ID   COFC_NATMM              Reviewed;         236 AA.
AC   D3SYZ8;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   25-MAY-2022, entry version 49.
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=Nmag_2631;
OS   Natrialba magadii (strain ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 /
OS   IAM 13178 / JCM 8861 / NBRC 102185 / NCIMB 2190 / MS3) (Natronobacterium
OS   magadii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrialba.
OX   NCBI_TaxID=547559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43099 / DSM 3394 / CCM 3739 / CIP 104546 / IAM 13178 / JCM 8861
RC   / NBRC 102185 / NCIMB 2190 / MS3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Saunders E., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., De Castro R.E.,
RA   Maupin-Furlow J.A., Woyke T.;
RT   "Complete sequence of chromosome of Natrialba magadii ATCC 43099.";
RL   Submitted (FEB-2010) 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: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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADD06190.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001932; ADD06190.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004215145.1; NZ_AOHS01000029.1.
DR   AlphaFoldDB; D3SYZ8; -.
DR   SMR; D3SYZ8; -.
DR   STRING; 547559.Nmag_2631; -.
DR   EnsemblBacteria; ADD06190; ADD06190; Nmag_2631.
DR   GeneID; 8825486; -.
DR   KEGG; nmg:Nmag_2631; -.
DR   eggNOG; arCOG04472; Archaea.
DR   HOGENOM; CLU_076569_2_0_2; -.
DR   OrthoDB; 67356at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001879; 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; 2.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR03552; F420_cofC; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..236
FT                   /note="2-phospho-L-lactate guanylyltransferase"
FT                   /id="PRO_0000398761"
SQ   SEQUENCE   236 AA;  24520 MW;  203C5436A0726C36 CRC64;
     MHVVVPFAAD TPKTRLSEVL SPPERTALAR AMLADVLSAI TATGHVPTVL STSPLSLENG
     CSCDDLPSTT PPGLESASDI PVTVDDRPLT AAVNAQLEAA EEPVAIVMAD LALATPAALS
     TLFASGAADG VAIAPGRGGG TNALVVRHPD FRVDYHGASY LDHREHAAEI GAPLESVDSF
     RLGTDVDEPA DLVEVLIHGR ETAADGGESR TATRLRELGF ELETTDGRVT VARDRS