COBD_AERPE
ID COBD_AERPE Reviewed; 320 AA.
AC Q9YAA0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Probable cobalamin biosynthesis protein CobD;
GN Name=cobD; OrderedLocusNames=APE_2039.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA81049.2; -; Genomic_DNA.
DR PIR; A72508; A72508.
DR AlphaFoldDB; Q9YAA0; -.
DR STRING; 272557.APE_2039.1; -.
DR EnsemblBacteria; BAA81049; BAA81049; APE_2039.1.
DR KEGG; ape:APE_2039.1; -.
DR PATRIC; fig|272557.25.peg.1356; -.
DR eggNOG; arCOG04274; Archaea.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002518; 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.
PE 3: Inferred from homology;
KW Cell membrane; Cobalamin biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..320
FT /note="Probable cobalamin biosynthesis protein CobD"
FT /id="PRO_0000150939"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 320 AA; 33894 MW; 3EABCFA78536610A CRC64;
MFEWLARALY PEPEVLAAGL AVGLMLDLAY PEHRGLALKL HPVHTSYIMA LRLVRPGAGR
AWGAAIWLLT ISSHMMVYAS LLAASYLVHP ALHTLAVGVI VKLSMPLRLL LDTCIKASRM
AAAGRVECSR RLVQGIVRRD LSGEPLGRVL SACIESTAES LVDGYTSPLT YYILLGPLGA
LLQRLSNTLD GAVGFKTPLL YRQGWFSAKA DTLLNFIPAR LTAVMVALAA PLAGASTLGS
LRCIARCARL LESVNAGYPI SAFAGALDVR LEKKGFYIVN GGAPYPGWRD GLKASRLAVS
AASLYTVLAA LAIALGGGAG