Reviewed, UniProtKB/Swiss-Prot A6VND5 (HEM1_ACTSZ)

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:	Asuc_1116

Organism

Actinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]

Taxonomic identifier

339671 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	435 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 – 435	435	Glutamyl-tRNA reductase		PRO_1000071245
Regions
	Nucleotide binding	204 – 209	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	119 – 121	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	114	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity
	Site	104	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6VND5-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: F6A876382802D60B	FASTA	435	49,073
	10 20 30 40 50 60 MTILVLGINH KTATVALREK VAFSEEKRLS ALNQIEQLKL AQSTVILSTC NRTEVYLHNK 70 80 90 100 110 120 FIQPEQNSAW IDECVAWFAA IHQIQLTDLQ DCLYFYQNQQ AVTHLMRVAC GLDSLILGEP 130 140 150 160 170 180 QILGQVKQAY QLAEEYYQRA HGLGKSAVIS SELSRLFQKT FSTAKRVRTE TNIGESAVSV 190 200 210 220 230 240 AYAACSLGRQ IFESLQELTI LLVGAGETIE LAARHLLRHG VKKLMIANRT RARAEALVAK 250 260 270 280 290 300 LESPFIEILS LSELQDGLNQ ADIVISSTGS PTTLISYEMM KQAQIQRRYR PVLIVDIAVP 310 320 330 340 350 360 RDVEESIVKL DSVYHYTVDD LQNIINHNLS EREKASEQAE EIIAEECAAF FEWLKVRQAS 370 380 390 400 410 420 NLIRTYRESA DEIRQELLEK AQFSLSQGES ADKILDEFST KLMNKLLHSP TLVMQTMVKQ 430 GDSRGLQNFL SVIKK

References

[1]

"Complete sequence of Actinobacillus succinogenes 130Z." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000746 Genomic DNA. Translation: ABR74482.1.
RefSeq	YP_001344417.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5348066.
GenomeReviews	Gene locus Asuc_1116 in contig CP000746_GR.
KEGG	asu:Asuc_1116.
Organism-specific databases
CMR	Search...
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_ACTSZ

Accession

Primary (citable) accession number: A6VND5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	August 21, 2007
Last modified:	November 25, 2008
This is version 14 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)