A2Z928 (HEM1_ORYSI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

ORF Names:

OsI_033071

Organism

Oryza sativa subsp. indica (Rice)

Taxonomic identifier

39946 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza › Oryza sativa

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 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.
Sequence caution	The sequence BAA25003.1 differs from that shown. Reason: Frameshift at positions 22 and 31. The sequence EAY79112.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway response to light stimulus Inferred from electronic annotation. Source: EnsemblPlants/Gramene response to oxidative stress Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Transit peptide	1 – 48	48	Chloroplast Potential
	Chain	49 – 537	489	Glutamyl-tRNA reductase, chloroplastic		PRO_0000295656
Regions
	Nucleotide binding	276 – 281	6	NADP By similarity
	Region	134 – 137	4	Substrate binding By similarity
	Region	199 – 201	3	Substrate binding By similarity
Sites
	Active site	135	1	Nucleophile By similarity
	Binding site	194	1	Substrate By similarity
	Binding site	205	1	Substrate By similarity
	Site	184	1	Important for activity By similarity
Experimental info
	Sequence conflict	151	1	I → L in BAA25003. Ref.1
	Sequence conflict	201	1	Q → E in BAA25003. Ref.1
	Sequence conflict	463	1	S → A in BAA25003. Ref.1
	Sequence conflict	468	1	M → T in BAA25003. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A2Z928 [UniParc]. Last modified July 24, 2007. Version 2. Checksum: 51414A99FFF50A9A	FASTA	537	58,435
	10 20 30 40 50 60 MMASTTSATA AGGAFAAAKT RAGSSAAGGG ACARVAAGGR RRSGVVVRCD AGVEAQAQAQ 70 80 90 100 110 120 AVAKAASVAA LEQFKISADR YMKERSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL 130 140 150 160 170 180 TSLNHIEEAA VLSTCNRMEI YVVALSWNRG IREVVDWMSK KSGIPASELR EHLFMLRDSD 190 200 210 220 230 240 ATRHLFEVSA GLDSLVLGEG QILAQVKQVV RSGQNSGGLG KNIDRMFKDA ITAGKRVRCE 250 260 270 280 290 300 TNISSGAVSV SSAAVELALM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN 310 320 330 340 350 360 RSVERVDAIR EEMKDIEIVY RPLTEMYEAA AEADVVFTST ASETPLFTKE HAEALPAISD 370 380 390 400 410 420 AMGGVRLFVD ISVPRNVSAC VSEVGHARVY NVDDLKEVVE ANKEDRLRKA MEAQTIITQE 430 440 450 460 470 480 LKRFEAWRDS LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDSLTKKMRR SIEELSTGIV 490 500 510 520 530 NKLLHGPLQH LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAIIEQKIKA KVEKSQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a cDNA clone encoding glutamyl-tRNA reductase from rice." Nakayashiki T., Inokuchi H. Plant Gene Register PGR98-080 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. IR36.
[2]	"The genomes of Oryza sativa: a history of duplications." Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H. PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. 93-11.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011416 mRNA. Translation: BAA25003.1. Frameshift. CM000135 Genomic DNA. Translation: EAY79112.1. Different initiation.
3D structure databases
ProteinModelPortal	A2Z928.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
KEGG	dosa:Os10t0502400-01.
Organism-specific databases
Gramene	A2Z928.
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109651.
Enzyme and pathway databases
UniPathway	UPA00251; UER00316.
Gene expression databases
ArrayExpress	A2Z928.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
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]
Pfam	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
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_ORYSI

Accession

Primary (citable) accession number: A2Z928
Secondary accession number(s): O48674 , Q0IWL0, Q337F6, Q8LNE9, Q9FW00

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 24, 2007
Last sequence update:	July 24, 2007
Last modified:	April 3, 2013
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program