Reviewed, UniProtKB/Swiss-Prot A7Z7A7 (HEM1_BACA2)

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:	RBAM_025230

Organism

Bacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]

Taxonomic identifier

326423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	455 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 – 455	455	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335011
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)
	A7Z7A7-1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: A40E2CBA32BAAE6A	FASTA	455	50,798
	10 20 30 40 50 60 MHILVVGVDY KSAPIEIREK ISFQPDELAE AMLRLKGEKS VLENIIVSTC NRTEIYAVVD 70 80 90 100 110 120 QLHTGRYYIK TFLSEWFSLP KEELSPFLKF YESDAAIEHL FRVACGLDSM VIGETQILGQ 130 140 150 160 170 180 VRSSFKTAQA EKTIGTIFNE LFKQAVTVGK RTHAETDIGA NAVSVSYAAV ELAKKIFGSL 190 200 210 220 230 240 SNKHILILGA GKMGELAAEN LHGQGIGKVT VINRTFLKAK ALADRFSGEA RSLNQLEHAL 250 260 270 280 290 300 AEADILISST GASDFVVSKE MMERAGRQRK GRPLFMVDIA VPRDLDPALN DLEGVFLYDI 310 320 330 340 350 360 DDLEGIVEAN LQERRETAEK VELFIEAAIV EFKQWLNTLG VVPVISALRE KALSIQSDTM 370 380 390 400 410 420 QSIERKLPHL TVREKKLLSK HTKSIINQML RDPILKAKEL AAEADSEEKL KLFMQIFDIE 430 440 450 EEAGRQLDKS LDNRQTVHSF QKAEAKTGLR PLVSE

References

[1]

"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42." Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R. Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000560 Genomic DNA. Translation: ABS74883.1. Different initiation.
RefSeq	YP_001422114.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5460787.
GenomeReviews	Gene locus RBAM_025230 in contig CP000560_GR.
KEGG	bay:RBAM_025230.
Organism-specific databases
CMR	Search...
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_BACA2

Accession

Primary (citable) accession number: A7Z7A7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	June 16, 2009
This is version 17 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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