Reviewed, UniProtKB/Swiss-Prot O67314 (HEM1_AQUAE)

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:	aq_1279

Organism

Aquifex aeolicus [Complete proteome] [HAMAP]

Taxonomic identifier

63363 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	406 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 – 406	406	Glutamyl-tRNA reductase		PRO_0000113987
Regions
	Nucleotide binding	187 – 192	6	NADP By similarity
	Region	50 – 53	4	Substrate binding By similarity
	Region	112 – 114	3	Substrate binding By similarity
Sites
	Active site	51	1	Nucleophile By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	118	1	Substrate By similarity
	Site	97	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	O67314-1 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 77F3ECC488FC4394	FASTA	406	46,648
	10 20 30 40 50 60 MGEIFVAGVN FKVAPVEVRE KLACSLEETK KVLPILKRET PLEEVMLLST CNRVEVYAYN 70 80 90 100 110 120 FVENSEDLIN KLLEIKRLNP SFKRYFFVKR GEEAVYHIFK VASSLDSMVI GEPQIVAQFK 130 140 150 160 170 180 EAYRVAKEAG TVGKILNRVY EKALRASKRV RTETGISRSA VSVSYAAVEL AKKIFGDLKE 190 200 210 220 230 240 AKVLLIGAGE MGELAANYLR RFGAKLHITN RTYERALKLV KELSGNVLRF EELKEYLPLM 250 260 270 280 290 300 DIVIVSTGAK DYILKREDFE RSVRERHYEP QFVIDIAVPR NVDPEAGNVE GVFLYDIDDL 310 320 330 340 350 360 KQVVEENLKE RIKEAQRGEI ILWDEVKKFM NWYESLKAEP YILELKASVE GKEVSPYIKK 370 380 390 400 LVHRAIKEIK RNPEVADIIL RIFKEVEKNE PRRKELSNVY NGTHGA

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000657 Genomic DNA. Translation: AAC07274.1.
PIR	G70410.
RefSeq	NP_213878.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBase	Search...
Genome annotation databases
GeneID	1192752.
GenomeReviews	Gene locus aq_1279 in contig AE000657_GR.
KEGG	aae:aq_1279.
NMPDR	fig|224324.1.peg.893.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O67314.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_1279-MON.
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. 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	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_AQUAE

Accession

Primary (citable) accession number: O67314

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	November 25, 2008
This is version 63 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)