COFD_NATPD
ID COFD_NATPD Reviewed; 334 AA.
AC Q3IRY6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=NP_2028A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49105.1; -; Genomic_DNA.
DR RefSeq; WP_011322734.1; NC_007426.1.
DR AlphaFoldDB; Q3IRY6; -.
DR SMR; Q3IRY6; -.
DR STRING; 348780.NP_2028A; -.
DR EnsemblBacteria; CAI49105; CAI49105; NP_2028A.
DR GeneID; 3701331; -.
DR KEGG; nph:NP_2028A; -.
DR eggNOG; arCOG04395; Archaea.
DR HOGENOM; CLU_055795_1_0_2; -.
DR OMA; DLDTVMY; -.
DR OrthoDB; 31831at2157; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000002698; 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; -; 2.
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..334
FT /note="2-phospho-L-lactate transferase"
FT /id="PRO_0000259480"
FT BINDING 49
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 334 AA; 35792 MW; E62B29A122C81042 CRC64;
MVTFLAGGTG TPKLRYGAET VFDTADTPVV CNTGDDVELG GLVVCPDVDT VLFAAADRLD
RETWWGIDGD TTETHEELRA LADAADLDTG PRYLPDKKQT AGRDIARWRR FSGVAEFMEI
GDTDRAVHIT RTSLLDEGKR LTEATATLAD ALGVDHPVLP MSDDPVATLI DTDEGLVHFQ
EFWVHRRAEP TINGVEFRGA DAAEPTPEVR EALADPVVIG PSNPITSIGP MVALDGIRKA
LAETPVVAVS PFVEDRVFSG PADDLMAADG YAPSTAGVAE AYPFADAFVV DEADETPLER
PTVRTDTELG SPADGERVCR AVREAFDRLG VEVA
