ID   CBIB_SALAR              Reviewed;         319 AA.
AC   A9MLR0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Cobalamin biosynthesis protein CbiB {ECO:0000255|HAMAP-Rule:MF_00024};
GN   Name=cbiB {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=SARI_00854;
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group. However, the true cosubstrate
CC       could be (R)-1-amino-2-propanol O-2-phosphate, leading to cobinamide
CC       phosphate. {ECO:0000255|HAMAP-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; CP000880; ABX20773.1; -; Genomic_DNA.
DR   RefSeq; WP_000153641.1; NC_010067.1.
DR   AlphaFoldDB; A9MLR0; -.
DR   STRING; 41514.SARI_00854; -.
DR   EnsemblBacteria; ABX20773; ABX20773; SARI_00854.
DR   KEGG; ses:SARI_00854; -.
DR   HOGENOM; CLU_054212_0_0_6; -.
DR   OMA; WGYRNER; -.
DR   OrthoDB; 2029688at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002084; 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..319
FT                   /note="Cobalamin biosynthesis protein CbiB"
FT                   /id="PRO_1000074383"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   319 AA;  35616 MW;  E966F1BCEDA2DD0E CRC64;
     MTILAWCIAW VLDFIIGDPQ HWPHPVRWIG RLITFVQHIV RRYCHSDKAL RIGGGVMWIV
     VVGATWGMAW GVLALAQRIH PWLGWSVEVW MIFTVLAGRS LARAAQDVER PLRENDLAES
     RIKLSWIVGR DTSQLQPEQI NRAVVETVAE NTVDGIIAPL FFLFLGGAPL AMAYKAVNTL
     DSMVGYKHEK YRAIGMVSAR MDDVANYLPA RLSWLLLGIA AGLCRLSGWR ALRIGWRDRY
     NHSSPNCAWS EACVAGALGI QLGGPNNYFG ERVDKPWIGD AQRDISVDDI SRTIRLMWGA
     STLALALFIA ARCWLSGVA