(data stored in SCRATCH zone)

SWISSPROT: D5E9J4_METMS

ID   D5E9J4_METMS            Unreviewed;       275 AA.
AC   D5E9J4;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 57.
DE   RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000256|HAMAP-Rule:MF_00719};
DE            EC=2.7.8.26 {ECO:0000256|HAMAP-Rule:MF_00719};
DE   AltName: Full=Cobalamin synthase {ECO:0000256|HAMAP-Rule:MF_00719};
DE   AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00719};
GN   Name=cobS {ECO:0000256|HAMAP-Rule:MF_00719};
GN   OrderedLocusNames=Mmah_0313 {ECO:0000313|EMBL:ADE35845.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35845.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35845.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate
CC       adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin
CC       5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00719}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate =
CC         adenosylcob(III)alamin 5'-phosphate + GMP + H(+);
CC         Xref=Rhea:RHEA:23560, ChEBI:CHEBI:15378, ChEBI:CHEBI:57918,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:60487, ChEBI:CHEBI:60493; EC=2.7.8.26;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00719};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosylcob(III)inamide-GDP + alpha-ribazole =
CC         adenosylcob(III)alamin + GMP + H(+); Xref=Rhea:RHEA:16049,
CC         ChEBI:CHEBI:10329, ChEBI:CHEBI:15378, ChEBI:CHEBI:18408,
CC         ChEBI:CHEBI:58115, ChEBI:CHEBI:60487; EC=2.7.8.26;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00719};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00719};
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
CC       {ECO:0000256|HAMAP-Rule:MF_00719}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00719};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00719}.
CC   -!- SIMILARITY: Belongs to the CobS family. {ECO:0000256|HAMAP-
CC       Rule:MF_00719}.
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DR   EMBL; CP001994; ADE35845.1; -; Genomic_DNA.
DR   RefSeq; WP_013036788.1; NC_014002.1.
DR   EnsemblBacteria; ADE35845; ADE35845; Mmah_0313.
DR   GeneID; 8982446; -.
DR   KEGG; mmh:Mmah_0313; -.
DR   eggNOG; arCOG04338; Archaea.
DR   eggNOG; COG0368; LUCA.
DR   HOGENOM; HOG000228087; -.
DR   KO; K02233; -.
DR   OMA; CACCGIP; -.
DR   OrthoDB; 108934at2157; -.
DR   BioCyc; MMAH547558:G1GHT-309-MONOMER; -.
DR   UniPathway; UPA00148; UER00238.
DR   Proteomes; UP000001059; 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:0051073; F:adenosylcobinamide-GDP ribazoletransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00719; CobS; 1.
DR   InterPro; IPR003805; CobS.
DR   PANTHER; PTHR34148; PTHR34148; 1.
DR   Pfam; PF02654; CobS; 1.
DR   TIGRFAMs; TIGR00317; cobS; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9J4.
DR   SWISS-2DPAGE; D5E9J4.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00719};
KW   Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00719};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00719};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00719, ECO:0000313|EMBL:ADE35845.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00719};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00719}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00719"
FT   TRANSMEM        34..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00719"
FT   TRANSMEM        57..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00719"
FT   TRANSMEM        109..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00719"
FT   TRANSMEM        192..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00719"
FT   TRANSMEM        253..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00719"
SQ   SEQUENCE   275 AA;  28578 MW;  D1A285E9812470F4 CRC64;
     MSGLLLAVRT GFGFLSTIPV GITMEGLDEL VKRSYLFVFT GIVLGLLIGM FTGIVEYVFP
     ANISAALVIV FIYYLTGLNH LDGLADFGDG CTAHGSLEKK IKALKDMSLG IGGVAYCVIG
     LILLYASISS LQQQIYITGT ISSLPQWTLL PLSLLVAEIG AKQGMLTIAA FGKSIHEGLG
     SMVIDKTDVG KYLAGLAMGG VVSVLSLGLI GLIGFVAAIL GAFGVLNVSN RHFGGVNGDC
     IGTANEIARL TSLIAITLAL IAINAGYGGL SWMLL
//

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