Reviewed, UniProtKB/Swiss-Prot A0KMZ9 (HEM1_AERHH)

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:	AHA_3150

Organism

Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]

Taxonomic identifier

380703 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	419 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 – 419	419	Glutamyl-tRNA reductase HAMAP MF_00087		PRO_0000335004
Regions
	Nucleotide binding	187 – 192	6	NADP By similarity
	Region	49 – 52	4	Substrate binding By similarity
	Region	112 – 114	3	Substrate binding By similarity
Sites
	Active site	50	1	Nucleophile By similarity
	Binding site	107	1	Substrate By similarity
	Binding site	118	1	Substrate By similarity
	Site	97	1	Important for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0KMZ9-1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: BA5E894610F3841E	FASTA	419	46,547
	10 20 30 40 50 60 MSLLALGINH NTASVALRER VAFGPDCIDR ALRELVAQPG VSEAVIVSTC NRTELYCSLA 70 80 90 100 110 120 QGQGEQVLQW LQRFHGLDAA EVVSAIYQHQ DEEAVRHLMR VACGLDSLVL GEPQILGQIK 130 140 150 160 170 180 QSYAHAQQSE AVKGSLERLF QKSFSVAKRV RTDTEIGASA VSVAFAAVSL GRRIFSDLSQ 190 200 210 220 230 240 TKVLLVGAGE TIELVARHLR EQNVTQMMVA NRTLQRAQLL AEEFGAQVMT LEEIPDYLHE 250 260 270 280 290 300 ADIVISSTAS PLPIIGKGMV ERALKARRFK PMFLVDIAVP RDIEAEVDEL SDAYLYTVDD 310 320 330 340 350 360 LQGIIEQNLE TRKRAAAEAE LIVQEERDDF MGWYRSQHSV DLIRDYRHQS QQVADEELQR 370 380 390 400 410 ALLALQQGEN AEQALKALAH RLTNKLIHAP TQALRHAAAQ GDHHQLAQLR QMLGLSQES

References

[1]

"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades." Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F. J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000462 Genomic DNA. Translation: ABK39341.1. Different initiation.
RefSeq	YP_857650.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4489791.
GenomeReviews	Gene locus AHA_3150 in contig CP000462_GR.
KEGG	aha:AHA_3150.
TIGR	AHA_3150.
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_AERHH

Accession

Primary (citable) accession number: A0KMZ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	June 16, 2009
This is version 27 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)