COFC_METJA
ID COFC_METJA Reviewed; 224 AA.
AC Q58297;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=2-phospho-L-lactate guanylyltransferase {ECO:0000303|PubMed:18260642};
DE Short=LP guanylyltransferase;
DE EC=2.7.7.68 {ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:31469543};
GN Name=cofC; OrderedLocusNames=MJ0887;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ROLE IN F420
RP BIOSYNTHESIS, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=18260642; DOI=10.1021/bi702475t;
RA Grochowski L.L., Xu H., White R.H.;
RT "Identification and characterization of the 2-phospho-L-lactate
RT guanylyltransferase involved in coenzyme F420 biosynthesis.";
RL Biochemistry 47:3033-3037(2008).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=31469543; DOI=10.1021/acschembio.9b00605;
RA Braga D., Last D., Hasan M., Guo H., Leichnitz D., Uzum Z., Richter I.,
RA Schalk F., Beemelmanns C., Hertweck C., Lackner G.;
RT "Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-
RT overlooked derivatives of coenzyme F420.";
RL ACS Chem. Biol. 14:2088-2094(2019).
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 (PubMed:18260642,
CC PubMed:31469543). Is able to utilize other purine nucleotides including
CC ATP, dGTP and ITP as cosubstrates in place of GTP but with a lower
CC activity. Does not display lactate kinase activity (PubMed:18260642).
CC {ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:31469543}.
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;
CC Evidence={ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:31469543};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for (2S)-2-phospholactate {ECO:0000269|PubMed:18260642};
CC KM=56 uM for GTP {ECO:0000269|PubMed:18260642};
CC Vmax=3 umol/min/mg enzyme {ECO:0000269|PubMed:18260642};
CC Temperature dependence:
CC Retains all activity when heated up to 90 degrees Celsius for 10
CC minutes and retained 38% activity after 10 minutes at 100 degrees
CC Celsius. {ECO:0000269|PubMed:18260642};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18260642}.
CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000305}.
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DR EMBL; L77117; AAB98891.1; -; Genomic_DNA.
DR PIR; G64410; G64410.
DR AlphaFoldDB; Q58297; -.
DR SMR; Q58297; -.
DR STRING; 243232.MJ_0887; -.
DR EnsemblBacteria; AAB98891; AAB98891; MJ_0887.
DR KEGG; mja:MJ_0887; -.
DR eggNOG; arCOG04472; Archaea.
DR HOGENOM; CLU_076569_2_0_2; -.
DR InParanoid; Q58297; -.
DR OMA; FRVDYHG; -.
DR PhylomeDB; Q58297; -.
DR BioCyc; MetaCyc:MON-14615; -.
DR BRENDA; 2.7.7.105; 3260.
DR BRENDA; 2.7.7.68; 3260.
DR SABIO-RK; Q58297; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0043814; F:phospholactate guanylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052645; P:F420-0 metabolic process; IDA:UniProtKB.
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 GTP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..224
FT /note="2-phospho-L-lactate guanylyltransferase"
FT /id="PRO_0000107091"
SQ SEQUENCE 224 AA; 25683 MW; 0565EDD51F313278 CRC64;
MNCGIKMKVI IPVSPINSLK TRLSEFLSGE ERKNLLLNML KDIIKALDGL DIVIVSRDEE
ILDFAKNELK AETIKEKYKG LNNAIKQAFE EIEDKEVIII PADIPLIKKK HIEDILKLSK
NYDLIIAPSR GGGTNLLYLK SKDLIEIKYE GFSFLKHLEE AKKRNLRYYI YDSFLISVDI
NTPEDLGEIF IHGNDTYTKN YLKSLGIDVE PKHSSAGRFV VKRR
