Reviewed, UniProtKB/Swiss-Prot Q9Y9J2 (HEM1_AERPE)

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:	APE_2296

Organism

Aeropyrum pernix [Complete proteome] [HAMAP]

Taxonomic identifier

56636 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum

Protein attributes

Sequence length	416 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
Molecular function	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 – 416	416	Glutamyl-tRNA reductase		PRO_0000114097
Regions
	Nucleotide binding	178 – 183	6	NADP By similarity
	Region	46 – 49	4	Substrate binding By similarity
	Region	102 – 104	3	Substrate binding By similarity
Sites
	Active site	47	1	Nucleophile By similarity
	Binding site	97	1	Substrate By similarity
	Binding site	108	1	Substrate By similarity
	Site	87	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Y9J2-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 6E087B36EFC6853D	FASTA	416	45,245
	10 20 30 40 50 60 MIDRLAMIGV NVKTASREHV ARLEKEWEKH LDTIGYASRG TVIIATCNRF EVYLDSPSRL 70 80 90 100 110 120 VEDLASSIAS PGGEGLVRLQ GIDAARHLFR VASGLESQII GDHEVLGQVR RAWLKSREKG 130 140 150 160 170 180 FTTPLLDEVF HRALKTGARV RSESAISSGG VGYSSAAVSL AASLLGGGLD GARVGIVGAG 190 200 210 220 230 240 MAAVGIARAL CTRWRPRVVA VFNRTPERGW EVAGKCRGVE SLVLPLDELA KLINELDALF 250 260 270 280 290 300 VAIAGSTNIL ERGRVERGVS PRVIVDISNP PVTPKVAGRV FHMPEVEEEA KRMMEERLRW 310 320 330 340 350 360 IPAAEAIIEE ELEALLDALS RRRARESSRS VMRALSILAE REYERTLAGL RNGVDPREAV 370 380 390 400 410 ELALNSYTKK VGGALRRLLE EASDRGQLSL EDIEAILVSE FARIAENSGF KNGSTG

References

[1]

"Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. , Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H. DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000002 Genomic DNA. Translation: BAA81308.1.
PIR	D72456.
RefSeq	NP_148521.1.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBase	Search...
Genome annotation databases
GeneID	1445329.
GenomeReviews	Gene locus APE_2296 in contig BA000002_GR.
KEGG	ape:APE_2296.
NMPDR	fig|272557.1.peg.1629.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9Y9J2.
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]
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

HEM1_AERPE

Accession

Primary (citable) accession number: Q9Y9J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	November 4, 2008
This is version 56 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)