ID   COBD_SINSX              Reviewed;         323 AA.
AC   P21634;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Cobalamin biosynthesis protein CobD;
GN   Name=cobD;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=2211520; DOI=10.1128/jb.172.10.5968-5979.1990;
RA   Crouzet J., Cauchois L., Blanche F., Debussche L., Thibaut D.,
RA   Rouyez M.-C., Rigault S., Mayaux J.-F., Cameron B.;
RT   "Nucleotide sequence of a Pseudomonas denitrificans 5.4-kilobase DNA
RT   fragment containing five cob genes and identification of structural genes
RT   encoding S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase
RT   and cobyrinic acid a,c-diamide synthase.";
RL   J. Bacteriol. 172:5968-5979(1990).
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M59236; AAA25776.1; -; Genomic_DNA.
DR   AlphaFoldDB; P21634; -.
DR   BioCyc; MetaCyc:MON-142; -.
DR   UniPathway; UPA00148; -.
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   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
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; Porphyrin biosynthesis;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..323
FT                   /note="Cobalamin biosynthesis protein CobD"
FT                   /id="PRO_0000150934"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  34197 MW;  F7BE46C93BE14EA3 CRC64;
     MSETILLILA LALVIDRVVG DPDWLWARVP HPVVFFGKAI GFFDARLNRE DLEDSARKFR
     GVVAILLLLG ISAWFGHLLH RLFAVLGPLG FLLEAVLVAV FLAQKSLADH VRRVAGGLRQ
     GGLEGGRAAV SMIVGRDPKT LDEPAVCRAA IESLAENFSD GVVAPAFWYA VAGLPGLLAY
     KMLNTADSMI GHKSPKYLHF GWASARLDDL ANLPAARLSI LLISAGALIH RGASAAKDAL
     TVALRDHGLH RSPNSGWPEA AMAGALDLQL AGPRIYGGVK VSEPMINGPG RAVATSEDID
     AGIAVFYGAC TVMAGFVLAI AMI