COFD_METAC
ID COFD_METAC Reviewed; 307 AA.
AC Q8TST1;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=2-phospho-L-lactate transferase {ECO:0000255|HAMAP-Rule:MF_01257};
DE EC=2.7.8.28 {ECO:0000255|HAMAP-Rule:MF_01257};
GN Name=cofD {ECO:0000255|HAMAP-Rule:MF_01257}; OrderedLocusNames=MA_0714;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM04154.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE010299; AAM04154.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048066127.1; NC_003552.1.
DR AlphaFoldDB; Q8TST1; -.
DR SMR; Q8TST1; -.
DR STRING; 188937.MA_0714; -.
DR EnsemblBacteria; AAM04154; AAM04154; MA_0714.
DR GeneID; 1472606; -.
DR KEGG; mac:MA_0714; -.
DR HOGENOM; CLU_055795_1_0_2; -.
DR InParanoid; Q8TST1; -.
DR OMA; DLDTVMY; -.
DR OrthoDB; 31831at2157; -.
DR PhylomeDB; Q8TST1; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IBA:GO_Central.
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 3: Inferred from homology;
KW Magnesium; Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_0000145771"
FT BINDING 48
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
FT BINDING 87
FT /ligand="7,8-didemethyl-8-hydroxy-5-deazariboflavin"
FT /ligand_id="ChEBI:CHEBI:59904"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01257"
SQ SEQUENCE 307 AA; 33816 MW; 3B20A9FC13A1BB14 CRC64;
MIILSGGTGT PKLLDGLKEI LPLEELTVVV NTAEDLWVSG NLISPDLDTV LYLFSDQIDR
KKWWGIENDT FRTYERMHEL GIEESMKLGD RDRATHIIRS NLIRGGTSLT EATVKLASLF
GIDANILPMS DDPVSTYVET LQGVMHFQDF WVGKHGDPDV LGVDIRGVSE ASVAKKVLEA
FEKDDNVLIG PSNPITSIGP IISLPGMREL LKRKKVIAVS PIIGNAPVSG PAGKLMQACG
LEVSSMGVAE YYQEFLDVFV FDERDRADEF AFERLGCRAS RADTLMTSTE KSRELAEFVV
GLFDTVC