COBD_PYRHO
ID COBD_PYRHO Reviewed; 283 AA.
AC O58114;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Probable cobalamin biosynthesis protein CobD;
GN Name=cobD; OrderedLocusNames=PH0376;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29450.1; -; Genomic_DNA.
DR PIR; E71145; E71145.
DR RefSeq; WP_010884464.1; NC_000961.1.
DR AlphaFoldDB; O58114; -.
DR STRING; 70601.3256767; -.
DR PRIDE; O58114; -.
DR EnsemblBacteria; BAA29450; BAA29450; BAA29450.
DR GeneID; 1444251; -.
DR KEGG; pho:PH0376; -.
DR eggNOG; arCOG04274; Archaea.
DR OMA; NSGYTMA; -.
DR OrthoDB; 101304at2157; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000000752; 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..283
FT /note="Probable cobalamin biosynthesis protein CobD"
FT /id="PRO_0000150945"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 283 AA; 32421 MW; 974A1CFCFE6D44EA CRC64;
MYELILALGW DLLLGEPPAV VHPVVWFGKL IAFIDSHYSR RSPAIDFLAG LFATLVVLSF
AFLLSILPLY APYPLNYLLS VYLLKSSFAI RSLYEHVRRT MKDDVEEMRK EVSMIVSRDT
SKLGREHLIS ASIESLAENT NDSVVAPLFY YLLFGLPGAL VYRAVNTLDA MVGYRTSRYE
YFGKFSARLD DILNFLPARI TVLLFLPLNP RRVIRYYKMA RFKVNSDKPI AAMSAVLGIW
LEKPNIYRFP GRDPRMEDIE RALKVYVIVV SEWILLLLLG VIL
