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Database: UniProt
Entry: L0AEL9_NATGS
LinkDB: L0AEL9_NATGS
Original site: L0AEL9_NATGS 
ID   L0AEL9_NATGS            Unreviewed;       225 AA.
AC   L0AEL9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 68.
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   ECO:0000313|EMBL:PLK20332.1};
GN   OrderedLocusNames=Natgr_1126 {ECO:0000313|EMBL:AFZ72353.1};
GN   ORFNames=C490_14775 {ECO:0000313|EMBL:ELY64262.1}, CYV19_10235
GN   {ECO:0000313|EMBL:PLK20332.1};
OS   Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 / CIP
OS   104747 / IAM 13177 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronobacterium.
OX   NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ72353.1, ECO:0000313|Proteomes:UP000010468};
RN   [1] {ECO:0000313|Proteomes:UP000010468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC   {ECO:0000313|Proteomes:UP000010468};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFZ72353.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SP2 {ECO:0000313|EMBL:AFZ72353.1};
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., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ELY64262.1, ECO:0000313|Proteomes:UP000011613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:ELY64262.1,
RC   ECO:0000313|Proteomes:UP000011613};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
RN   [4] {ECO:0000313|EMBL:PLK20332.1, ECO:0000313|Proteomes:UP000234484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|EMBL:PLK20332.1,
RC   ECO:0000313|Proteomes:UP000234484};
RC   TISSUE=Freeze-dried powder thallus {ECO:0000313|EMBL:PLK20332.1};
RA   Jiang L., He B., Kang J., Yu M., Li N., Fang Y., Tang Z., Wu P., Yao P.,
RA   Huang J.;
RT   "The characterization of oligonucleotides binding to NgAgo.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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; CP003377; AFZ72353.1; -; Genomic_DNA.
DR   EMBL; AOIC01000109; ELY64262.1; -; Genomic_DNA.
DR   EMBL; PKKI01000028; PLK20332.1; -; Genomic_DNA.
DR   RefSeq; WP_005580680.1; NZ_PKKI01000028.1.
DR   AlphaFoldDB; L0AEL9; -.
DR   STRING; 797304.Natgr_1126; -.
DR   GeneID; 14206994; -.
DR   KEGG; nge:Natgr_1126; -.
DR   PATRIC; fig|797304.7.peg.2995; -.
DR   eggNOG; arCOG04472; Archaea.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000010468; Chromosome.
DR   Proteomes; UP000011613; Unassembled WGS sequence.
DR   Proteomes; UP000234484; Unassembled WGS sequence.
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:AFZ72353.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010468};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:ELY64262.1}.
FT   REGION          49..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   225 AA;  23859 MW;  96661D72DA40DA22 CRC64;
     MQVVVPFAAE SPKTRLESVL SFSEREALAR AMLGDVLEAI LETGHEPTVV STARLSPESE
     SDPVTGHADI GTLVDRGVTI EVDDRPLTDA VNTRLTAANG PVAVVMADLA LATPDALTKL
     FATTADVAIA PGLGGGTNAL LASHPEFRVD YHGASYLDHC RIAGEIDASL ETVDSFRLAT
     DVDEPTDLVE LLVHGSERQR ALSTLLAFGF DLETTAGRTD LRRVK
//
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