, ECO:0000313|Proteomes:UP000010798};
RN [1] {ECO:0000313|EMBL:AGA25984.1, ECO:0000313|Proteomes:UP000010798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1392 / DSM 18658 / VKM B-2454 / MOB10
RC {ECO:0000313|Proteomes:UP000010798};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Singulisphaera acidiphila DSM 18658.";
RL Submitted (FEB-2012) 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:0000256|HAMAP-
CC Rule:MF_00024}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|HAMAP-Rule:MF_00024}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_00024}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CobD/CbiB family.
CC {ECO:0000256|ARBA:ARBA00006263, ECO:0000256|HAMAP-Rule:MF_00024}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00024}.
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DR EMBL; CP003364; AGA25984.1; -; Genomic_DNA.
DR RefSeq; WP_015245154.1; NZ_JH621477.1.
DR AlphaFoldDB; L0D9B8; -.
DR STRING; 886293.Sinac_1605; -.
DR KEGG; saci:Sinac_1605; -.
DR eggNOG; COG1270; Bacteria.
DR HOGENOM; CLU_054212_0_0_0; -.
DR OrthoDB; 9811967at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000010798; 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 {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00024};
KW Reference proteome {ECO:0000313|Proteomes:UP000010798};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00024};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00024}.
FT TRANSMEM 64..88
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT TRANSMEM 302..321
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ SEQUENCE 325 AA; 34611 MW; 5081C2C212BD94B1 CRC64;
MPGLPLAVWS LPLGATLDLL LGDPRGWPHP VRAIGHLIVR LEAVARRLIK QAGGGERTER
LAGIWLTGHV VGIVGVAAWM IIVACDWLGP VPSLLGRSLL IYWGLAARSL GDETLQASEA
PDLKTARREL SMIVGRDTAT LDEAEIGRAC VETVAENYAD AVVAPLFWFV IGGPVGLWAF
KAVSTLDSMV GYRNAKYRDL GWASARFDDV AALIPSRLAW LLIGLAAWVA GERPGNALRI
GWRDGRKHPS PNAGWGEAAM AGALGIQLGG PATYGGVPGF KPLLGEPDEP IDRTTVRRSV
RVMRIAATLA VAFAWGVRSG LFGSP
//
