P48077 (HEM1_CYAPA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

hemA

Encoded on

Plastid; Cyanelle

Organism

Cyanophora paradoxa

Taxonomic identifier

2762 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Glaucocystophyceae › Cyanophoraceae › Cyanophora

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087 Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP-Rule MF_00087
Subunit structure	Homodimer By similarity.
Subcellular location	Plastid › cyanelle HAMAP-Rule MF_00087.
Domain	Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization By similarity. HAMAP-Rule MF_00087
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. HAMAP-Rule MF_00087
Sequence similarities	Belongs to the glutamyl-tRNA reductase family.
Sequence caution	The sequence CAC35456.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Chlorophyll biosynthesis Porphyrin biosynthesis
Cellular component	Cyanelle Plastid
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cyanelle 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: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 432	432	Glutamyl-tRNA reductase HAMAP-Rule MF_00087		PRO_0000114096
Regions
	Nucleotide binding	189 – 194	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	114 – 116	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	120	1	Substrate By similarity
	Site	99	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P48077 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: F14378FC72FFD05B	FASTA	432	48,542
	10 20 30 40 50 60 MNIIVVGLSH KTAPVDFREK LSIPKVRIGE AIRELCNYPH IEEVAILSTC NRLEIYLLTS 70 80 90 100 110 120 DTYQGIREAT QFLADSSDLS LPELRQHLFI LLHQDAVMHL MRVTAGLDSL IIGEGQILSQ 130 140 150 160 170 180 VKQCYQLGQQ YQGIGPVLNN IFKQAISAGK RVRTETQIST GAVSISSAAV ELAQIKKQDL 190 200 210 220 230 240 RTANITILGA GKMSRLLVQH LLSKRVKDIN IVNRSVERAK LLVDQFKEAN INIYNLSELK 250 260 270 280 290 300 TILQNSDIVF TGTSSQEPII TPELINDCDN LPSELMLFDI AVPRNVDPNV SQFDNIKVFN 310 320 330 340 350 360 VDDLKVVVSQ NQQTRRKMAK AAEILLEEEL SAFNIWWGSL EAIPTINKLR EKAEIIRVKE 370 380 390 400 410 420 LEKAISRLGN EFVSDHQEIV ESLTRGIVNK ILHDPMVQLR AQQDIEIRGR ALKILQTLFN 430 LDTIKNGMSP TL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa." Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., Bryant D.A. Plant Mol. Biol. Rep. 13:327-332(1995) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTEX LB 555 / Pringsheim.
[2]	"The complete sequence of the cyanelle genome of Cyanophora paradoxa: the genetic complexity of a primitive plastid." Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A. (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W. (eds.); Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: UTEX LB 555 / Pringsheim.
[3]	"The cyanelle genome of Cyanophora paradoxa encodes ribosomal proteins not encoded by the chloroplasts genomes of higher plants." Bryant D.A., Stirewalt V.L. FEBS Lett. 259:273-280(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 407-432. Strain: UTEX LB 555 / Pringsheim.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U30821 Genomic DNA. Translation: AAA81194.1. X17063 Genomic DNA. Translation: CAC35456.1. Different initiation.
PIR	T06851.
RefSeq	NP_043163.1. NC_001675.1.
3D structure databases
ProteinModelPortal	P48077.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	801525.
Enzyme and pathway databases
UniPathway	UPA00251; UER00316. UPA00668.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_00087. Glu-tRNA_reductase.
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

HEM1_CYAPA

Accession

Primary (citable) accession number: P48077
Secondary accession number(s): Q9BA13

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)