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Database: UniProt
Entry: F7KBZ4_9FIRM
LinkDB: F7KBZ4_9FIRM
Original site: F7KBZ4_9FIRM 
ID   F7KBZ4_9FIRM            Unreviewed;       320 AA.
AC   F7KBZ4;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Cobalamin biosynthesis protein CobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   ORFNames=HMPREF0994_03373 {ECO:0000313|EMBL:EGN39880.1};
OS   Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=658086 {ECO:0000313|EMBL:EGN39880.1, ECO:0000313|Proteomes:UP000003336};
RN   [1] {ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EGN39880.1, ECO:0000313|Proteomes:UP000003336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EGN39880.1,
RC   ECO:0000313|Proteomes:UP000003336};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA   McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1.";
RL   Submitted (APR-2013) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGN39880.1}.
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DR   EMBL; ACTP02000012; EGN39880.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7KBZ4; -.
DR   STRING; 658086.HMPREF0994_03373; -.
DR   PATRIC; fig|658086.3.peg.3686; -.
DR   eggNOG; COG1270; Bacteria.
DR   HOGENOM; CLU_054212_0_0_9; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000003336; Unassembled WGS sequence.
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:UP000003336};
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        54..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        297..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   320 AA;  34674 MW;  63DC095918BB3B99 CRC64;
     MYTTISIFAG FILDLLFGDP YWMPHPVRAM GKGIQALEKK LRRPDGTPAA QMRAGALLVC
     MIVAVSILIP VLLLWLAYWL HPAAGLVLES FMCYQIMATK CLKVESMKVC RALRDGDVEK
     AREAVSMIVG RDTAVLSAEG ITKAAVETVA ENTSDGSIAP LFFMLLGGPA AGFAYKAVNT
     MDSMLGYKNE KYLYFGRPAA RLDDVVNFIP SRLAALLMIA AAWLCGMDGK GAFRIWRRDR
     FKHASPNSAQ TESVCAGALG IALAGDAVYF GKVVKKPFIG DGKRPAEPED IARANRLLYV
     SASLLCAAGL LIRCVLPLVF
//
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