CBIB_SALPA
ID CBIB_SALPA Reviewed; 319 AA.
AC Q5PDS9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Cobalamin biosynthesis protein CbiB {ECO:0000255|HAMAP-Rule:MF_00024};
GN Name=cbiB {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=SPA0837;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76825.1; -; Genomic_DNA.
DR RefSeq; WP_000153664.1; NC_006511.1.
DR AlphaFoldDB; Q5PDS9; -.
DR EnsemblBacteria; AAV76825; AAV76825; SPA0837.
DR KEGG; spt:SPA0837; -.
DR HOGENOM; CLU_054212_0_0_6; -.
DR OMA; WGYRNER; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008185; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..319
FT /note="Cobalamin biosynthesis protein CbiB"
FT /id="PRO_1000057218"
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 296..316
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ SEQUENCE 319 AA; 35500 MW; 65FEB58447578E6F CRC64;
MTILAWCIAW VLDFIIGDPQ HWPHPVRWIG RLITFVQRIV RRYCPGDKAL RIGGGVMWVV
VVGVTWGVAW GVLALAQRIH PWFGWSVEVW MIFTTLAGRS LARAAQEFER PLRENDLAES
RIKLSWIVGR DTSQLQPAQI NRAVVETVAE NTVDGIIAPL FFLFLGGAPL AMAYKAVNTL
DSMVGYKHEK YRAIGMVSAR MDDVANYLPA RLSWLLLGIA AGLCRLSDWR ALRIGWRDRY
NHSSPNCAWS EACVAGALGI QLGGPNNYFG ERVDKPWIGD AQRGISVDDI SRTIRLMWVA
STLALALFIA ARCGLSGVA