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Database: UniProt
Entry: F8ALC2_METOI
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Original site: F8ALC2_METOI 
ID   F8ALC2_METOI            Unreviewed;       328 AA.
AC   F8ALC2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Probable cobalamin biosynthesis protein CobD {ECO:0000256|ARBA:ARBA00016185, ECO:0000256|HAMAP-Rule:MF_00024};
GN   Name=cobD {ECO:0000256|HAMAP-Rule:MF_00024};
GN   OrderedLocusNames=Metok_0530 {ECO:0000313|EMBL:AEH06510.1};
OS   Methanothermococcus okinawensis (strain DSM 14208 / JCM 11175 / IH1).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=647113 {ECO:0000313|EMBL:AEH06510.1, ECO:0000313|Proteomes:UP000009296};
RN   [1] {ECO:0000313|EMBL:AEH06510.1, ECO:0000313|Proteomes:UP000009296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14208 / JCM 11175 / IH1
RC   {ECO:0000313|Proteomes:UP000009296};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M., Takai K.,
RA   Miyazaki J., Whitman W., Woyke T.;
RT   "Complete sequence of chromosome of Methanothermococcus okinawensis IH1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEH06510.1, ECO:0000313|Proteomes:UP000009296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14208 / JCM 11175 / IH1
RC   {ECO:0000313|Proteomes:UP000009296};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M., Takai K.,
RA   Miyazaki J., Whitman W., Woyke T.;
RT   "Complete sequence of chromosome of Methanothermococcus okinawensis IH1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of
CC       aminopropanol on the F carboxylic group.
CC       {ECO:0000256|ARBA:ARBA00003384, ECO:0000256|HAMAP-Rule:MF_00024}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00024}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC       ECO:0000256|HAMAP-Rule:MF_00024}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|HAMAP-Rule:MF_00024}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CobD/CbiB family.
CC       {ECO:0000256|ARBA:ARBA00006263, ECO:0000256|HAMAP-Rule:MF_00024}.
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DR   EMBL; CP002792; AEH06510.1; -; Genomic_DNA.
DR   AlphaFoldDB; F8ALC2; -.
DR   STRING; 647113.Metok_0530; -.
DR   KEGG; mok:Metok_0530; -.
DR   eggNOG; arCOG04274; Archaea.
DR   HOGENOM; CLU_054212_0_2_2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000009296; Chromosome.
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   Gene3D; 1.10.287.70; -; 1.
DR   HAMAP; MF_00024; CobD_CbiB; 1.
DR   InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB.
DR   NCBIfam; TIGR00380; cobal_cbiB; 1.
DR   PANTHER; PTHR34308; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR   PANTHER; PTHR34308:SF1; COBALAMIN BIOSYNTHESIS PROTEIN CBIB; 1.
DR   Pfam; PF03186; CobD_Cbib; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00024};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00024};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00024}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        64..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        105..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        178..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        226..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
FT   TRANSMEM        308..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00024"
SQ   SEQUENCE   328 AA;  37135 MW;  E8C03A06DF87B035 CRC64;
     MPLENYKIRE TMINPIILIL SVLFDRVYGE LPEKIHPVVW IGNIIYFFEK LFKSSYSKNK
     IKDFVFGILI TLLVIIIVFA VVYVIEMLID NLGNILNDNN ISKSIKYILY SFLLSTTIGY
     KSLLSFSKKP IDYLKNNDLE NARTAVQCIV SRDASKLDKE HILSASIESA SENITDSIIA
     PLFYATLFGL PGAFIYRAVN TMDAMMGYRN EKYEYYGKFA ARLDDLLNFI PSRIAGLLLI
     ISAPLYGGSI KRALHGFLKE GHKTPSPNSG YTMATLSHGL NMTLEKIGYY KLGTGKINID
     KAYNSLKAID VVIVMFLIIY LIIYYSLK
//
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