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Protein

2-phospho-L-lactate transferase

Gene

cofD

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Pathwayi: coenzyme F420 biosynthesis

This protein is involved in the pathway coenzyme F420 biosynthesis, which is part of Cofactor biosynthesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway coenzyme F420 biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMMAZ192952:GCK2-1923-MONOMER.
BRENDAi2.7.8.28. 3270.
UniPathwayiUPA00071.

Names & Taxonomyi

Protein namesi
Recommended name:
2-phospho-L-lactate transferaseUniRule annotation (EC:2.7.8.28UniRule annotation)
Alternative name(s):
LPPG:FO 2-phospho-L-lactate transferaseUniRule annotation
Gene namesi
Name:cofDUniRule annotation
Ordered Locus Names:MM_1874
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000000595 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3033032-phospho-L-lactate transferasePRO_0000145774Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi192952.MM_1874.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 54Combined sources
Helixi9 – 179Combined sources
Turni18 – 203Combined sources
Helixi23 – 253Combined sources
Beta strandi27 – 304Combined sources
Beta strandi36 – 383Combined sources
Beta strandi41 – 433Combined sources
Helixi45 – 539Combined sources
Turni54 – 563Combined sources
Turni60 – 634Combined sources
Beta strandi64 – 663Combined sources
Helixi72 – 798Combined sources
Helixi90 – 10415Combined sources
Helixi109 – 12012Combined sources
Beta strandi124 – 1296Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi144 – 1463Combined sources
Helixi147 – 1515Combined sources
Turni152 – 1565Combined sources
Beta strandi160 – 1667Combined sources
Turni167 – 1704Combined sources
Helixi175 – 1839Combined sources
Beta strandi186 – 1894Combined sources
Turni194 – 1974Combined sources
Helixi199 – 2035Combined sources
Helixi207 – 2126Combined sources
Beta strandi214 – 2196Combined sources
Beta strandi226 – 2305Combined sources
Helixi232 – 2354Combined sources
Helixi237 – 2393Combined sources
Helixi245 – 2528Combined sources
Turni253 – 2553Combined sources
Beta strandi258 – 2625Combined sources
Helixi263 – 2653Combined sources
Helixi269 – 2757Combined sources
Beta strandi278 – 2825Combined sources
Helixi289 – 30315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3DX-ray2.50A/B/C/D1-303[»]
3C3EX-ray3.00A/B/C/D1-303[»]
3CGWX-ray3.10A1-303[»]
ProteinModelPortaliQ8PVT6.
SMRiQ8PVT6. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8PVT6.

Family & Domainsi

Sequence similaritiesi

Belongs to the CofD family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04395. Archaea.
COG0391. LUCA.
HOGENOMiHOG000230060.
KOiK11212.
OMAiHFQEYWV.

Family and domain databases

HAMAPiMF_01257. CofD.
InterProiIPR002882. CofD/UPF0052.
IPR010115. P-lactate_Trfase.
[Graphical view]
PfamiPF01933. UPF0052. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01819. F420_cofD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8PVT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIFSGGTGT PKLLDGLKEI LPEEELTVVV NTAEDLWVSG NLISPDLDTV
60 70 80 90 100
LYLFSDQIDR KRWWGIENDT FGTYERMKEL GIEEGLKLGD RDRATHIIRS
110 120 130 140 150
NIIRDGASLT DSTVKLSSLF GIKANILPMS DDPVSTYIET AEGIMHFQDF
160 170 180 190 200
WIGKRGEPDV RGVDIRGVSE ASISPKVLEA FEKEENILIG PSNPITSIGP
210 220 230 240 250
IISLPGMREL LKKKKVVAVS PIIGNAPVSG PAGKLMPACG IEVSSMGVAE
260 270 280 290 300
YYQDFLDVFV FDERDRADEF AFERLGCHAS RADTLMTSTE KSKELAEIVV

QAF
Length:303
Mass (Da):33,357
Last modified:October 1, 2002 - v1
Checksum:iDBBBF4BAB5659C63
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31570.1.
RefSeqiWP_011033809.1. NC_003901.1.

Genome annotation databases

EnsemblBacteriaiAAM31570; AAM31570; MM_1874.
GeneIDi1480216.
KEGGimma:MM_1874.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008384 Genomic DNA. Translation: AAM31570.1.
RefSeqiWP_011033809.1. NC_003901.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3DX-ray2.50A/B/C/D1-303[»]
3C3EX-ray3.00A/B/C/D1-303[»]
3CGWX-ray3.10A1-303[»]
ProteinModelPortaliQ8PVT6.
SMRiQ8PVT6. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi192952.MM_1874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM31570; AAM31570; MM_1874.
GeneIDi1480216.
KEGGimma:MM_1874.

Phylogenomic databases

eggNOGiarCOG04395. Archaea.
COG0391. LUCA.
HOGENOMiHOG000230060.
KOiK11212.
OMAiHFQEYWV.

Enzyme and pathway databases

UniPathwayiUPA00071.
BioCyciMMAZ192952:GCK2-1923-MONOMER.
BRENDAi2.7.8.28. 3270.

Miscellaneous databases

EvolutionaryTraceiQ8PVT6.

Family and domain databases

HAMAPiMF_01257. CofD.
InterProiIPR002882. CofD/UPF0052.
IPR010115. P-lactate_Trfase.
[Graphical view]
PfamiPF01933. UPF0052. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01819. F420_cofD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
    Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R.
    , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
    J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88.

Entry informationi

Entry nameiCOFD_METMA
AccessioniPrimary (citable) accession number: Q8PVT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: October 1, 2002
Last modified: November 11, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.