ID   COFC_HALUD              Reviewed;         202 AA.
AC   C7NN78;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=2-phospho-L-lactate guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            Short=LP guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_02114};
DE            EC=2.7.7.68 {ECO:0000255|HAMAP-Rule:MF_02114};
GN   Name=cofC {ECO:0000255|HAMAP-Rule:MF_02114}; OrderedLocusNames=Huta_1302;
OS   Halorhabdus utahensis (strain DSM 12940 / JCM 11049 / AX-2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=519442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12940 / JCM 11049 / AX-2;
RX   PubMed=21304660; DOI=10.4056/sigs.31864;
RA   Anderson I., Tindall B.J., Pomrenke H., Goker M., Lapidus A., Nolan M.,
RA   Copeland A., Glavina Del Rio T., Chen F., Tice H., Cheng J.F., Lucas S.,
RA   Chertkov O., Bruce D., Brettin T., Detter J.C., Han C., Goodwin L.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Pitluck S., Pati A.,
RA   Mavromatis K., Ivanova N., Ovchinnikova G., Chen A., Palaniappan K.,
RA   Chain P., Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Halorhabdus utahensis type strain (AX-2).";
RL   Stand. Genomic Sci. 1:218-225(2009).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_02114};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02114}.
CC   -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC       Rule:MF_02114}.
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DR   EMBL; CP001687; ACV11478.1; -; Genomic_DNA.
DR   RefSeq; WP_015789052.1; NC_013158.1.
DR   AlphaFoldDB; C7NN78; -.
DR   SMR; C7NN78; -.
DR   STRING; 519442.Huta_1302; -.
DR   EnsemblBacteria; ACV11478; ACV11478; Huta_1302.
DR   GeneID; 8383579; -.
DR   KEGG; hut:Huta_1302; -.
DR   eggNOG; arCOG04472; Archaea.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   OMA; FRVDYHG; -.
DR   OrthoDB; 67356at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000002071; 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; 3.90.550.10; -; 1.
DR   HAMAP; MF_02114; CofC; 1.
DR   InterPro; IPR002835; CofC.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR40392; PTHR40392; 1.
DR   Pfam; PF01983; CofC; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03552; F420_cofC; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..202
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398731"
SQ   SEQUENCE   202 AA;  21936 MW;  27D29491B767B965 CRC64;
     MHVVVPFDGR DPKTRLAPVL DAPERRDFAR AMLADVAETI ESISFEPTIL ATTDVECEWP
     VVVDERSLDA AVNDQLAVAD GPVAVVMADL ALVTPDALDR LFRAGGEVVL APGRGGGTNA
     FVARHHDFRV DYHDASITDH RSIAEEIGAD TVEVDSFRLA SDVDEPDDLA EVLLHGEGRA
     AAWLREHGFD LSMDEGRVSV QR