Reviewed, UniProtKB/Swiss-Prot A4WN38 (HEM12_PYRAR)

Names and origin

Protein names

Recommended name:
    Glutamyl-tRNA reductase 2
      Short name=GluTR 2
    EC=1.2.1.70

Gene names

Name:	hemA2
Ordered Locus Names:	Pars_2261

Organism

Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321) [Complete proteome] [HAMAP]

Taxonomic identifier

340102 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Pyrobaculum

Protein attributes

Sequence length	403 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087
Subunit structure	Homodimer By similarity.
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.
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	Porphyrin biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutamyl-tRNA reductase activity Inferred from electronic annotation. Source: HAMAP 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
	Chain	1 – 403	403	Glutamyl-tRNA reductase 2 HAMAP MF_00087		PRO_0000335097
Regions
	Nucleotide binding	177 – 182	6	NADP By similarity
	Region	47 – 50	4	Substrate binding By similarity
	Region	103 – 105	3	Substrate binding By similarity
Sites
	Active site	48	1	Nucleophile By similarity
	Binding site	98	1	Substrate By similarity
	Binding site	109	1	Substrate By similarity
	Site	88	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4WN38-1 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: 67ACEFEC46ADA556	FASTA	403	43,952
	10 20 30 40 50 60 MDLLSPLSAV ILTYREADAN ALGRIGEEMR RCIEVIGPKT PMFVLHTCHR VEAYLYGASE 70 80 90 100 110 120 EELSSLVERY KRHVESARIL RGIEAARHLF RVAAGLESML LGETDILGQL EEAYDRQVRA 130 140 150 160 170 180 GFTRGLLKTV VERAVRVGKK VRTETGISRG PAGLGSLSII YVSQFVDLKS AKVAVLGAGA 190 200 210 220 230 240 VGAGLAKELA ERGVAKLYIL NRTLEKATEV AKKTGAEARP LTREEVERCL LECDVVFSAV 250 260 270 280 290 300 HTLEYVIDMI PPGASVKVVV DLGVPQSVAP GLPIKVVRLS DLAELAQRYS ALRKEEAKKA 310 320 330 340 350 360 EAIVEEELEM LPKALAKRAV EEAVAEVMAR AVEIAEEEGR RAGCEVAQLA AKTTVKRLLL 370 380 390 400 PIVEELKKMA ENGRVEHALE VSQIFTRLVG APHGEPQNLK TVK

References

[1]

"Complete sequence of Pyrobaculum arsenaticum DSM 13514." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000660 Genomic DNA. Translation: ABP51805.1.
RefSeq	YP_001154457.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5055414.
GenomeReviews	Gene locus Pars_2261 in contig CP000660_GR.
KEGG	pas:Pars_2261.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A4WN38. VDLGVPQ.
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015895. 4pyrrol_synth_GluRdtase_N. IPR016040. NAD(P)-bd_dom. IPR018214. pyrrol_synth_GluRdtase_CS. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	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

HEM12_PYRAR

Accession

Primary (citable) accession number: A4WN38

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 29, 2007
Last modified:	June 16, 2009
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)