Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B8ZQE1 (B8ZQE1_MYCLB) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Coenzyme F420:L-glutamate ligase HAMAP-Rule MF_01259

EC=6.3.2.31 HAMAP-Rule MF_01259
EC=6.3.2.34 HAMAP-Rule MF_01259
Alternative name(s):
Coenzyme F420-0:L-glutamate ligase HAMAP-Rule MF_01259
Coenzyme F420-1:gamma-L-glutamate ligase HAMAP-Rule MF_01259
Gene names
Name:fbiB HAMAP-Rule MF_01259
Ordered Locus Names:MLBr00758 EMBL CAR70852.1
OrganismMycobacterium leprae (strain Br4923) [Complete proteome] [HAMAP] EMBL CAR70852.1
Taxonomic identifier561304 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the GTP-dependent successive addition of multiple gamma-linked L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (F420-0) to form polyglutamated F420 derivatives By similarity. HAMAP-Rule MF_01259

Catalytic activity

GTP + coenzyme F420-0 + L-glutamate = GDP + phosphate + coenzyme F420-1. HAMAP-Rule MF_01259

GTP + coenzyme F420-0 + n L-glutamate = GDP + phosphate + coenzyme gamma-F420-n. HAMAP-Rule MF_01259

GTP + coenzyme F420-1 + L-glutamate = GDP + phosphate + coenzyme gamma-F420-2. HAMAP-Rule MF_01259

Cofactor

Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese By similarity. HAMAP-Rule MF_01259

Monovalent cation. The ion could be potassium By similarity. HAMAP-Rule MF_01259

Pathway

Cofactor biosynthesis; coenzyme F420 biosynthesis. HAMAP-Rule MF_01259

Sequence similarities

In the N-terminal section; belongs to the CofE family. HAMAP-Rule MF_01259

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding29 – 324GTP By similarity HAMAP-Rule MF_01259
Region1 – 253253F420-0:gamma-glutamyl ligase By similarity HAMAP-Rule MF_01259
Region254 – 457204Unknown By similarity HAMAP-Rule MF_01259

Sites

Metal binding1181Divalent metal cation 1 By similarity HAMAP-Rule MF_01259
Metal binding1591Divalent metal cation 1 By similarity HAMAP-Rule MF_01259
Metal binding1601Divalent metal cation 2 By similarity HAMAP-Rule MF_01259
Binding site591GTP By similarity HAMAP-Rule MF_01259
Binding site641GTP By similarity HAMAP-Rule MF_01259
Binding site1211GTP By similarity HAMAP-Rule MF_01259

Sequences

Sequence LengthMass (Da)Tools
B8ZQE1 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 42BEF5D8A3333327

FASTA45748,562
        10         20         30         40         50         60 
MTSSDSHRSA PSPEHGTAST IEILPVAGLP EFRPGDDLSA ALAAAAPWLR DGDVVVVTSK 

        70         80         90        100        110        120 
VVSKCEGRLV PAPEDTRGRN ELRRKLINDE TIRVLARKGR TLIIENGLGL VQAAAGVDGS 

       130        140        150        160        170        180 
NVGRGELALL PVNPDASAAV LRIGLRAMLG VNVAVVITDT MGRAWRNGQT DVAIGAAGLA 

       190        200        210        220        230        240 
VLHNYSGAVD RYGNELVVTE IAVADEVAAA TDLVKGKLTA MPVAVVRGLS PTDDGSTAQH 

       250        260        270        280        290        300 
LLRNGPDDLF WLGTTEALEL GRQQAQLLRR SVRQFSDEPI AAELIETAVA EALTAPAPHH 

       310        320        330        340        350        360 
TRPVRFVWLQ TPAVRTRLLD RMADKWRLDL ASDALPADAI AQRVARGQIL YDAPEVIIPF 

       370        380        390        400        410        420 
MVPDGAHAYP DAARASAEHT MFIVAVGAAV QALLVALAVR GLGSCWIGST IFADDLVRAE 

       430        440        450 
LELPADWEPL GAIAIGYAHE PTDLREPVRV ADLLLRK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM211192 Genomic DNA. Translation: CAR70852.1.
RefSeqYP_002503218.1. NC_011896.1.

3D structure databases

ProteinModelPortalB8ZQE1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561304.MLBr_00758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR70852; CAR70852; MLBr00758.
GeneID7326230.
KEGGmlb:MLBr_00758.
PATRIC18042282. VBIMycLep121698_1372.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1478.
KOK12234.
OMAGEEDLFW.
OrthoDBEOG6P8TS8.
ProtClustDBPRK13294.

Enzyme and pathway databases

BioCycMLEP561304:GJP6-773-MONOMER.
UniPathwayUPA00071.

Family and domain databases

Gene3D3.40.109.10. 1 hit.
HAMAPMF_01259. F420_ligase_FbiB.
InterProIPR002847. F420-0_gamma-glut_ligase-dom.
IPR008225. F420-0_gamma-glutamyl_ligase.
IPR019943. F420_FbiB_C.
IPR023661. F420_gamma-glut_ligase_bact.
IPR000415. Nitroreductase-like.
[Graphical view]
PfamPF01996. F420_ligase. 1 hit.
PF00881. Nitroreductase. 1 hit.
[Graphical view]
SUPFAMSSF55469. SSF55469. 1 hit.
TIGRFAMsTIGR01916. F420_cofE. 1 hit.
TIGR03553. F420_FbiB_CTERM. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB8ZQE1_MYCLB
AccessionPrimary (citable) accession number: B8ZQE1
Entry history
Integrated into UniProtKB/TrEMBL: March 3, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)