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G0THN8 (G0THN8_MYCCP) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
2-phospho-L-lactate transferase HAMAP-Rule MF_01257

EC=2.7.8.28 HAMAP-Rule MF_01257
Alternative name(s):
LPPG:FO 2-phospho-L-lactate transferase HAMAP-Rule MF_01257
Gene names
Name:fbiA EMBL CCC45611.1
Synonyms:cofD HAMAP-Rule MF_01257
Ordered Locus Names:MCAN_32801 EMBL CCC45611.1
OrganismMycobacterium canettii (strain CIPT 140010059) [Complete proteome] [HAMAP] EMBL CCC45611.1
Taxonomic identifier1048245 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of the 2-phospholactate moiety from lactyl (2) diphospho-(5')guanosine (LPPG) to 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) with the formation of the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) and GMP By similarity. HAMAP-Rule MF_01257

Catalytic activity

(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = guanosine 5'-phosphate + coenzyme F420-0. HAMAP-Rule MF_01257

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01257

Pathway

Cofactor biosynthesis; coenzyme F420 biosynthesis. HAMAP-Rule MF_01257

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01257

Sequence similarities

Belongs to the CofD family. HAMAP-Rule MF_01257

Sequences

Sequence LengthMass (Da)Tools
G0THN8 [UniParc].

Last modified October 19, 2011. Version 1.
Checksum: 4D144F9A17F792C6

FASTA33135,335
        10         20         30         40         50         60 
MKVTVLAGGV GGARFLLGVQ QLLGLGQFAA NSAHSDADHQ LSAVVNVGDD AWIHGLRVCP 

        70         80         90        100        110        120 
DLDTCMYTLG GGVDPQRGWG QRDETWHAMQ ELVRYGVQPD WFELGDRDLA THLVRTQMLQ 

       130        140        150        160        170        180 
AGYPLSQITE ALCDRWQPGA RLLPATDDRC ETHVVITDPV DESRKAIHFQ EWWVRYRAQV 

       190        200        210        220        230        240 
PTHSFAFVGA EKSSAATEAI AALADADIIM LAPSNPVVSI GAILAVPGIR AALREATAPI 

       250        260        270        280        290        300 
VGYSPIIGEK PLRGMADTCL SVIGVDSTAA AVGRHYGARC ATGILDCWLV HDGDHAEIDG 

       310        320        330 
VTVRSVPLLM TDPNATAEMV RAGCDLAGVV A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HE572590 Genomic DNA. Translation: CCC45611.1.
RefSeqYP_004746691.1. NC_015848.1.

3D structure databases

ProteinModelPortalG0THN8.
SMRG0THN8. Positions 3-328.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC45611; CCC45611; MCAN_32801.
GeneID10987268.
KEGGmce:MCAN_32801.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK11212.
OMAHFQEYWV.

Enzyme and pathway databases

BioCycMCAN1048245:GJCJ-3313-MONOMER.
UniPathwayUPA00071.

Family and domain databases

HAMAPMF_01257. CofD.
InterProIPR002882. CofD/UPF0052.
IPR010115. LPPG-Fo_P-lactate_Trfase.
[Graphical view]
PfamPF01933. UPF0052. 1 hit.
[Graphical view]
TIGRFAMsTIGR01819. F420_cofD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameG0THN8_MYCCP
AccessionPrimary (citable) accession number: G0THN8
Entry history
Integrated into UniProtKB/TrEMBL: October 19, 2011
Last sequence update: October 19, 2011
Last modified: February 19, 2014
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)