Reviewed, UniProtKB/Swiss-Prot Q63QF1 (HEM1_BURPS)

Names and origin

Protein names

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

Gene names

Name:	hemA
Ordered Locus Names:	BPSL3072

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	441 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 – 441	441	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000114001
Regions
	Nucleotide binding	203 – 208	6	NADP By similarity
	Region	64 – 67	4	Substrate binding By similarity
	Region	128 – 130	3	Substrate binding By similarity
Sites
	Active site	65	1	Nucleophile By similarity
	Binding site	123	1	Substrate By similarity
	Binding site	134	1	Substrate By similarity
	Site	113	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q63QF1-1 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 06D2A7C3C3F1D032	FASTA	441	48,258
	10 20 30 40 50 60 MGLNDSLLDM QLLTIGINHH TAPVALRERV AFPLEQIKPA LSTFKSVFLG HPAPNAPEAA 70 80 90 100 110 120 ILSTCNRTEL YCATNDRAAR DAAIRWMSDY HRIPADELAP HVYALPQSEA VRHAFRVASG 130 140 150 160 170 180 LDSMVLGETQ ILGQMKNAVR TASEAGSLGT YLNQLFQRTF AVAKEVRGTT EIGAQSVSMA 190 200 210 220 230 240 AAAVRLAQRI FEQVAQQRVL FIGAGEMIEL CATHFAAQGP RELVVANRTA ERGAKLAERF 250 260 270 280 290 300 GGRAMPLADL PARMHEFDII VSCTASTLPI IGLGAVERAV KARRHRPIFM VDLAVPRDIE 310 320 330 340 350 360 PEVGKLKDVF LYTVDDLGAI VREGNASRQA AVAQAEAIIE TRVQNFMQWL DARSIVPVIR 370 380 390 400 410 420 HMHTQADALR RAEVERARKM LARGDDPDAV LDALSQALTN KLIHGPTSAL NRANGADRDS 430 440 LIDLMRGFYQ HAPRSSDTSD R

References

[1]

"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571965 Genomic DNA. Translation: CAH37083.1.
RefSeq	YP_109667.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3094369.
GenomeReviews	Gene locus BPSL3072 in contig BX571965_GR.
KEGG	bps:BPSL3072.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q63QF1.
OMA	Q63QF1. GPILNRL.
Enzyme and pathway databases
BioCyc	BPSE272560:BPSL3072-MON.
BRENDA	1.2.1.70. 275934.
Family and domain databases
HAMAP	MF_00087. [Tree]
InterPro	IPR000343. 4pyrrol_synth_GluRdtase. IPR015896. 4pyrrol_synth_GluRdtase_C. 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	PF00745. GlutR_dimer. 1 hit. PF05201. GlutR_N. 1 hit. PF01488. Shikimate_DH. 1 hit. [Graphical view]
PIRSF	PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_BURPS

Accession

Primary (citable) accession number: Q63QF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	October 25, 2004
Last modified:	June 16, 2009
This is version 39 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)