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Database: UniProt
Entry: E3GW69_METFV
LinkDB: E3GW69_METFV
Original site: E3GW69_METFV 
ID   E3GW69_METFV            Unreviewed;       223 AA.
AC   E3GW69;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=2-phospho-L-lactate guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE            Short=LP guanylyltransferase {ECO:0000256|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.68 {ECO:0000256|HAMAP-Rule:MF_02114};
GN   Name=cofC {ECO:0000256|HAMAP-Rule:MF_02114};
GN   OrderedLocusNames=Mfer_1039 {ECO:0000313|EMBL:ADP77834.1};
OS   Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP77834.1, ECO:0000313|Proteomes:UP000002315};
RN   [1] {ECO:0000313|EMBL:ADP77834.1, ECO:0000313|Proteomes:UP000002315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC   {ECO:0000313|Proteomes:UP000002315};
RX   PubMed=21304736;
RA   Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA   Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA   Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL   Stand. Genomic Sci. 3:315-324(2010).
CC   -!- FUNCTION: Guanylyltransferase that catalyzes the activation of (2S)-2-
CC       phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the
CC       condensation of 2-PL with GTP. It is involved in the biosynthesis of
CC       coenzyme F420, a hydride carrier cofactor. {ECO:0000256|HAMAP-
CC       Rule:MF_02114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-phospholactate + GTP + H(+) = (2S)-lactyl-2-diphospho-
CC         5'-guanosine + diphosphate; Xref=Rhea:RHEA:63424, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:59435,
CC         ChEBI:CHEBI:59906; EC=2.7.7.68; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02114};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_02114}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02114}.
CC   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000256|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; CP002278; ADP77834.1; -; Genomic_DNA.
DR   RefSeq; WP_013414112.1; NC_014658.1.
DR   AlphaFoldDB; E3GW69; -.
DR   STRING; 523846.Mfer_1039; -.
DR   GeneID; 9962780; -.
DR   KEGG; mfv:Mfer_1039; -.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   OMA; FRVDYHG; -.
DR   OrthoDB; 11179at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000002315; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043814; F:phospholactate guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 6.10.140.50; -; 1.
DR   HAMAP; MF_02114; CofC; 1.
DR   InterPro; IPR002835; CofC.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   NCBIfam; TIGR03552; F420_cofC; 1.
DR   PANTHER; PTHR40392; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR   PANTHER; PTHR40392:SF1; 2-PHOSPHO-L-LACTATE GUANYLYLTRANSFERASE; 1.
DR   Pfam; PF01983; CofC; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02114};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_02114,
KW   ECO:0000313|EMBL:ADP77834.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002315};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:ADP77834.1}.
SQ   SEQUENCE   223 AA;  25384 MW;  8CA18F9DDEB67395 CRC64;
     MRTCSMIPVS ELPRAKTRLS TILSTAEREN LLKAMIRDVT SALNNFVDEI VIVSSDENIL
     EFGYEIGVEI FEESEIIELN GALEKAIDEY RDFDKVLIIP ADVPLVLKCD IHTLINKGKE
     YDIVIAPSKG GGTNALLLEP KAIPLRFGEL SFFKHIEEAK KRNLSFYVYD SFYLSVDVNT
     KEDLGEILLH GRGTSTYKYL KKLGFSVKPW HGNIRLKVER EKW
//
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