Reviewed, UniProtKB/Swiss-Prot A1TTC3 (HEM1_ACIAC)

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:	Aave_3663

Organism

Acidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]

Taxonomic identifier

397945 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

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_0000335001
Regions
	Nucleotide binding	193 – 198	6	NADP By similarity
	Region	55 – 58	4	Substrate binding By similarity
	Region	118 – 120	3	Substrate binding By similarity
Sites
	Active site	56	1	Nucleophile By similarity
	Binding site	113	1	Substrate By similarity
	Binding site	124	1	Substrate By similarity
	Site	103	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1TTC3-1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: F1AF378B845BE924	FASTA	432	46,734
	10 20 30 40 50 60 MAVWALGINH TTAPLDLRGR FAFAIDQIAP TLQGLRQSLG GATRHPQVET AILSTCNRTE 70 80 90 100 110 120 IYCAGQQPAL DHTLDWLAHS GGVSPSLLRS HSYTLEESLV ARHAFRVASG LDSMVLGEAQ 130 140 150 160 170 180 ILGQMKDAVR AAETAGALGT TLNQLFQRSF AVAKEVRTST EIGAHSISMA AAAVRLAGQL 190 200 210 220 230 240 FEDLTEIRIL FVGAGEMIEL AATHFAAKNP KSLAIANRTL ERGEKLASRF GGEVMRLADL 250 260 270 280 290 300 PDRLHEFDAV VSCTASSLPI IGLGAVERAL KKRRHRPMFM VDLAVPRDIE PEVKALEDIY 310 320 330 340 350 360 LYTVDDLASV VQTAQASRQA AVAQAEAIID AGVQSFMHWM DQRSPVGGVV PLIQQIHAQA 370 380 390 400 410 420 DEWRALEIAR AKKLIARGED MDAVLEALSR GLTQKMLHGT LAELRAGDAD TRAQTAQTVS 430 RLFLRSQSRS GL

References

[1]

"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000512 Genomic DNA. Translation: ABM34211.1.
RefSeq	YP_971985.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	A1TTC3.
Genome annotation databases
GeneID	4665154.
GenomeReviews	Gene locus Aave_3663 in contig CP000512_GR.
KEGG	aav:Aave_3663.
NMPDR	fig|397945.5.peg.3129.
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_ACIAC

Accession

Primary (citable) accession number: A1TTC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 6, 2007
Last modified:	November 3, 2009
This is version 32 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)