COBD_MYCTO
ID COBD_MYCTO Reviewed; 313 AA.
AC P9WP92; L0T982; Q10518;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Cobalamin biosynthesis protein CobD;
GN Name=cobD; OrderedLocusNames=MT2295;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC aminopropanol on the F carboxylic group. {ECO:0000250}.
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}.
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DR EMBL; AE000516; AAK46579.1; -; Genomic_DNA.
DR PIR; H70777; H70777.
DR RefSeq; WP_003901355.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WP92; -.
DR EnsemblBacteria; AAK46579; AAK46579; MT2295.
DR GeneID; 45426214; -.
DR KEGG; mtc:MT2295; -.
DR PATRIC; fig|83331.31.peg.2472; -.
DR HOGENOM; CLU_054212_1_2_11; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001020; 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..313
FT /note="Cobalamin biosynthesis protein CobD"
FT /id="PRO_0000426992"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 313 AA; 32992 MW; EA787B7E79005692 CRC64;
MFASTWQTRA VGVLIGCLLD VVFGDPKRGH PVALFGRAAA KLEQITYRDG RVAGAVHVGL
LVGAVGLLGA ALQRLPGRCW PVAATATATW AALGGTSLAR TGRQISDLLE RDDVEAARRL
LPSLCGRDPA QLGGPGLTRA ALESVAENTA DAQVVPLLWA ASSGVPAVLG YRAINTLDSM
IGYRSPRYLR FGWAAARLDD WANYVGARAT AVLVVICAPV VGGSPRGAVR AWRRDAARHP
SPNAGVVEAA FAGALDVRLG GPTRYHHELQ IRPTLGDGRS PKVADLRRAV VLSRVVQAGA
AVLAVMLVYR RRP