COBD_METTP
ID COBD_METTP Reviewed; 316 AA.
AC A0B5W6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Probable cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=Mthe_0295;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
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., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
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; CP000477; ABK14090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B5W6; -.
DR STRING; 349307.Mthe_0295; -.
DR EnsemblBacteria; ABK14090; ABK14090; Mthe_0295.
DR KEGG; mtp:Mthe_0295; -.
DR HOGENOM; CLU_054212_0_2_2; -.
DR OMA; NSGYTMA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000674; 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..316
FT /note="Probable cobalamin biosynthesis protein CobD"
FT /id="PRO_1000116429"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 165..185
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 316 AA; 33940 MW; 74343A840F610B6A CRC64;
MITEIFPFSV LILALLIDIV LGEPPAALHP VVIIGTAVDR LRRMMPRRKI SGMIISVLVI
SGAVLAGFAL IRIAYATGSL AGSSEMGDIL ALIISSYLLK STFAFKSLIM TSREIGNLID
EDLDAAKHLL PALVSRNPLN LTHAQARSAV IESLSENYVD TIVSPLFYYV LFSCAGLGVE
AALAFKAVST MDSMLGYKSD DLREIGYVPA RLDDILNWIP ARLSLPLIMI ASPRKSMDIL
KACMRYHSVT PSPNSGWPMA AAAGALGTRM AKPGVYTILD EGRDPESEDV SSAISLIGRA
MVLAALLSAL LLILLR