Coenzyme F420:L-glutamate ligase - Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1)

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A1T5V5 (A1T5V5_MYCVP) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 44. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended 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:	Mvan_1732

Organism

Mycobacterium vanbaalenii (strain DSM 7251 / PYR-1) [Complete proteome] [HAMAP] EMBL ABM12555.1

Taxonomic identifier

350058 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium ›

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Inferred 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

Ontologies

Keywords
Ligand	GTP-binding HAMAP-Rule MF_01259 Magnesium HAMAP-Rule MF_01259 Manganese HAMAP-Rule MF_01259 Metal-binding HAMAP-Rule MF_01259 Nucleotide-binding Potassium HAMAP-Rule MF_01259
Molecular function	Ligase HAMAP-Rule MF_01259 EMBL ABM12555.1
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	F420-0 metabolic process Inferred from electronic annotation. Source: HAMAP coenzyme biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation-reduction process Inferred from electronic annotation. Source: GOC
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW coenzyme F420-0 gamma-glutamyl ligase activity Inferred from electronic annotation. Source: InterPro coenzyme F420-0:L-glutamate ligase activity Inferred from electronic annotation. Source: HAMAP coenzyme F420-1:gamma-L-glutamate ligase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

18 – 21

GTP By similarity HAMAP-Rule MF_01259

Region

1 – 242

242

F420-0:gamma-glutamyl ligase By similarity HAMAP-Rule MF_01259

Region

243 – 446

204

Unknown By similarity HAMAP-Rule MF_01259

Sites

Metal binding

107

Divalent metal cation 1 By similarity HAMAP-Rule MF_01259

Metal binding

148

Divalent metal cation 1 By similarity HAMAP-Rule MF_01259

Metal binding

149

Divalent metal cation 2 By similarity HAMAP-Rule MF_01259

Binding site

GTP By similarity HAMAP-Rule MF_01259

Binding site

GTP By similarity HAMAP-Rule MF_01259

Binding site

110

GTP By similarity HAMAP-Rule MF_01259

Sequences

Sequence

Length

Mass (Da)

Tools

A1T5V5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 923BF878CDF43F2F
Show »

FASTA

446

47,419

        10         20         30         40         50         60 
MTDHGTSARV ELLPVPGLPE FRPGDNLSAA IAEAAPWLQD DDVLVVTSKV LSKTEGRMVA 

        70         80         90        100        110        120 
APADPEERDA LRRKLIDSEA VRVLARKGRT LITENALGLV QAAAGVDGSN VESNELALLP 

       130        140        150        160        170        180 
VDPDGSAAAL VAALRERLGV RIGVVVTDTM GRAWRTGQTD VAIGAAGLTV LHAYAGERDQ 

       190        200        210        220        230        240 
HGNELIVTEI AVADEIAAAA DLVKGKLTAV PVAVVRGLSL RDDGSSARNL VRAGEEDLFW 

       250        260        270        280        290        300 
LGTEEALALG RSQAQLLRRS VRTFNSEPVP GDVIEAAVGE ALTAPAPHHT RPVRFVWVQD 

       310        320        330        340        350        360 
ASVRVGLLDK MKDRWRADLL GDGRDPESVE RRVNRGQILY DAPELVIPFM VPDGAHSYPD 

       370        380        390        400        410        420 
ARRTAAEHTM FTVAAGAAVQ GLLVALAARS VGSCWIGSTI FAPDLVRAEL GVPDDWEPLG 

       430        440 
AIAIGYPEAP LAPRHPVPTD DLLVRR

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References

[1]

"Complete sequence of Mycobacterium vanbaalenii PYR-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.J., Miller C., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 7251 / PYR-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000511 Genomic DNA. Translation: ABM12555.1.
RefSeq	YP_952561.1. NC_008726.1.
3D structure databases
ProteinModelPortal	A1T5V5.
ModBase	Search...
Protein-protein interaction databases
STRING	350058.Mvan_1732.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM12555; ABM12555; Mvan_1732.
GeneID	4647254.
KEGG	mva:Mvan_1732.
PATRIC	18181693. VBIMycVan31953_1776.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1478.
HOGENOM	HOG000223628.
KO	K12234.
OMA	PAPHHTT.
ProtClustDB	PRK13294.
Enzyme and pathway databases
BioCyc	MVAN350058:GIWR-1741-MONOMER.
UniPathway	UPA00071.
Family and domain databases
Gene3D	3.40.109.10. 1 hit.
HAMAP	MF_01259. F420_ligase_CofE_2.
InterPro	IPR002847. F420-0_gamma-glut_ligase-rel. IPR008225. F420-0_gamma-glutamyl_ligase. IPR019943. F420_FbiB_C. IPR023661. F420_ligase_CofE_2_bact. IPR000415. Nitroreductase-like. [Graphical view]
Pfam	PF01996. F420_ligase. 1 hit. PF00881. Nitroreductase. 1 hit. [Graphical view]
SUPFAM	SSF55469. Nitroreductase. 1 hit.
TIGRFAMs	TIGR01916. F420_cofE. 1 hit. TIGR03553. F420_FbiB_CTERM. 1 hit.
ProtoNet	Search...

Entry information

Entry name

A1T5V5_MYCVP

Accession

Primary (citable) accession number: A1T5V5

Entry history

Integrated into UniProtKB/TrEMBL:	February 6, 2007
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information