Reviewed, UniProtKB/Swiss-Prot A3MZC2 (HEM1_ACTP2)

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:	APL_0404

Organism

Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]

Taxonomic identifier

416269 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	436 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 – 436	436	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_1000004588
Regions
	Nucleotide binding	203 – 208	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	123 – 125	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	118	1	Substrate By similarity
	Binding site	129	1	Substrate By similarity
	Site	108	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A3MZC2-1 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 91663CBAE40792C4	FASTA	436	49,467
	10 20 30 40 50 60 MTILALGINH KTASVNLRSK VAFDDQKRQL AFEQIQHRAL AESVVILSTC NRTELYFHNA 70 80 90 100 110 120 EITPREEHED NIAWREQCFE WFAEIHQLEH NELRECIYFK QNMESARHLM RVACGLDSLI 130 140 150 160 170 180 LGEPQILGQV KQAYQYSENF YQSQNSHIST KLSRLFQRTF STAKRVRSET EIGSSAVSVA 190 200 210 220 230 240 YAACGLARQI FDNFGKLRFL LVGAGETIEL VARYLIQHGA KNIMIANRTP QRAETLAERL 250 260 270 280 290 300 NTPMQILSLS ALQIGLNQAD IVISSTGSPD MLISKEMVEI AQKQRQFDPM LLIDIAVPRD 310 320 330 340 350 360 IDENAGELDA VYSYSVDDLQ HIIQRNMAQR EQAAEQAAQI VDEECKAFFE WLKQQQSSDL 370 380 390 400 410 420 IKRYRQDAEQ TRQELLAKAL VALTSGQDSE KVLNELSYKL TNSLLHVPTQ ALQAMAKSGN 430 SQGLQSFSKA LKLEEQ

References

[1]	"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000569 Genomic DNA. Translation: ABN73508.1.
RefSeq	YP_001053113.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4849853.
GenomeReviews	Gene locus APL_0404 in contig CP000569_GR.
KEGG	apl:APL_0404.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	A3MZC2. 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_ACTP2

Accession

Primary (citable) accession number: A3MZC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	June 16, 2009
This is version 22 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)