Reviewed, UniProtKB/Swiss-Prot Q96563 (HEM12_HORVU)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 2
      Short name=GluTR
    EC=1.2.1.70

Gene names

Name:

HEMA2

Organism

Hordeum vulgare (Barley)

Taxonomic identifier

4513 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	465 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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.
Subcellular location	Plastid › chloroplast.
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	Chlorophyll biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: EC 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 – 465	›465	Glutamyl-tRNA reductase 2		PRO_0000114114
Regions
	Nucleotide binding	204 – 209	6	NADP By similarity
	Region	62 – 65	4	Substrate binding By similarity
	Region	127 – 129	3	Substrate binding By similarity
	Compositional bias	224 – 227	4	Poly-Val
Sites
	Active site	63	1	Nucleophile By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	133	1	Substrate By similarity
	Site	112	1	Important for activity By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q96563-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: E42A50A3E749CE6D	FASTA	465	51,675
	10 20 30 40 50 60 QFKISADRYI KEKSSIAVIG LSVHTAPVDM REKLAVAEEL WPRAISELTS LNHIEEAAVL 70 80 90 100 110 120 STCNRMEIYV VALSWNRGIR EVVDWMSKKS GIPASELREH LFMLRDSGAT RHLFEVSAGL 130 140 150 160 170 180 DSLVLGEGQI LAQVKQVVRN GQNSGGLGKN IDRMFKDAIT AGKRARCETN ISAGAVSVSS 190 200 210 220 230 240 AAVELAMMKL PKSECLSARM LLIGAGKMGK LVVKHLIAKG CKKVVVVNRS VERVDAIREE 250 260 270 280 290 300 MKDIEIVYRP LTEMYEAAAD ADVVFTSTAS ESLLFTKEHA EALPPISLAM GGVRLFVDIS 310 320 330 340 350 360 VPRNVGACLS QVEHARVYNV DDLKEVVEAN KEDRVRKAME AQAIITQELK RFEAWRDSLE 370 380 390 400 410 420 TVPTIKKLRS YADRIRASEL DKCLQKIGED NLNKKTRRSI EELSTGIVNK LLHGPLQHLR 430 440 450 460 CDGSDSRTLD ETLDNMHALN RMFNLDTEKA VLEQKIKAKV EKTQS

References

[1]	"Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley." Bougri O., Grimm B. Plant J. 9:867-878(1996) [PubMed: 8696365] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Bonus.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X86102 mRNA. Translation: CAA60055.1.
PIR	T05734.
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBase	Search...
Organism-specific databases
Gramene	Q96563.
Enzyme and pathway databases
BRENDA	1.2.1.70. 283.
Family and domain databases
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

HEM12_HORVU

Accession

Primary (citable) accession number: Q96563

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)