COFD_METMA
ID COFD_METMA Reviewed; 303 AA.
AC Q8PVT6;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=2-phospho-L-lactate transferase {ECO:0000255|HAMAP-Rule:MF_01257, ECO:0000303|PubMed:18252724};
DE EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257};
GN Name=cofD {ECO:0000255|HAMAP-Rule:MF_01257}; OrderedLocusNames=MM_1874;
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 (2.50 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP 7,8-DIDEMETHYL-8-HYDROXY-5-DEAZARIBOFLAVIN; GDP AND PHOSPHATE.
RX PubMed=18252724; DOI=10.1074/jbc.m710352200;
RA Forouhar F., Abashidze M., Xu H., Grochowski L.L., Seetharaman J.,
RA Hussain M., Kuzin A., Chen Y., Zhou W., Xiao R., Acton T.B.,
RA Montelione G.T., Galinier A., White R.H., Tong L.;
RT "Molecular insights into the biosynthesis of the F420 coenzyme.";
RL J. Biol. Chem. 283:11832-11840(2008).
CC -!- FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety from
CC (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5-
CC deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and
CC GMP. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-
CC hydroxy-5-deazariboflavin = GMP + H(+) + oxidized coenzyme F420-0;
CC Xref=Rhea:RHEA:63444, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:59435, ChEBI:CHEBI:59904, ChEBI:CHEBI:59907; EC=2.7.8.28;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01257};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01257}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01257}.
CC -!- SIMILARITY: Belongs to the CofD family. {ECO:0000255|HAMAP-
CC Rule:MF_01257}.
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DR EMBL; AE008384; AAM31570.1; -; Genomic_DNA.
DR RefSeq; WP_011033809.1; NC_003901.1.
DR PDB; 3C3D; X-ray; 2.50 A; A/B/C/D=1-303.
DR PDB; 3C3E; X-ray; 3.00 A; A/B/C/D=1-303.
DR PDB; 3CGW; X-ray; 3.10 A; A=1-303.
DR PDBsum; 3C3D; -.
DR PDBsum; 3C3E; -.
DR PDBsum; 3CGW; -.
DR AlphaFoldDB; Q8PVT6; -.
DR SMR; Q8PVT6; -.
DR STRING; 192952.MM_1874; -.
DR EnsemblBacteria; AAM31570; AAM31570; MM_1874.
DR GeneID; 1480216; -.
DR KEGG; mma:MM_1874; -.
DR PATRIC; fig|192952.21.peg.2159; -.
DR eggNOG; arCOG04395; Archaea.
DR HOGENOM; CLU_055795_1_0_2; -.
DR OMA; DLDTVMY; -.
DR BRENDA; 2.7.8.28; 3270.
DR UniPathway; UPA00071; -.
DR EvolutionaryTrace; Q8PVT6; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07186; CofD_like; 1.
DR Gene3D; 3.40.50.10680; -; 1.
DR HAMAP; MF_01257; CofD; 1.
DR InterPro; IPR002882; CofD.
DR InterPro; IPR038136; CofD-like_dom_sf.
DR InterPro; IPR010115; FbiA/CofD.
DR PANTHER; PTHR43007; PTHR43007; 1.
DR Pfam; PF01933; CofD; 1.
DR SUPFAM; SSF142338; SSF142338; 1.
DR TIGRFAMs; TIGR01819; F420_cofD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_0000145774"
FT BINDING 48
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000269|PubMed:18252724"
FT BINDING 87
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000269|PubMed:18252724"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 152..156
FT /evidence="ECO:0007829|PDB:3C3E"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 194..197
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 207..212
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:3C3D"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 269..275
FT /evidence="ECO:0007829|PDB:3C3D"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3C3D"
FT HELIX 289..303
FT /evidence="ECO:0007829|PDB:3C3D"
SQ SEQUENCE 303 AA; 33357 MW; DBBBF4BAB5659C63 CRC64;
MIIFSGGTGT PKLLDGLKEI LPEEELTVVV NTAEDLWVSG NLISPDLDTV LYLFSDQIDR
KRWWGIENDT FGTYERMKEL GIEEGLKLGD RDRATHIIRS NIIRDGASLT DSTVKLSSLF
GIKANILPMS DDPVSTYIET AEGIMHFQDF WIGKRGEPDV RGVDIRGVSE ASISPKVLEA
FEKEENILIG PSNPITSIGP IISLPGMREL LKKKKVVAVS PIIGNAPVSG PAGKLMPACG
IEVSSMGVAE YYQDFLDVFV FDERDRADEF AFERLGCHAS RADTLMTSTE KSKELAEIVV
QAF
