Reviewed, UniProtKB/Swiss-Prot Q13TU3 (HEM1_BURXL)

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:	Bxeno_A3958
ORF Names:	Bxe_A0437

Organism

Burkholderia xenovorans (strain LB400) [Complete proteome] [HAMAP]

Taxonomic identifier

266265 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length	428 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.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
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 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 – 428	428	Glutamyl-tRNA reductase		PRO_1000004602
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)
	Q13TU3-1 [UniParc]. Last modified August 22, 2006. Version 1. Checksum: 3C512238DA1D253B	FASTA	428	47,044
	10 20 30 40 50 60 MQLLTIGINH HTAPVALRER VAFPLEQIKP ALDTFKSIWL GPSARTAPEA AILSTCNRTE 70 80 90 100 110 120 LYCATDDQAA REAAIQWLSR YHNLPIGELA PHVYALPQSE AVRHAFRVAS GLDSMVLGET 130 140 150 160 170 180 QIVGQMKDAV RTASEAGALG TYLNQLFQRT FAVAKEVRST TEIGAQSVSM AAAAVRLAQR 190 200 210 220 230 240 IFDKVANQRV LFIGAGEMIE LCATHFAAQQ PKELVVANRT AERGTRLAER FNGRAIPLSE 250 260 270 280 290 300 LPSRMHEFDI IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGQLEDV 310 320 330 340 350 360 FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDARSIVPVI RHMHTQADVL 370 380 390 400 410 420 RRAEVERAQK MLARGDDPAA VLEALSQALT NKLIHGPTHA LNRASSENRD TLIELMSGFY KHSGSTER

References

[1]

"Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome shaped for versatility." Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., Parnell J.J. , Ramette A., Richardson P., Seeger M., Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M. Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006) [PubMed: 17030797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000270 Genomic DNA. Translation: ABE32496.1.
RefSeq	YP_560548.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4005980.
GenomeReviews	Gene locus Bxeno_A3958 in contig CP000270_GR.
KEGG	bxe:Bxe_A0437.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q13TU3.
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. IPR006151. Shikm_DHase/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_BURXL

Accession

Primary (citable) accession number: Q13TU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	August 22, 2006
Last modified:	November 25, 2008
This is version 24 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)