Reviewed, UniProtKB/Swiss-Prot P42804 (HEM11_ARATH)

Names and origin

Protein names

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

Gene names

Name:	HEMA1
Synonyms:	HEMA
Ordered Locus Names:	At1g58290
ORF Names:	F19C14.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	543 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.
Tissue specificity	Present in all tissues tested. Slightly more abundant in leaves.
Induction	By light.
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
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
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-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: InterPro 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
	Transit peptide	1 – ?		Chloroplast Potential
	Chain	? – 543		Glutamyl-tRNA reductase 1, chloroplastic		PRO_0000013307
Regions
	Nucleotide binding	285 – 290	6	NADP By similarity
	Region	143 – 146	4	Substrate binding By similarity
	Region	208 – 210	3	Substrate binding By similarity
	Compositional bias	23 – 33	11	Poly-Ser
	Compositional bias	305 – 308	4	Poly-Val
Sites
	Active site	144	1	Nucleophile By similarity
	Binding site	203	1	Substrate By similarity
	Binding site	214	1	Substrate By similarity
	Site	193	1	Important for activity By similarity
Experimental info
	Sequence conflict	62	1	E → V in AAA19118. Ref.1
	Sequence conflict	169	1	K → N in AAA19118. Ref.1
	Sequence conflict	291	1	K → L in AAA19118. Ref.1
	Sequence conflict	542	1	Q → H in AAA19118. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P42804-1 [UniParc]. Last modified April 3, 2002. Version 2. Checksum: 04A095FEC96CC014	FASTA	543	59,515
	10 20 30 40 50 60 MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR TRRGLIQKAR 70 80 90 100 110 120 CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI GLSIHTAPVE MREKLAIPEA 130 140 150 160 170 180 EWPRAIAELC GLNHIEEAAV LSTCNRMEIY VLALSQHRGV KEVTEWMSKT SGIPVSEICQ 190 200 210 220 230 240 HRFLLYNKDA TQHIFEVSAG LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI 250 260 270 280 290 300 TVGKRVRTET NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK 310 320 330 340 350 360 GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA SETPLFLKEH 370 380 390 400 410 420 VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN VDDLKEVVAA NKEDRMRKAM 430 440 450 460 470 480 EAQTIITEES TQFEAWRDSL ETVPTIKKLR AYAERIRVAE LEKCMSKMGD DINKKTTRAV 490 500 510 520 530 540 DDLSRGIVNR FLHGPMQHLR CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ QQK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis." Ilag L.L., Kumar A.M., Soell D. Plant Cell 6:265-275(1994) [PubMed: 7908550] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia. Tissue: Leaf.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U03774 Genomic DNA. Translation: AAA19118.1. AC008051 Genomic DNA. Translation: AAF82258.1. AY072223 mRNA. Translation: AAL60044.1. AY096600 mRNA. Translation: AAM20250.1.
PIR	E96616.
RefSeq	NP_176125.1.
UniGene	At.241
3D structure databases
HSSP	HSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBase	Search...
Genome annotation databases
GeneID	842198.
GenomeReviews	Gene locus AT1G58290 in contig CT485782_GR.
KEGG	ath:AT1G58290.
NMPDR	fig|3702.1.peg.5290.
Organism-specific databases
TAIR	At1g58290.
Enzyme and pathway databases
BioCyc	MetaCyc:AT1G58290-MON.
Gene expression databases
ArrayExpress	P42804.
GermOnline	AT1G58290. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd. IPR006151. Shikm_DHase/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]
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM11_ARATH

Accession

Primary (citable) accession number: P42804
Secondary accession number(s): Q9LQB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	April 3, 2002
Last modified:	November 25, 2008
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)