ID E4NN10_HALBP Unreviewed; 207 AA.
AC E4NN10;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=Hbor_06400 {ECO:0000313|EMBL:ADQ66240.1};
GN ORFNames=C499_09384 {ECO:0000313|EMBL:ELY27264.1};
OS Halogeometricum borinquense (strain ATCC 700274 / DSM 11551 / JCM 10706 /
OS KCTC 4070 / PR3).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halogeometricum.
OX NCBI_TaxID=469382 {ECO:0000313|EMBL:ADQ66240.1, ECO:0000313|Proteomes:UP000006663};
RN [1] {ECO:0000313|EMBL:ADQ66240.1, ECO:0000313|Proteomes:UP000006663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700274 / DSM 11551 / JCM 10706 / KCTC 4070 / PR3
RC {ECO:0000313|Proteomes:UP000006663}, and PR 3
RC {ECO:0000313|EMBL:ADQ66240.1};
RX PubMed=21304651; DOI=10.4056/sigs.23264;
RA Malfatti S., Tindall B.J., Schneider S., Fahnrich R., Lapidus A.,
RA Labuttii K., Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Anderson I.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Halogeometricum borinquense type strain
RT (PR3).";
RL Stand. Genomic Sci. 1:150-159(2009).
RN [2] {ECO:0000313|EMBL:ELY27264.1, ECO:0000313|Proteomes:UP000011585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11551 {ECO:0000313|EMBL:ELY27264.1,
RC ECO:0000313|Proteomes:UP000011585};
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).
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; CP001690; ADQ66240.1; -; Genomic_DNA.
DR EMBL; AOHT01000033; ELY27264.1; -; Genomic_DNA.
DR RefSeq; WP_006055193.1; NZ_AOHT01000033.1.
DR AlphaFoldDB; E4NN10; -.
DR STRING; 469382.Hbor_06400; -.
DR GeneID; 9992460; -.
DR KEGG; hbo:Hbor_06400; -.
DR PATRIC; fig|469382.19.peg.1842; -.
DR eggNOG; arCOG04472; Archaea.
DR HOGENOM; CLU_076569_2_0_2; -.
DR OMA; FRVDYHG; -.
DR OrthoDB; 11179at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000006663; Chromosome.
DR Proteomes; UP000011585; 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:ADQ66240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006663};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02114, ECO:0000313|EMBL:ADQ66240.1}.
SQ SEQUENCE 207 AA; 22033 MW; A1A160967CAAF11F CRC64;
MQVVIPYTTR DPKSRLAGVL DEDERRAFAR AMRTDVVRAV RAAGGAPTIL TTDADDIDDV
DAPVIGDDRA LTPAVNAVLD DATSDVSVVM ADLALVTPDA LRRLFESEGE VVIAPGRGGG
TNALVVRHPD FRVDYHGASY RDHQAIADDA GLSVTVIDSM RLATDVDEPA DLAEVLLHGA
GNARTWLEDA GFELEVTDGR VGVTRSD
//