COFC_METMA
ID COFC_METMA Reviewed; 208 AA.
AC Q8PU52;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=MM_2497;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "The crystal structure of a hypothetical protein MM_2497 from
RT Methanosarcina mazei Go1.";
RL Submitted (FEB-2009) to the PDB data bank.
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:0000305|Ref.2}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000255|HAMAP-
CC Rule:MF_02114}.
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DR EMBL; AE008384; AAM32193.1; -; Genomic_DNA.
DR RefSeq; WP_011034415.1; NC_003901.1.
DR PDB; 2I5E; X-ray; 2.10 A; A/B=1-208.
DR PDBsum; 2I5E; -.
DR AlphaFoldDB; Q8PU52; -.
DR SMR; Q8PU52; -.
DR STRING; 192952.MM_2497; -.
DR EnsemblBacteria; AAM32193; AAM32193; MM_2497.
DR GeneID; 44087889; -.
DR GeneID; 66135458; -.
DR KEGG; mma:MM_2497; -.
DR PATRIC; fig|192952.21.peg.2858; -.
DR eggNOG; arCOG04472; Archaea.
DR HOGENOM; CLU_076569_2_0_2; -.
DR OMA; FRVDYHG; -.
DR UniPathway; UPA00071; -.
DR EvolutionaryTrace; Q8PU52; -.
DR Proteomes; UP000000595; 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 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..208
FT /note="2-phospho-L-lactate guanylyltransferase"
FT /id="PRO_0000398757"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2I5E"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:2I5E"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 22..42
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:2I5E"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2I5E"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:2I5E"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2I5E"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:2I5E"
SQ SEQUENCE 208 AA; 23051 MW; FBD850747C2D769B CRC64;
MRAVIPYKKA GAKSRLSPVL SLQEREEFVE LMLNQVISSL KGAGIEQVDI LSPSVYGLEE
MTEARVLLDE KDLNEALNRY LKEAEEPVLI VMADLPLLSP EHIKEISSTE KDVCIVPGKG
GGTNALFIKN PSKYRVKYYG SSFLTHCSIA TDSGQDFEIY DSFMAGTDID EPEDLVELLI
HGKGAAKDYI ESKFRLEVKK GRVGLVPL
