Reviewed, UniProtKB/Swiss-Prot B1JUS5 (HEM1_BURCC)

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:	Bcenmc03_0483

Organism

Burkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]

Taxonomic identifier

406425 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	432 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 – 432	432	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_1000093116
Regions
	Nucleotide binding	194 – 199	6	NADP By similarity
	Region	55 – 58	4	Substrate binding By similarity
	Region	119 – 121	3	Substrate binding By similarity
Sites
	Active site	56	1	Nucleophile By similarity
	Binding site	114	1	Substrate By similarity
	Binding site	125	1	Substrate By similarity
	Site	104	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1JUS5-1 [UniParc]. Last modified April 29, 2008. Version 1. Checksum: F67F22ED445360EB	FASTA	432	47,491
	10 20 30 40 50 60 MQLLTIGINH HTAPVALRER VAFPLEQIKP ALVTFKNVFL GPQAPNTPEA AILSTCNRTE 70 80 90 100 110 120 LYCATDDRAA REGAVRWLSE YHRIPVDELA PHVYALPQSE AVRHAFRVAS GLDSMVLGET 130 140 150 160 170 180 QILGQMKDAV RTATEAGALG TYLNQLFQRT FAVAKEVRGT TEIGTQSVSM AAAAVRLAQR 190 200 210 220 230 240 IFEKVSDQRV LFIGAGEMIE LCATHFAAQG PRELVVANRT AERGQRLAER FNGRAMPLAD 250 260 270 280 290 300 LPTRMHEFDI IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGKLKDV 310 320 330 340 350 360 FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDTRSVVPVI RHMHTQADAL 370 380 390 400 410 420 RRAEVEKAQK LLARGDDPAA VLEALSQALT NKLIHGPTSA LNRVNGADRD SLIDLMRGFY 430 QHAPRSNDQS GH

References

[1]

"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3." Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., 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., Tiedje J., Richardson P. Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000958 Genomic DNA. Translation: ACA89661.1.
RefSeq	YP_001763783.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6122164.
GenomeReviews	Gene locus Bcenmc03_0483 in contig CP000958_GR.
KEGG	bcm:Bcenmc03_0483.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	GPILNRL.
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_BURCC

Accession

Primary (citable) accession number: B1JUS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 29, 2008
Last modified:	November 3, 2009
This is version 13 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)