Reviewed, UniProtKB/Swiss-Prot Q5P7G6 (HEM1_AZOSE)

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:	AZOSEA06230
ORF Names:	ebA1179

Organism

Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]

Taxonomic identifier

76114 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length	418 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 – 418	418	Glutamyl-tRNA reductase		PRO_1000004594
Regions
	Nucleotide binding	185 – 190	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	110 – 112	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	105	1	Substrate By similarity
	Binding site	116	1	Substrate By similarity
	Site	95	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5P7G6-1 [UniParc]. Last modified January 4, 2005. Version 1. Checksum: 308581D58B76AC8C	FASTA	418	46,624
	10 20 30 40 50 60 MQLYALGLNH HTAPLTIREQ VAFQPERLDD ALHDLTHERT VREAAILSTC NRTELYFATE 70 80 90 100 110 120 QPQHAADWLA RFHHMPLSEV SPYLYTYPQR DAIRHVFRVA SGLDSMVLGE PQILGQVKDA 130 140 150 160 170 180 VRRAEEAGTM GTLLHKLFQN TFAVAKEVRS TTAIGANIVS MAAAALHLSE RIFERMSDQR 190 200 210 220 230 240 VLFIGAGEMI ELCAAYFAGA CPKRIAVANR TEARAQLVAH RFGAEVMRLD VVGEMLPHFD 250 260 270 280 290 300 VVVSCTASPL PIVGLGMVER AIKARRHRPI VMVDLAVPRD IEAEVGELDD VFLYTVDDLA 310 320 330 340 350 360 QIVDAGLESR QQAVLEAEEI IDSRVNGFLH WMQARDAVPT IRALRQHAET VRAVELERAT 370 380 390 400 410 RLLAKGEDPR KVLDALSHGL INKLMHSPTR YLNQSEGEQQ ADASRLVQQL FNLSNSPD

References

[1]	"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1." Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R. Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR555306 Genomic DNA. Translation: CAI06745.1.
RefSeq	YP_157646.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3179696.
GenomeReviews	Gene locus AZOSEA06230 in contig CR555306_GR.
KEGG	eba:ebA1179.
NMPDR	fig|76114.4.peg.1742.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5P7G6.
Enzyme and pathway databases
BioCyc	ASP76114:EBA1179-MON.
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_AZOSE

Accession

Primary (citable) accession number: Q5P7G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 4, 2005
Last modified:	November 4, 2008
This is version 32 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)