Q42843 (HEM11_HORVU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamyl-tRNA reductase 1, chloroplastic
Short name=GluTR
EC=1.2.1.70

Gene names

Name:

HEMA1

Organism

Hordeum vulgare (Barley)

Taxonomic identifier

4513 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › BEP clade › Pooideae › Triticeae › Hordeum

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Ref.3
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
Pathway	Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Subunit structure	Homodimer. Ref.3
Subcellular location	Plastid › chloroplast.
Miscellaneous	Was shown to bind heme, but the precise role of heme is unclear. 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 CAA60054.1 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
Technical term	3D-structure Direct protein sequencing
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
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 – 43

43

Chloroplast Ref.2

Chain

44 – 527

484

Glutamyl-tRNA reductase 1, chloroplastic

PRO_0000013311

Regions

Nucleotide binding

266 – 271

6

NADP By similarity

Region

124 – 127

4

Substrate binding By similarity

Region

189 – 191

3

Substrate binding By similarity

Compositional bias

286 – 289

4

Poly-Val

Sites

Active site

125

1

Nucleophile By similarity

Binding site

184

1

Substrate By similarity

Binding site

195

1

Substrate By similarity

Site

174

1

Important for activity By similarity

Secondary structure

1

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527

Helix Strand Turn

Details...

Beta strand

79 – 81

3

Beta strand

96 – 99

4

Helix

104 – 125

22

Beta strand

133 – 137

5

Turn

150 – 152

3

Helix

155 – 159

5

Helix

170 – 182

13

Helix

193 – 197

5

Helix

209 – 213

5

Beta strand

215 – 222

8

Helix

225 – 230

6

Helix

233 – 251

19

Beta strand

262 – 265

4

Helix

269 – 281

13

Beta strand

285 – 288

4

Helix

293 – 302

10

Helix

313 – 315

3

Turn

316 – 318

3

Helix

319 – 321

3

Beta strand

324 – 327

4

Beta strand

334 – 336

3

Helix

347 – 350

4

Beta strand

356 – 358

3

Beta strand

361 – 363

3

Beta strand

365 – 367

3

Helix

368 – 376

9

Beta strand

380 – 383

4

Helix

386 – 389

4

Beta strand

392 – 397

6

Helix

398 – 404

7

Beta strand

406 – 410

5

Helix

413 – 421

9

Helix

423 – 436

14

Helix

443 – 457

15

Sequences

	Sequence		Length	Mass (Da)
	Q42843 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: D329E56458BE1165	FASTA	527	57,653
	10 20 30 40 50 60 MAGATSATAA AGAFAAAKAR GPAAACPWLV AAGGRRRSGV VRCDAGGDAQ AASKAASITA 70 80 90 100 110 120 LEQFKISADR YMKEKSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL TSLNHIEEAA 130 140 150 160 170 180 VLSTCNRMEI YVVALSWNRG IREVVDWMSK KSGIPASELR EHLFMLRDSD ATRHLFEVSA 190 200 210 220 230 240 GLDSLVLGEG QILAQVKQVV RNGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISAGAVSV 250 260 270 280 290 300 SSAAVELAMM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN RSVERVDAIR 310 320 330 340 350 360 EEMKDIEIVY RPLTEMYEAA ADADVVFTST ASESLLFTKE HAEVLPPISL AMGGVRLFVD 370 380 390 400 410 420 ISVPRNVGAC LSEVEHARVY NVDDLKEVVE ANKEDRVRKA MEAQTIITQE LKRFEAWRDS 430 440 450 460 470 480 LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDNLNKKMRR SIEELSTGIV NKLLHGPLQH 490 500 510 520 LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAVLEQKIKA KVEKTQS

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Klages.
[2]	"Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis." Pontoppidan B., Kannangara C.G. Eur. J. Biochem. 225:529-537(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 44-65, CHARACTERIZATION.
[3]	"Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase." Vothknecht U.C., Kannangara C.G., von Wettstein D. Proc. Natl. Acad. Sci. U.S.A. 93:9287-9291(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, HEME BINDING, SUBUNIT.
[4]	"Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins." Brody S.S., Gough S.P., Kannangara C.G. Proteins 37:485-493(1999) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 76-460.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X92403 mRNA. Translation: CAA63140.1.
X86101 mRNA. Translation: CAA60054.1. Different initiation.

PIR

T05732.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B29	model	-	A	76-460	[»]
1B61	model	-	A	76-460	[»]

ProteinModelPortal

Q42843.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

Gramene

Q42843.

Enzyme and pathway databases

UniPathway

UPA00251; UER00316.

Gene expression databases

Genevestigator

Q42843.

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]

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

HEM11_HORVU

Accession

Primary (citable) accession number: Q42843
Secondary accession number(s): Q42844

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 29, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program