P42804 (HEM11_ARATH) 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
Synonyms:	HEMA
Ordered Locus Names:	At1g58290
ORF Names:	F19C14.9

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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 protein 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.
Subunit structure	Interacts (via C-terminus) with FLU. Ref.5
Subcellular location	Plastid › chloroplast Ref.1.
Tissue specificity	Present in all tissues tested. Slightly more abundant in leaves. Ref.1
Induction	By light. Ref.1
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 Reference proteome
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from mutant phenotype PubMed 10631248. Source: TAIR heme biosynthetic process Inferred from mutant phenotype PubMed 10631248. Source: TAIR protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	chloroplast Inferred from direct assay PubMed 15028209. Source: TAIR
Molecular_function	NADP binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Traceable author statement PubMed 10631248. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 64	64	Chloroplast Potential
	Chain	65 – 543	479	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 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1), the target of metabolic feedback inhibition of tetrapyrrole biosynthesis, in dark- and light-grown Arabidopsis plants." Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K. Plant J. 40:957-967(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FLU. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U03774 Genomic DNA. Translation: AAA19118.1. AC008051 Genomic DNA. Translation: AAF82258.1. CP002684 Genomic DNA. Translation: AEE33532.1. AY072223 mRNA. Translation: AAL60044.1. AY096600 mRNA. Translation: AAM20250.1.
IPI	IPI00535419.
PIR	E96616.
RefSeq	NP_176125.1. NM_104609.3.
UniGene	At.241.
3D structure databases
ProteinModelPortal	P42804.
SMR	P42804. Positions 97-468.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42804. 4 interactions.
Proteomic databases
PaxDb	P42804.
PRIDE	P42804.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G58290.1; AT1G58290.1; AT1G58290.
GeneID	842198.
KEGG	ath:AT1G58290.
Organism-specific databases
TAIR	At1g58290.
Phylogenomic databases
eggNOG	COG0373.
HOGENOM	HOG000109651.
InParanoid	P42804.
KO	K02492.
OMA	GPILNRL.
PhylomeDB	P42804.
ProtClustDB	PLN00203.
Enzyme and pathway databases
BioCyc	ARA:AT1G58290-MONOMER. MetaCyc:AT1G58290-MONOMER.
UniPathway	UPA00251; UER00316.
Gene expression databases
ArrayExpress	P42804.
Genevestigator	P42804.
GermOnline	AT1G58290. Arabidopsis thaliana.
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

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:	May 1, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program