Reviewed, UniProtKB/Swiss-Prot A3M2X7 (HEM1_ACIBT)

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:	A1S_0837

Organism

Acinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]

Taxonomic identifier

400667 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	427 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 – 427	427	Glutamyl-tRNA reductase		PRO_0000335003
Regions
	Nucleotide binding	185 – 190	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	110 – 112	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	105	1	Substrate By similarity
	Binding site	116	1	Substrate By similarity
	Site	95	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3M2X7-1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: A42E068563D88393	FASTA	427	47,964
	10 20 30 40 50 60 MSFFALGVNH QTASVELREQ IAFNAERLSN LLAEQRHHES LKDLVVVSTC NRTEVYAMAE 70 80 90 100 110 120 DAESLLKWLA DANNIDVKQL IHHVYRYENA QAITHLMRVA SGLDSLMLGE PQILGQVKSA 130 140 150 160 170 180 LALSKEAQTV SPELNSVFEY AFYAAKRVRS ETAVGSHAVS MGYAVAQLAL QVFSKPEKLT 190 200 210 220 230 240 VMVVAAGEMN SLVAKHLAEM GVAKMIICNR SRERADQLAQ EIAHQVEVEI IDFSDLAENL 250 260 270 280 290 300 YRADVVSSCT GSLHQVIAYA DVKTALKKRR YQQMLMVDLA VPRDIDPKVE SLDGVYLYGV 310 320 330 340 350 360 DDLQSVIDEN LAQRRQAAVE AEVMVNQLAT QLITHQKVKE AGSTIHAYRQ HSEEISQREL 370 380 390 400 410 420 THALEALHHG GNPEQVLQQF AHRLTQKLIH PTSMLLREAA KAESPDYFEW LQQHLQDVFD HERKPKR

References

[1]

"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis." Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M. Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000521 Genomic DNA. Translation: ABO11271.1. Different initiation.
RefSeq	YP_001083873.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4917062.
GenomeReviews	Gene locus A1S_0837 in contig CP000521_GR.
KEGG	acb:A1S_0837.
NMPDR	fig|400667.4.peg.861.
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. 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]
TIGRFAMs	TIGR01035. hemA. 1 hit.
PROSITE	PS00747. GLUTR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEM1_ACIBT

Accession

Primary (citable) accession number: A3M2X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	November 25, 2008
This is version 23 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)