Reviewed, UniProtKB/Swiss-Prot A1R8A6 (HEM1_ARTAT)

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:	AAur_2756

Organism

Arthrobacter aurescens (strain TC1) [Complete proteome] [HAMAP]

Taxonomic identifier

290340 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
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. HAMAP MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087
Subunit structure	Homodimer By similarity. HAMAP MF_00087
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. HAMAP MF_00087
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. HAMAP MF_00087
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 or NADPH 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 – 440	440	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335009
Regions
	Nucleotide binding	192 – 197	6	NADP By similarity
	Region	47 – 50	4	Substrate binding By similarity
	Region	115 – 117	3	Substrate binding By similarity
Sites
	Active site	48	1	Nucleophile By similarity
	Binding site	110	1	Substrate By similarity
	Binding site	121	1	Substrate By similarity
	Site	100	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1R8A6-1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: FC01F5CD3ADA7D8C	FASTA	440	45,893
	10 20 30 40 50 60 MVLFSLVATH ADIDLETVAQ LSNGSSELAS AALTDSSVVS GAVVLATCNR YEVYGETANG 70 80 90 100 110 120 ADLEAARSAL VSQISELSGL NEQLVSRSFA THTGPDVTRH LFAVSAGLDS AVVGEREIAG 130 140 150 160 170 180 QVRRALITAQ QEGTASSGLV RLFQAASKTA KDVGAQTALG SRGLSIVSVA LDLATDLAEN 190 200 210 220 230 240 DDWTTKKVVV FGTGAYAGAT MSLLRERGCT DISVYSSSGR AEGFVATRGG TALDADTLPA 250 260 270 280 290 300 AVAAADVMIG CSGSDNRVEA ADLARVRANS GKPLIAIDLA LTHDFDPAVG ELDGVELLTL 310 320 330 340 350 360 ESVRLAAPQE QAESLSQASA IVNGAATSFE SEREARSVDT AIVALRRHTM NVLDAEMEKV 370 380 390 400 410 420 RARHGCTAAA EEVEFALRRM VKQLLHIPTV RARELAANGQ QDDYVAALEA LYGIQVEQPQ 430 440 AAAPASECPV DHEQLRSESA

References

[1]

"Secrets of soil survival revealed by the genome sequence of Arthrobacter aurescens TC1." Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B., Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J. PLoS Genet. 2:2094-2106(2006) [PubMed: 17194220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000474 Genomic DNA. Translation: ABM08676.1. Different initiation.
RefSeq	YP_948468.1.
3D structure databases
SMR	A1R8A6. Positions 3-396.
ModBase	Search...
Protein-protein interaction databases
STRING	A1R8A6.
Genome annotation databases
GeneID	4638618.
GenomeReviews	Gene locus AAur_2756 in contig CP000474_GR.
KEGG	aau:AAur_2756.
TIGR	AAur_2756.
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HBG732626.
Family and domain databases
HAMAP	MF_00087. Glu-tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/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_ARTAT

Accession

Primary (citable) accession number: A1R8A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	February 9, 2010
This is version 34 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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