COBD_PYRFU
ID COBD_PYRFU Reviewed; 285 AA.
AC Q8U403;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Probable cobalamin biosynthesis protein CobD {ECO:0000255|HAMAP-Rule:MF_00024};
GN Name=cobD {ECO:0000255|HAMAP-Rule:MF_00024}; OrderedLocusNames=PF0296;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
CC -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC aminopropanol on the F carboxylic group. {ECO:0000255|HAMAP-
CC 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; AE009950; AAL80420.1; -; Genomic_DNA.
DR RefSeq; WP_011011410.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U403; -.
DR STRING; 186497.PF0296; -.
DR EnsemblBacteria; AAL80420; AAL80420; PF0296.
DR GeneID; 41712086; -.
DR KEGG; pfu:PF0296; -.
DR PATRIC; fig|186497.12.peg.308; -.
DR eggNOG; arCOG04274; Archaea.
DR HOGENOM; CLU_054212_0_2_2; -.
DR OMA; NSGYTMA; -.
DR OrthoDB; 101304at2157; -.
DR PhylomeDB; Q8U403; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001013; 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..285
FT /note="Probable cobalamin biosynthesis protein CobD"
FT /id="PRO_0000150944"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 145..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
FT TRANSMEM 266..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00024"
SQ SEQUENCE 285 AA; 32452 MW; CD0DE676909F8640 CRC64;
MDMTLPIALL IDLMFGEPPA IIHPVVGFGK VIEFFDNKYR RRSPYLDFLV GAISSLVVIG
LAFILSHLPN FLPNPFNLIL SIYLLKSSFA IRSLHDHVKR TITPDLEEKR RAVSMIVSRD
TKSLDEPHLN SAAIESLSEN INDSVIAPLF YYLIFGLPGA VVYRAVNTLD AMIGYRNEKY
EYFGKFAARL DDLLNFVPAR ITVLLFLSLG GRKVIRYYRM AKYKINSDKP IAAMSAVLGV
WLEKPNYYKF PGRRPENEDI KRALKVYWII VVEFLLIVAI ILYGG
