Q8DI53 (HEM1_THEEB) Reviewed, UniProtKB/Swiss-Prot

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:	tll1738

Organism

Thermosynechococcus elongatus (strain BP-1)

Taxonomic identifier

197221 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Thermosynechococcus

Protein attributes

Sequence length	426 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 Porphyrin biosynthesis; chlorophyll biosynthesis. 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	Chlorophyll biosynthesis Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 426	426	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000114077
Regions
	Nucleotide binding	189 – 194	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity
	Site	99	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8DI53 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D84CE5A1D2AA777E	FASTA	426	47,597
	10 20 30 40 50 60 MNIAVIGLSH KTAPVDVREK LSVPEDVRER ALQHLCGYAH IQEATILSTC NRLEIYIVTS 70 80 90 100 110 120 DTEVGVREVH QFLSEWSHIP LPQLRPYLFI LLHQDAVMHL MRVASGLDSL VIGEGQILSQ 130 140 150 160 170 180 VKRCHQLGQQ YKSIGPILNR VFTGAIAAGK RVRTETSIGT GAVSISSAAV ELADLRLQNL 190 200 210 220 230 240 QNCRIAVVGA GKMSRLVVQH LIARGVKEIR IINRSLERAQ ELAQQFPEVR FELFTMTDLL 250 260 270 280 290 300 PIVAAMDLVF TSTAATEPLL DRDNLGAVLV GDRSLAIIDI SVPRNVHANV TELGTVQLFN 310 320 330 340 350 360 VDDLQAVVAQ NQEARRQLAQ EAEGILEEEL ETFLAWWHAL ETVPIIRSLR QKMEAIRTQE 370 380 390 400 410 420 LEKALSRLGS EFADKHQGVI EAMTRTIINK ILHDPTVQLQ SQRDLESRQR AMQTLQDLFN LEPIEA

References

[1]

"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1." Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. , Takeuchi C., Yamada M., Tabata S. DNA Res. 9:123-130(2002) [PubMed: 12240834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BP-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000039 Genomic DNA. Translation: BAC09290.1.
RefSeq	NP_682528.1. NC_004113.1.
3D structure databases
ProteinModelPortal	Q8DI53.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8DI53.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1011595.
GenomeReviews	Gene locus tll1738 in contig BA000039_GR.
KEGG	tel:tll1738.
NMPDR	fig|197221.1.peg.1737.
PATRIC	23928856. VBITheElo119873_1819.
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HBG732626.
OMA	IRENEIC.
ProtClustDB	PRK00045.
Enzyme and pathway databases
BioCyc	TELO197221:TLL1738-MONOMER.
Family and domain databases
HAMAP	MF_00087. Glu-tRNA_reductase. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_dimer. 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.
KO	K02492.
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.
SUPFAM	SSF69075. 4pyrrol_synth_GluRdtase_C. 1 hit. SSF69742. GlutR. 1 hit.
TIGRFAMs	TIGR01035. HemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_THEEB

Accession

Primary (citable) accession number: Q8DI53

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	March 1, 2003
Last modified:	January 25, 2012
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program