Glutamyl-tRNA reductase - Mycobacterium bovis (strain BCG / Pasteur 1173P2)

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A1KFY5 (HEM1_MYCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 57. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase
Short name=GluTR
EC=1.2.1.70

Gene names

Name:	hemA
Ordered Locus Names:	BCG_0552

Organism

Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP]

Taxonomic identifier

410289 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP⁺ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_00087
Domain	Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP-Rule MF_00087
Miscellaneous	During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA By similarity. HAMAP-Rule MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 468

468

Glutamyl-tRNA reductase HAMAP-Rule MF_00087

PRO_1000004646

Regions

Nucleotide binding

189 – 194

NADP By similarity

Region

49 – 52

Substrate binding By similarity

Region

114 – 116

Substrate binding By similarity

Sites

Active site

Nucleophile By similarity

Binding site

109

Substrate By similarity

Binding site

120

Substrate By similarity

Site

Important for activity By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A1KFY5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: DDC257648FF6EAAB
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FASTA

468

49,361

        10         20         30         40         50         60 
MSVLLFGVSH RSAPVVVLEQ LSIDESDQVK IIDRVLASPL VTEAMVLSTC NRVEVYAVVD 

        70         80         90        100        110        120 
AFHGGLSVIG QVLAEHSGMS MGELTKYAYV RYSEAAVEHL FAVASGLDSA VIGEQQVLGQ 

       130        140        150        160        170        180 
VRRAYAVAES NRTVGRVLHE LAQRALSVGK RVHSETAIDA AGASVVSVAL GMAERKLGSL 

       190        200        210        220        230        240 
AGTTAVVIGA GAMGALSAVH LTRAGVGHIQ VLNRSLSRAQ RLARRIRESG VPAEALALDR 

       250        260        270        280        290        300 
LANVLADADV VVSCTGAVRP VVSLADVHHA LAAARRDEAT RPLVICDLGM PRDVDPAVAR 

       310        320        330        340        350        360 
LPCVWVVDVD SVQHEPSAHA AAADVEAARH IVAAEVASYL VGQRMAEVTP TVTALRQRAA 

       370        380        390        400        410        420 
EVVEAELLRL DNRLPGLQSV QREEVARTVR RVVDKLLHAP TVRIKQLASA PGGDSYAEAL 

       430        440        450        460 
RELFELDQTA VDAVATAGEL PVVPSGFDAE SRRGGGDMQS SPKRSPSN

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References

[1]

"Genome plasticity of BCG and impact on vaccine efficacy."
Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.
Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BCG / Pasteur 1173P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM408590 Genomic DNA. Translation: CAL70537.1.
RefSeq	YP_976650.1. NC_008769.1.
3D structure databases
ProteinModelPortal	A1KFY5.
SMR	A1KFY5. Positions 178-297.
ModBase	Search...
Protein-protein interaction databases
STRING	410289.BCG_0552.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL70537; CAL70537; BCG_0552.
GeneID	4696020.
KEGG	mbb:BCG_0552.
PATRIC	18011635. VBIMycBov80988_0597.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109649.
KO	K02492.
OMA	GPILNRL.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	MBOV410289:GJW7-558-MONOMER.
UniPathway	UPA00251; UER00316.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00087. Glu-tRNA_reductase.
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. Pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Pfam	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAM	SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit. SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_MYCBP

Accession

Primary (citable) accession number: A1KFY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 6, 2007
Last modified:	May 29, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

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

Relevant documents