Reviewed, UniProtKB/Swiss-Prot A2RYL1 (HEM1_BURM9)

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:	BMA10229_0971

Organism

Burkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]

Taxonomic identifier

412022 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	L-glutamate 1-semialdehyde + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Subunit structure	Homodimer By similarity.
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.
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.
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	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 434	434	Glutamyl-tRNA reductase		PRO_0000335013
Regions
	Nucleotide binding	196 – 201	6	NADP By similarity
	Region	57 – 60	4	Substrate binding By similarity
	Region	121 – 123	3	Substrate binding By similarity
Sites
	Active site	58	1	Nucleophile By similarity
	Binding site	116	1	Substrate By similarity
	Binding site	127	1	Substrate By similarity
	Site	106	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2RYL1-1 [UniParc]. Last modified March 6, 2007. Version 1. Checksum: D9DC915D8233453A	FASTA	434	47,546
	10 20 30 40 50 60 MDMQLLTIGI NHHTAPVALR ERVAFPLEQI KPALSTFKSV FLGHPAPNAP EAAILSTCNR 70 80 90 100 110 120 TELYCATNDR AARDAAIRWM SDYHRIPADE LAPHVYALPQ SEAVRHAFRV ASGLDSMVLG 130 140 150 160 170 180 ETQILGQMKN AVRTASEAGS LGTYLNQLFQ RTFAVAKEVR GTTEIGAQSV SMAAAAVRLA 190 200 210 220 230 240 QRIFEQVAQQ RVLFIGAGEM IELCATHFAA QGPRELVVAN RTAERGAKLA ERFGGRAMPL 250 260 270 280 290 300 ADLPARMHEF DIIVSCTAST LPIIGLGAVE RAVKARRHRP IFMVDLAVPR DIEPEVGKLK 310 320 330 340 350 360 DVFLYTVDDL GAIVREGNAS RQAAVAQAEA IIETRVQNFM QWLDARSIVP VIRHMHTQAD 370 380 390 400 410 420 ALRRAEVERA RKMLARGDDP DAVLDALSQA LTNKLIHGPT SALNRANGAD RDSLIDLMRG 430 FYQHAPRSSD TSDR

References

[1]	DeShazer D., Woods D.E., Nierman W.C. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000545 Genomic DNA. Translation: ABN00173.1.
RefSeq	YP_001024780.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4790207.
GenomeReviews	Gene locus BMA10229_0971 in contig CP000545_GR.
KEGG	bml:BMA10229_0971.
TIGR	BMA10229_0971.
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd. IPR006151. Shikm_DHase/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
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.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_BURM9

Accession

Primary (citable) accession number: A2RYL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	March 6, 2007
Last modified:	November 25, 2008
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)